Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Status of Application/Election/Restrictions
Applicant’s election without traverse of Group I (claims 1-24) and MEDI1814 (SEQ ID NOs: 9-10 for VH and VL) in the reply filed on September 25, 2025 is acknowledged.
Claim 25 is canceled. Claims 1-24 and 26-34 are pending in this application. Claims 26-34 are withdrawn without traverse (filed 09/25/2025) from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim.
Upon reconsideration, the species election between MEDI1814 and Abet0380 and the species election between SEQ ID NOs: 9 and 7 and between SEQ ID NOs: 10 and 8 are withdrawn because the subject matter can be found in the same prior art reference. The subject matter to the extent of Abet0380 and SEQ ID NOs: 7-8 is included and under examination in this office action. Election was made without traverse in the reply filed on September 25, 2025.
Claims 1-24 are under examination in this office action.
Specification
The attempt to incorporate subject matter into this application by reference to “the Abet0380-GL/MEDI1814 nucleic acid sequence deposited under NCIMB accession number 41890….” is ineffective because based on MPEP 608.01(p) Completeness, the recitation of nucleic acid sequence under NCIMB accession number to define genes/proteins/antibodies in the claims is inappropriate because the nucleic acid sequence as defined by accession no. is an essential material, which is required by the claimed method. Thus, the incorporation by reference as by recitation of NCIMB accession no. is not effective. The incorporation of essential material in the specification by reference to an unpublished U.S. application, foreign application or patent, or to a publication or accession number is improper. Applicant is required to amend the disclosure to include the material incorporated by reference, if the material is relied upon to overcome any objection, rejection, or other requirement imposed by the Office. The amendment must be accompanied by a statement executed by the applicant, or a practitioner representing the applicant, stating that the material being inserted is the material previously incorporated by reference and that the amendment contains no new matter. 37 CFR 1.57(f). Also See MPEP 608.01 (p). I. Incorporation by reference & 37CFR 1.57. Incorporation by reference:
“(c) “Essential material” may be incorporated by reference, but only by way of an incorporation by reference to a U.S. patent or U.S. patent application publication, which patent or patent application publication does not itself incorporate such essential material by reference. “Essential material” is material that is necessary to: (1) Provide a written description of the claimed invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and set forth the best mode contemplated by the inventor of carrying out the invention as required by the first paragraph of 35 U.S.C. 112; (2) Describe the claimed invention in terms that particularly point out and distinctly claim the invention as required by the second paragraph of 35 U.S.C. 112…”
The disclosure is objected to because of the following informalities: The use of the term “SIMOA-HD1” (p. 4; p. 38; p. 76, Table 3), which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. Appropriate correction is required.
Claim Objections
Claims 1, 6,13-15 and 17 are objected to because of the following informalities:
The recitation “a binding of a binding member” in claim 1 is objected to because it should be “a binding member”. The recitations “ELISA” “SIMOA-HD1”, “VH”, “HCDRs1-3” “VL”, “LCDRs1-3”, MEDI1814” “Abet0380” “Abet0380-GL”, “IgG1-TM” “IgG1-YTE” “IgG1-TM-YTE” recited in claims 6, 13-15 and 17 are not unique or common abbreviations in the art. Applicants are required to spell out “ELISA” “SIMOA-HD1”, “VH”, “HCDRs1-3” “VL”, “LCDRs1-3”, MEDI1814” “Abet0380” “Abet0380-GL”, “IgG1-TM” “IgG1-YTE” “IgG1-TM-YTE” at the first usage. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-24 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claims 1-24 are indefinite because:
i. Claim 1 or 2 recites the limitation "the level " in line 3 of the claim. There is insufficient antecedent basis for this limitation in the claim.
ii. Regarding claim 5 or 18, the phrase "preferably” “more preferably” “even more preferably” renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
iii. Claim 6 contains the trademark/trade name “SIMOA-HD1”. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112, second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name “SIMOA-HD1” is used to identify/describe a fully automated platform instrument for running immunoassays for detecting biomarkers in biological fluids (digital ELISA) and, accordingly, the identification/description is indefinite.
iv. Claim 13 recites the limitation “…., wherein the amino acid sequences of the Abet0380 HCDRs are….” in line 3 of the claim. There is insufficient antecedent basis for this limitation in the claim.
v. Regarding claim 15, the limitation “by the Abet0380-GL nucleic acid sequence deposited under accession number 41890” renders the claim indefinite because the accession number is recited in the claim without a reference to a precise amino acid sequence identified by a proper SEQ ID NO:. The claim and the specification depend on the description of “NCIMB accession number 41890” to define the nucleic acid sequence encompassed by the claim, but since the accession number can be updated, the specification fails to define the claimed sequence and therefore the claim includes any number of undefined variants. It is not known what the sequence was at the time of filing and it is also not known whether the sequence is updated or annotated by date and/or unique sequence accession numbers. It is unclear which sequence, the initial or the updated, should be used in the claimed method. Thus, the claim is indefinite.
vi. The rest of claims are indefinite as depending from an indefinite claim.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 15 is rejected under 35 U.S.C. 112, first paragraph, as containing subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention. The invention appears to employ a novel biological material, specifically Abet0830-GL under accession number 41890. Since the biological material is essential to the claimed invention, they must be obtainable by a repeatable method set forth in the specification or otherwise readily available to the public. If the biological material is not so obtainable or available, the requirements of 35 U.S.C. § 112 may be satisfied by a deposit of the biological materials. The specification does not disclose a repeatable process to obtain the biological material, and it is not apparent if the biological materials are readily available to the public.
It is noted that Applicant has deposited the biological material (p. 24 of the specification), but there is no indication in the specification as to public availability.
Based on p. 24 of the instant specification, the specification states that “a preferred Ab1-42 binding member of the invention is an antibody the antibody comprises a VH and a VL encoded by ‘the Abet0380-GL/MEDI1814 nucleic acid sequence deposited under NCIMB accession number 41890 (deposited with NCIMB, Ferguson Building, Craibstone Estate, Bucksburn, Aberdeen, AB219YA, Scotland, UK on 02 November 2011)’…”. However, no information regarding the recited accession number can be found on the NCIMB website. It is not known what the sequence was at the time of filing. It is also not known whether updates to the sequence are annotated by date and/or unique sequence accession numbers.
If the deposit is made under the Budapest Treaty, then an affidavit or declaration by Applicant, or a statement by an attorney of record over his or her signature and registration number, stating that the specific biological materials have been deposited under the Budapest Treaty and that the biological materials will be irrevocably and without restriction or condition released to the public upon the issuance of a patent, and that the deposit will be maintained in a public depository for a period of 30 years or 5 years after the last request or for the effective life of the patent, whichever is longer, would satisfy the deposit requirement made herein.
If the deposit has not been made under the Budapest Treaty, then in order to certify that the deposit meets the criteria set forth in 37 C.F.R. §§ 1.801-1.809, Applicant may provide assurance of compliance by an affidavit or declaration, or by a statement by an attorney of record over his or her signature and registration number, showing that:
(a) during the pendency of this application, access to the invention will be afforded to the Commissioner upon request;
(b) all restrictions upon availability to the public will be irrevocably removed upon granting of the patent;
(c) the deposit will be maintained in a public depository for a period of 30 years or 5 years after the last request or for the effective life of the patent, whichever is longer;
(d) a test of the viability of the biological material at the time of deposit will be made (see 37 C.F.R. § 1.807); and
(e) the deposit will be replaced if it should ever become inviable.
Applicant’s attention is directed to M.P.E.P. §2400 in general, and specifically to §2411.05, as well as to 37 C.F.R. § 1.809(d), wherein it is set forth that “the specification shall contain the accession number for the deposit, the date of the deposit, the name and address of the depository, and a description of the deposited material sufficient to specifically identify it and to permit examination.” The specification should be amended to include this information, however, Applicant is cautioned to avoid the entry of new matter into the specification by adding any other information. Finally, the address for the ATCC is:
American Type Culture Collection
10801 University Boulevard
Manassas, VA 20110-2209
Claim Rejections - 35 USC § 112
9. Claims 1-24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for decreasing CSF free Ab1-42 levels and CSF NfL levels in patients with mild to moderate AD after administering to the patients an anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody at a MAD IV 1800mg wherein the MEDI1814 antibody comprises a VH of SEQ ID NO:9 and a VL of SEQ ID NO:10 or wherein the Abet0380 antibody comprises a VH of SEQ ID NO:7 and a VL of SEQ ID NO:8, does not reasonably provide enablement for a method for treating all forms of AD or preventing axonal damages in patients with all forms of CNS neurodegenerative diseases using the claimed structurally and functionally undefined binding member as broadly claimed. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims. In addition, the specification does not enable the invention of claims 1-24 that is directed to a method of prevention and curing.
“There are many factors to be considered when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any necessary experimentation is ‘undue’. These factors include, but are not limited to: (A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)”. See MPEP § 2164.01.
Claims 1-24 are drawn to methods for treating Alzheimer’s disease (AD) and preventing neuronal axonal damage in a patient, comprising administering a therapeutically effective amount of a binding member that selectively binds human amyloid beta 1-42 peptide (Ab1-42) to a patient, wherein the binding member decreases the level of neurofilament light chain (NfL) in the patient compared with the level of NfL in the patient pre-treatment with the binding member.
The claims encompass methods of treating, preventing and curing all forms of AD using a structurally and functionally undefined binding member that selectively binds human Ab1-42 and decreases the level of NfL as compared with the level of NfL in the patient before the treatment in view of paragraph [0251] of instant specification (based on published application) or p. 48-49 of the specification filed 8/30/19.
The instant invention is based on findings that intravenous administration of an anti-Ab1-42 antibody MEDI1814/Abet0380-GL or Abet0380 antibody at a dose of 25, 100, 300, 900 and 1800mg to patients with mild to moderate AD resulted in reduced CSF free Ab1-42 by -90% change in the highest dose (300-1800mg IV) or by -72% (100mg IV), -11% (100mg SC) or -34% (25mg IV)(Example 3, Figure 1) and decreased CSF NfL by 50% for the MAD (multiple ascending dose) IV 1800mg or plasma NfL by 20% for the MAD IV 1800mg (Example 4, Figure 2-3) but there was no significant change in level of pTau181 in the CSF or plasma or tTau or Neurogranin (Ng) (Example 4, Figures 4-5).
Applicant extrapolates the above findings to the claimed methods of treating AD including preventing and curing all forms of AD using a structurally and functionally undefined binding member that selectively binds human Ab1-42 and decreases the level of NfL as compared with the level of NfL in the patient before the treatment.
First, Applicant is not enabled for a method treating including preventing a person from getting AD and curing AD. Based on the definition “treat/treating” in paragraph [0251] of the published Application, the limitation “treating AD” and “preventing neuronal axonal damage” encompasses preventing and curing all forms of AD or neurodegenerative diseases.
[0251] The term “treat” or “treating” as used herein encompasses prophylactic treatment (e.g. to prevent onset of neuronal axonal damage) as well as corrective treatment (treatment of a subject already suffering from neuronal axonal damage). Preferably, the term “treat” or “treating” as used herein means corrective treatment…...
However, neither the specification nor the prior art provides guidance as to how to prevent a person from having AD or neuronal axonal damage in all forms of neurodegenerative diseases caused by all possible mechanisms or cure AD or neuronal axonal damage in all forms of neurodegenerative diseases caused by all possible mechanisms. Currently, AD and neuronal axonal damage in all forms of CNS neurodegenerative diseases cannot be prevented or cured (see p.1; p. 3; p. 17; p.20 of the factsheet of Alzheimer’s disease from the Cleveland Clinic website site and p.14; p. 17-18 of the factsheet of CNS neurodegenerative diseases from the Cleveland Clinic website site).
Any individual has a potential to develop AD or any neurodegenerative disease caused by all possible mechanisms. Applicant fails to teach how to identify or predict when and which person would be susceptible to such a disease or developing the disease, and predict when the person would need administration of the claimed binding member binding to human Ab1-42 and decreasing the level of NfL to prevent the disease before the disease occurs. Neither the specification nor the prior art teaches that administration of the claimed binding member can prevent a person from getting AD or any CNS neurodegenerative disease caused by all possible mechanisms or cure AD or any CNS neurological disease caused by all possible mechanisms. The causes of AD or different forms of CNS neurodegenerative diseases are different. The cause of the diseases can be due to a genetic mutation, which is a natural process. For example, there are many factors involved in molecular mechanisms contributing to the formation of -amyloid deposits and neurofibrillary tangles in AD. They include genetic mutations affecting the processing of APP or other molecules involved in protein processing and targeting in view of Henstridge et al. (see p. 94, Henstridge et al., Nat. Rev. Neurosci. 2019; 20: 94-107), Tayebati (see p. 106, 1st col, 2nd paragraph, Tayebati, Mech. Ageing Dev. 2006. 127: 100-8) and Sarter (see p. 645, abstract, Sarter, Neurosci. and Biobehav. Rev. 2004. 28: 645-650). If the cause is due to genetic deficits or mutations, it is impossible to prevent a person from getting or developing AD or CNS neurodegenerative disease because the gene mutation or gene deficiency is a natural process result. The specification fails to provide sufficient guidance to enable one of skill in the art to practice the invention as it pertains to a method of prevention or curing. Further, Applicant also fails to provide specific guidance as to what specific amount of the claimed binding member can be used and thus would be effective to prevent or cure AD or any CNS neurodegenerative diseases caused by all possible mechanisms. Thus, a skilled artisan cannot contemplate a right amount to prevent the disease or to prevent a person from getting the disease or cure the disease.
Second, based on the specification and the prior art, Applicant is enabled for decreasing CSF free Ab1-42 levels and CSF NfL levels in patients with mild to moderate AD after administering to the patients an anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody at a MAD IV 1800mg wherein the MEDI1814 antibody comprises a VH of SEQ ID NO:9 and a VL of SEQ ID NO:10 or wherein the Abet0380 antibody comprises a VH of SEQ ID NO:7 and a VL of SEQ ID NO:8.
The claims are not limited to the antibody and the method set forth above but also encompass treatment of all forms of AD or all forms of CNS neurodegenerative diseases caused by all possible mechanisms and using structurally and functionally undefined binding members binding to human Ab1-42 and decreasing the level of NfL compared to pre-treatment.
However, the specification fails to provide sufficient guidance to enable one of skill in the art to practice the full scope of the claimed invention without undue experimentation because of the complexity and unpredictability of the diseases and lack of support and lack of a correlation between the mild to moderate AD and the pathogeneses or causes of other forms of AD or all forms of CNS neurodegenerative diseases caused by all possible mechanisms in vivo in view of Falkenburger et al. (see p.261, summary Falkenburger et al., J. Neural. Transm, 2006; 70:261-268), Tayebati (see p. 106, 1st col, 2nd paragraph, Tayebati, Mech. Ageing Dev. 2006. 127: 100-8) and Sarter (see p. 645, abstract, Sarter, Neurosci. and Biobehav. Rev. 2004. 28: 645-650). The specification also fails to provide sufficient guidance as to what structural and functional relationship between the claimed structurally and functionally undefined binding member and the Ab1-42 antibody MEDI1814 antibody in reducing the level of NfL in mild to moderate AD after treatment as compared to pre-treatment, indicating undue experimentation is required by a skilled artisan to perform while practicing the claimed invention.
Each type of animal models of AD or CNS neurodegenerative diseases only reflects part of pathogenesis of the disease as taught by Tayebati (see p. 106, 1st col, 2nd paragraph, Tayebati, Mech. Ageing Dev. 2006. 127: 100-8) and Sarter (see p. 645, abstract, Sarter, Neurosci. and Biobehav. Rev. 2004. 28: 645-650). Applicant obviously intended to treat all forms of AD and all forms of CNS neurodegenerative diseases including by using the claimed binding member. However, the specification fails to provide a well-established correlation among different forms of AD and different forms of CNS neurodegenerative diseases caused by different mechanisms. The specification fails to establish that different forms of AD and forms of CNS neurological diseases caused by different mechanisms can be treated by the same drugs or same conditions or have the same effects in response to the same drugs. Thus, it is unpredictable whether one treatment for one specific disorder can be applied to another disorder, indicating undue experimentation is required by a skilled artisan to perform while practicing the claimed invention.
While the skill level in the art is high, the level of predictability is low. For example, the molecular mechanisms underlying cognitive dysfunction or dementia of AD are unclear (see p. 94; Henstridge et al. Nat. Rev. Neurosci. 2019; 20: 94-107). The specification provides insufficient guidance to demonstrate that administration of the claimed binding member can treat cognitive dysfunction or dementia in AD because Abeta accumulation and/or hyperphosphorylated tau is not the only cause of cognitive dysfunction or dementia in AD. Several factors and genes are involved in pathogenesis of AD including ageing, inflammation and immune response, APP, presenilin1/2, ApoE and genes involved in the amyloid cascade, genes involved in the mitochondrial cascade as taught by Swerdlow (p. 348-344, Swerdlow, Clin. Interv. Ageing 2007; 2:347-359), Atwood et al. (p. abstract; Atwood et al., J. Alzheimer’s Disease; 2015; 47:33-47) and Henstridge et al. (p. 95-103; Henstridge et al., Nat. Rev. Neurosci. 2019; 20: 94-107).
It is also known that fully developed animal models for neurodegenerative diseases are still lacking especially for AD because the complexity of the disease and deficiency of characterized cognition (see p. 403, abstract. Anger. Neurotoxicology 1991. 12: 403-13). For example, the animal model of brain amyloidosis induced by acute or infusion of Ab as described in the instant case could only be used to screening for inhibiting the formation of Ab but not for evaluating the generation of Ab by the effects of b-and g-secretase, which is another molecular mechanism for the pathogenesis of AD (see p. 106, 1st col, 2nd paragraph, Tayebati. Mech. Ageing Dev. 2006. 127: 100-8). The art also recognizes that although the Morris water maze behavioral test is a popular choice used in studies determining effects of learning and memory, the test has been disappointing in the predictive validity of data from animal tests on learning and memory used to discover and characterize drugs for the treatment of cognitive impairment and dementia in clinical testing. The animal tasks generate a high rate of false positive (see p. 646, 2nd col. 2nd paragraph) and the validity of the test itself is also a part of the research process (see p. 645, abstract, Sarter. Neurosci. and Biobehav. Rev. 2004. 28: 645-650). Thus, in order to closely reflect the data obtained from animal models to the real situation of Alzheimer’s disease in humans, it has been proposed that a rodent model should include 1) tests currently used to identify in rodents deficits associated with AD; 2) tests to identify Alzheimer-related signs in patients; and 3) tests that relate to theoretical constructs of human and animal cognition, which should include at least spatial learning and memory (such as Morris Water Maze and Radial Arm Maze), delayed recall match-to-sample, serial response learning, and visual discrimination (such as vertical vs. horizontal stimuli).(see p. 403, abstract. Anger. Neurotoxicology 1991. 12: 403-13). Applicant is enabled for decreasing CSF free Ab1-42 levels and CSF NfL levels in patients with mild to moderate AD after administering to the patients an anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody at a MAD IV 1800mg, wherein the MEDI1814 antibody comprises a VH of SEQ ID NO:9 and a VL of SEQ ID NO:10 or wherein the Abet0380 antibody comprises a VH of SEQ ID NO:7 and a VL of SEQ ID NO:8.
However, the specification fails to provide sufficient guidance or evidence to demonstrate that all forms of AD or all forms of CNS neurodegenerative diseases caused by different mechanisms can be treated or prevented or cured by the claimed binding member because there is no well-established correlation between reduction of CSF free Ab1-42 levels and CSF NfL levels in patients with mild to moderate AD after treatment with an anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody at a MAD IV 1800mg and the pathogeneses or causes of different forms of AD caused by other mechanisms or CNS neurodegenerative diseases caused by other mechanisms. Since the pathogenesis of AD or other CNS neurodegenerative diseases is complex and the causes of dementia/cognitive dysfunction in AD have not been deciphered and are equally complex, it is unpredictable whether the reduction of CSF free Ab1-42 levels and CSF NfL levels in patients with mild to moderate AD after treatment with an anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody at a MAD IV 1800mg can be applied to other forms of AD caused by other mechanisms or other CNS neurodegenerative diseases caused by other mechanisms, or whether administration of the claimed binding member can treat all forms of AD or all forms of CNS neurodegenerative diseases, indicating that undue experimentation is required by a skilled artisan to perform while practicing the claimed invention.
Further, the specification fails to provide sufficient guidance as to what other binding members are and whether other binding members can be used in the claimed method because the specification fails to provide sufficient description as to what structures or sequences for the claimed genus of binding members or antibodies or their corresponding heavy chain, light chain, variable regions, or H/LCDRs1-3 are in order to generate binding members that can bind to human Ab1-42 and decrease CSF NfL levels in the AD patients compared to the NfL levels of the patients before treatment thereby treating AD or preventing axonal damage in all forms of CNS neurodegenerative diseases. The specification fails to teach the structural and functional relationship between the claimed binding members and the anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody, wherein the MEDI1814 antibody comprises a VH of SEQ ID NO:9 and a VL of SEQ ID NO:10 or wherein the Abet0380 antibody comprises a VH of SEQ ID NO:7 and a VL of SEQ ID NO:8. The specification fails to teach what other structures/amino acid sequences can or cannot not be included/changed in all binding members or variants of the anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody in order to preserve the activity of the anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody in reducing CSF free Ab1-42 levels and CSF NfL levels in patients with mild to moderate AD after treatment with the MEDI1814 or Abet0380 antibody at a MAD IV 1800mg as compared to pre-treatment, or even treating all forms of AD or all forms of CNS neurodegenerative diseases caused by all possible mechanisms, indicating undue experimentation is required by a skilled artisan to perform while practicing the claimed invention.
Therefore, in view of the breadth of the claims, the lack of guidance in the specification, the limited examples, the unpredictability of inventions, and the current status of the art, undue experimentation would be required by one of skill in the art to perform in order to practice the full scope of the claimed invention as it pertains to a method for treating AD or preventing axonal damage in a patients with all forms of CNS neurodegenerative disease by the claimed binding member.
Claim Rejections - 35 USC § 112
10. Claims 1-24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
To provide adequate written description and evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof.
Claims 1-24 encompass using a genus of structurally and functionally undefined binding member for treating AD and preventing neuronal axonal damage in all forms of CNS neurodegenerative diseases wherein the binding member decreases the level of neurofilament light chain (NfL) in the patient compared with the level of NfL pre-treatment with the binding member. Claims 11-12 and 16-19 encompass using a genus of anti-human Ab1-42 antibody, and claims 13-15 encompass using a genus of antibody comprising HCDRs1-3 and LCDRs1-3 of SEQ ID NOs: 1-6 respectively or a VH and a VL of SEQ ID NOs: 9-10 or SEQ ID NOs: 7-8 respectively or variants thereof with one or two amino acid mutations.
Applicant has not disclosed sufficient species for the broad genus of binding member. The specification only describes administration of an anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody at a MAD IV 1800mg to patients with mild to moderate AD to decrease CSF free Ab1-42 levels and CSF NfL levels in the patients compared to the NfL levels of the patients before treatment, wherein the MEDI1814 antibody comprises a VH of SEQ ID NO:9 and a VL of SEQ ID NO:10 or wherein the Abet0380 antibody comprises a VH of SEQ ID NO:7 and a VL of SEQ ID NO:8. However, the claims are not limited to the use of the anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody and patients with mild to moderate AD set forth above but also encompass using a genus of structurally and functionally undefined binding member for treating and preventing axonal damage in all forms of AD and all forms of CNS neurodegenerative diseases.
In making a determination of whether the application complies with the written description requirement of 35 U.S.C. 112, first paragraph, it is necessary to understand what Applicant is in possession of and what Applicant is claiming.
M.P.E.P. § 2163 instructs:
An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. . . .
An applicant may show possession of an invention by disclosure of drawings or structural chemical formulas that are sufficiently detailed to show that applicant was in possession of the claimed invention as a whole. . . .
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics.”
This standard has not been met in this case. From the specification, Applicant is in possession of using anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody to CSF free Ab1-42 levels and CSF NfL levels in the patients with mild to moderate AD as compared to pre-treatment with the MEDI1814 or Abet0380 antibody. However, Applicant is not in possession of using other structurally and functionally undefined binding members in treating all forms of AD or preventing axonal damage in all forms CNS neurodegenerative diseases because the specification fails to provide sufficient description as to what structures or sequences for the claimed genus of binding members or antibodies or their corresponding heavy chain, light chain, variable regions, or H/LCDRs1-3 are in order to generate binding members that can bind to human Ab1-42 and decrease CSF NfL levels in the AD patients compared to the NfL levels of the patients before treatment thereby treating AD or preventing axonal damage in all forms of CNS neurodegenerative diseases.
As an initial matter, Applicant has provided no structures or sequences sufficiently detailed to show that he/she was in possession of the claimed genus of binding member for treating AD or preventing axonal damage in all forms of patients as a whole. There was also no known or disclosed correlation between the required function (i.e. binding to human Ab1-42 and decreasing CSF NfL levels in the AD patients compared to the NfL levels of the patients prior to treatment) and any particular structure or sequence.
Applicant has not disclosed sufficient species for the broad genus of binding members. The specification only discloses anti-human Ab1-42 MEDI1814 antibody and Abet0380 antibody, wherein the MEDI1814 antibody comprises a VH of SEQ ID NO:9 and a VL of SEQ ID NO:10 and wherein the Abet0380 antibody comprises a VH of SEQ ID NO:7 and a VL of SEQ ID NO:8.
In light of Amgen, Inc. v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017), describing a “fully characterized antigen” for an antibody is no longer adequate on its own to demonstrate possession of the antibody. Based on MPEP§2161.01 and 2163, the USPTO guidance regarding written description requirement of 35 U.S.C.§C112 (a), specifically concerning the written description requirement for claims drawn to antibodies and Federal Circuit decisions, when an antibody is claimed, 35USC112(a) requires adequate written description of the antibody itself. See Amgen 872 F.3d at 1378-79.
The court of the Federal Circuit also stressed that the “newly characterized antigen" test could not stand because it contradicted the quid pro quo of the patent system whereby one must describe an invention in order to obtain a patent. See Amgen, 872 F.3d at 1378-79, quoting Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1345 (Fed. Cir.2010). In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional.
The specification’s general reference to binding members “binding to human Ab1-42 and decreasing CSF NfL levels in the AD patients compared to the NfL levels of the patients prior to treatment” in independent claims 1-2” does not clearly suggest any particular sequences that can be used in order to result in the claimed antibodies or the claimed features. As such, he cannot possibly have possessed the entire genus.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope.
The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. MacCallum et al. (J. Mol. Biol.,1996; 262: 732-745) teaches that although CDR3 of the heavy and light chain dominate, a number of residues outside the standard CDR definitions make antigen contacts (see p. 733, right col) and non-contacting residues within the CDRs coincide with residues as important in defining canonical backbone conformations (see page 735, left col.). Pascalis et al. (The Journal of Immunology, 2002; 169: 3076-3084) teaches that grafting of the CDRs into a human framework was performed by grafting CDR residues and maintaining framework residues that were deemed essential for preserving the structural integrity of the antigen binding site (see page 3079, right col.) and that although abbreviated CDR residues were used in the constructs, some residues in all 6 CDRs were used for the constructs (see page 3080, left col.). The fact that not just one CDR is essential for antigen binding or maintaining the conformation of the antigen binding site because although CDR H3 is at the center of most if not all antigen interactions, clearly other CDRs play an important role in the recognition process (page 199, left col.) and this is demonstrated in this work by using all CDRs except L2 and additionally using a framework residue located just before the H3 (see page 202, left col.; Casset et al., BBRC, 2003; 307: 198-205). Vajdos et al. (J. Mol. Biol. 2002; 320: 415-428) also teaches that antigen binding is primarily mediated by the CDRs more highly conserved framework segments which connect the CDRs are mainly involved in supporting the CDR loop conformations and in some cases framework residues also contact antigen (page 416, left col.). Holm et al.(Mol. Immunol., 2007; 44: 1075-1084) teaches that although residues in the CDR3 of the heavy chain were involved in antigen binding, unexpectedly a residue in CDR2 of the light chain was also involved (abstract). Chen et al. (J. Mol. Bio., 1999; 293: 865-881) teaches that the antigen binding site is almost entirely composed of residues from heavy chain CDRs, CDR-H1, H2, H3 (page 866). Wu et al. (J. Mol. Biol., 1999; 294:151-162) teaches that it is difficult to predict which framework residues serve a critical role in maintaining affinity and specificity due in part to the large conformational change in antibodies that accompany antigen binding (page 152 left col.) but certain residues have been identified as important for maintaining conformation. These references demonstrate that in order to generate a binding member or an antibody with the claimed binding activity or features (i.e. binding to human Ab1-42 and decreasing CSF NfL levels in the AD patients compared to the NfL levels of the patients prior to treatment), the binding member or antibody must comprise all 6 CDRs with defined sequences or structures in order to maintain the claimed antigen binding specificity and affinity. However, the specification provides no such information to demonstrate that Applicant is in possession of the claimed genus of binding members that bind to human Ab1-42 and decrease CSF NfL levels in the AD patients compared to the NfL levels of the patients prior to treatment). The specification fails to provide sufficient descriptive information, such as definitive structural or functional features of the claimed genus of binding member. There is no information regarding the relation of structure of other binding members to the function of anti-Ab1-42 antibody MEDI1814 or Abet0380 antibody.. Furthermore, the prior art does not provide compensatory structural or correlative teachings sufficient to enable one of skill to identify what other binding members might be. Since the common characteristics/features of other binding members and other forms of AD or CNS neurodegenerative diseases are unknown, a skilled artisan cannot envision the functional correlations of the genus with the claimed invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the genus of binding members or all forms of AD or CNS neurodegenerative diseases.
Based on MPEP § 2161.01 and §2163, “to satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116”.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116).
As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of binding member, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483.
Therefore, the claimed methods have not met the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115). Applicant is directed to the Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, ¶ 1 "Written Description" Requirement. See MPEP § 2161.01 and 2163.
10. In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Claim Rejections - 35 USC § 102
11. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-5 and 7-24 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Groves et al. (US9834598, issued Dec 5, 2017, priority Oct 15, 2012) as evidenced by Mielke et al. (Neurology, 2019; 93: e252-e260), Weston et al. (Neurology, 2017;89:2167-2175), Mattsson et al. (JAMA Neurol., 2019; 76:791-799) and DIAN-TU-NCT04623242 (DIAN-TU clinical Study Protocol for NCT04623242 clinical trials, published Dec 20, 2019).
Claims 1-5 and 7-24 are drawn to methods for treating Alzheimer’s disease (AD) and preventing neuronal axonal damage in a patient, comprising administering a therapeutically effective amount of a binding member that selectively binds human amyloid beta 1-42 peptide (Ab1-42) to a patient, wherein the binding member decreases the level of neurofilament light chain (NfL) in the patient compared with the level of NfL in the patient pre-treatment with the binding member.
Groves et al. (US9834598) teach methods for treating AD and reducing neuronal axonal damage in an AD patient (see col. 40, line 30-col.43, line 67), comprising intravenously or subcutaneously administering (see col. 42, line 35-col. 3, line 67) to a patient in need thereof a therapeutically effective amount of a pharmaceutical composition comprising an anti-human Ab1-42 antibody Abet0380 o MEDI1814 (see col. 5-10; col. 13-2), which meets the limitations recited in instant claims.
The an anti-human Ab1-42 antibody Abet0380 or Abet0380-GL comprises a VH having the amino acid sequence of SEQ ID NO:398 which is 100% identical to instant SEQ ID NO:7 and a VL comprising the amino acid sequence of SEQ ID NO:299, which is 100% identical to instant SEQ ID NO:8 (i.e. Abet0380 antibody recited in claims 13-15) or the anti-human Ab1-42 antibody Abet0380 comprises a VH comprising the amino acid sequence of SEQ ID NO:524, which is 100% identical to instant SEQ ID NO:9 and a VL comprising the amino acid sequence of SEQ ID NO:533, which is 100% identical to SEQ ID NO:10 (i.e. MEDI1814 recited in claims 13-14) and wherein the Abet0380 antibody or MEDI1814 antibody comprises HCDRS1-3 and LCDRs1-3 of instant SEQ ID NOs: 1-6 respectively or variants with one or two amino acid mutations (see the sequence alignment below; col. 5-10; col. 13-20), or encoded by Abet0380-GL under accession Number 41890 as in claim 15 (see col.9, lines 45-60) and also have the biological properties and features including binding Ab1-42 with a KD of 500pM or less and does not bind Ab1-40or with a KD greater than 1mM recited in claim 12 (see col. 67, table 4; col. 77, table 1). Groves teaches that the antibody is a human IgG including human IgG1 or IgG2 including human IgG1-TM, IgG1-YTE or IgG1-TM-YTE as in claims 16-17 (see col.12, line 1-col. 13, line 9; col. 28, lines 22-33).
Groves teaches that the anti-human Ab1-42 antibody is administered at a dose of 100ug to 1g or 5mg/kg or 10mg/kg or 30mg/kg for systemic application (see col. 43, lines 52-53; col. 86-88, Example 4), which is overlapping with the claimed dose of ≥ 200mg or optionally about 200mg or about 300mg, about 900mg or about 1800mg in claim 18, at twice-weekly, weekly or monthly intervals or every two to four weeks for subcutaneous administration and every four to eight weeks for intravenous administration as in claim 20, which meets the limitations of at intervals of 3.5-4.5 weeks, optionally at intervals of 4 weeks (Q4W) in claim 19 (see col. 43, lines 57-64).
Groves teaches that the patients are positive for amyloid, and optionally negative or positive for tau and/or neurodegeneration based on a CSF marker, plasma marker or an imaging marker as in claims 7-9, wherein the CSF marker for amyloid is CSF Ab1-42as in claims 10-11 (see col.40, lines 60-col.41, line 35) Groves teaches that the neuronal axonal damage is associated with AD optionally mild-to-moderate AD, pre-symptomatic AD and/or mild cognitive impairment due to AD as in claim 21 (see col. 10, lines 17-39), which is also evidenced by Mattsson et al. (JAMA Neurology, 2019, 76:791-799) and DIAN-TU-NCT04623242. Groves teaches that the antibody is in comprised within a pharmaceutical composition as in claim 24 (see col. 42, lines 16-col. 13,line 3).
Groves teaches that administration of anti-human Ab1-42 antibody decreases free Ab1-42 in the CSF and plasma and increases total Ab1-42 in the brain tissue as compared to pre-treatment as in claim 23 (see col.12, lines 39-45; col 41, lines 59-67; col. 42, lines 1-15). Groves also teach the limitations “wherein the binding member decrease the level of neurofilament light chain (NfL) in the plasma, CSF” in claims 3-4, “decrease the level of NfL by at least 10%, 20%, 30% or 50%” in claim 5, “the level of pTau217 compared to pre-treatment” in claim 22, “the level of free Ab1-42 compared to pre-treatment and/or increases the level of total Ab1-42 compared to pre-treatment” in claim 23 because these limitations are in a wherein clause and are inherent results and features of administration of the anti-human Ab1-42 antibody Abet0380, which is identical to the anti-human Ab1-42 antibody Abet0380 disclosed in the Groves’ method. If the claimed antibody can decrease the level of NfL in the plasma and CSF by at least 10%...50% or the level of pTau217 or free Ab1-42 compared to pre-treatment, the same antibody used in the Groves’s method for treating AD can achieve the same results as recited in instant claims, which is also evidenced by Weston et al. (Neurology, 2017;89:2167-2175), Mattsson et al. (JAMA Neurology, 2019, 76:791-799) and DIAN-TU-NCT04623242.
Weston et al. teach that the serum NfL in patients with familial AD is increased prior to symptom onset and correlates with measures of disease stage and severity (see p.2167, abstract; Weston et al. Neurology, 2017;89:2167-2175). Mattsson et al. teach that the NfL level was increased at baseline in patients with mild cognitive impairment and AD dementia and increased in all diagnostic groups, with the greatest increase in patients with AD dementia, and a longitudinal increase in NfL level correlated with baseline CSF biomarkers (low Aβ42, high total tau, and high phosphorylated tau levels), magnetic resonance imaging measures, low fluorodeoxyglucose–positron emission tomography uptake, and poor cognitive performance for a global cognitive score, and the faster increase in NfL levels correlated with faster increase in CSF biomarkers of neuronal injury, faster rates of atrophy and hypometabolism, and faster worsening in global cognition in patients with mild cognitive impairment and AD dementia (see abstract). Thus, claims 1-5 and 7-24 are anticipated by Groves et al. (US9834598) as evidenced by Weston, Mattsson and DIAN-TU-NCT04623242.
SEQ ID NO:1-SEQ ID NO:2-SEQ ID NO:3
US-14-435-520-398
(NOTE: this sequence has 4 duplicates in the database searched)
Sequence 398, US/14435520
Patent No. 9834598
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 398
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380
Query Match 88.7%; Score 193.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 YQTMW--------------VIGKTNENIAYADSVKG------------------------ 22
||||| |||||||||||||||||
Db 31 YQTMWWVRQAPGRGLEWVSVIGKTNENIAYADSVKGRFTISRDNSKNTLYLQMNSLRAED 90
Qy 23 --------EWMDHSRPYYYYGMDV 38
||||||||||||||||
Db 91 TAVYYCAREWMDHSRPYYYYGMDV 114
US-14-435-520-524
(NOTE: this sequence has 4 duplicates in the database searched)
Sequence 524, US/14435520
Patent No. 9834598
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 88.7%; Score 193.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 YQTMW--------------VIGKTNENIAYADSVKG------------------------ 22
||||| |||||||||||||||||
Db 31 YQTMWWVRQAPGKGLEWVSVIGKTNENIAYADSVKGRFTISRDNSKNTLYLQMNSLRAED 90
Qy 23 --------EWMDHSRPYYYYGMDV 38
||||||||||||||||
Db 91 TAVYYCAREWMDHSRPYYYYGMDV 114
SEQ ID NO:7
US-14-435-520-398
(NOTE: this sequence has 4 duplicates in the database searched)
Sequence 398, US/14435520
Patent No. 9834598
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 398
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGRGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGRGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:9
US-14-435-520-524
(NOTE: this sequence has 4 duplicates in the database searched)
Sequence 524, US/14435520
Patent No. 9834598
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:4-SEQ ID NO:5-SEQ ID NO:6
US-14-435-520-317
(NOTE: this sequence has 4 duplicates in the database searched)
Sequence 317, US/14435520
Patent No. 9834598
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 317
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0373
Query Match 82.1%; Score 113.3; Length 106;
Best Local Similarity 36.5%;
Matches 27; Conservative 0; Mismatches 0; Indels 47; Gaps 2;
Qy 1 SGHNLEDKFAS---------------RDDKRPS--------------------------- 18
||||||||||| |||||||
Db 23 SGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSEIPERFSASNSGHTATLTISGTQATDE 82
Qy 19 -----SSQDTVTRV 27
|||||||||
Db 83 ADYYCSSQDTVTRV 96
SEQ ID NO:8
US-14-435-520-299
(NOTE: this sequence has 9 duplicates in the database searched)
Sequence 299, US/14435520
Patent No. 9834598
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 299
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0372
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQATDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQATDEADYYCSSQDTVTRVFGGGTKLTVL 106
SEQ ID NO:10
Sequence 533, US/14435520
Patent No. 9834598
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
Claim Rejections - 35 USC § 103
12. The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102 of this title, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-24 are rejected under 35 U.S.C. 103 as being unpatentable over Groves et al. (US9834598) in view of Mielke et al. (Neurology, 2019; 93: e252-e260), Weston et al. (Neurology, 2017;89:2167-2175), Mattsson et al. (JAMA Neurol., 2019; 76:791-799) and DIAN-TU-NCT04623242 (DIAN-TU clinical Study Protocol for NCT04623242 clinical trials, published Dec 20, 2019).
Even if Groves does not teach that the anti-human Ab1-42 antibody decreases the level of NfL in the patient compared with the level of NfL in the patient pre-treatment with the antibody in in the plasma or CSF as in claims 3-4, by at least 10%, 20%, 30% or 50% as in claim 5 or decreases the level of pTau217 compared to pre-treatment as in claim 22 or the level of free Ab1-42 compared to pre-treatment and/or increases the level of total Ab1-42 compared to pre-treatment as in claim 23, Weston, Mattsson and DIAN-TU-NCT04623242 teach these limitations and provide motivation and an expectation of success for the reasons set forth above and below.
Weston et al. teach that the serum NfL in patients with familial AD is increased prior to symptom onset and correlates with measures of disease stage and severity (see p.2167, abstract) and the serum level of NfL can be measured by ELISA including SIMOA-HD1 (see p. 2167, abstract; p.2167).
Mattsson et al. teach that the NfL level was increased at baseline in patients with mild cognitive impairment and AD dementia and increased in all diagnostic groups, with the greatest increase in patients with AD dementia, and a longitudinal increase in NfL level correlated with baseline CSF biomarkers (low Aβ42, high total tau, and high phosphorylated tau levels), magnetic resonance imaging measures, low fluorodeoxyglucose–positron emission tomography uptake, and poor cognitive performance for a global cognitive score, and the faster increase in NfL levels correlated with faster increase in CSF biomarkers of neuronal injury, faster rates of atrophy and hypometabolism, and faster worsening in global cognition in patients with mild cognitive impairment and AD dementia, which meets the limitations “patients are positive for amyloid, and optionally negative or positive for tau and/or neurodegeneration based on a CSF marker, plasma marker or an imaging marker” as in claims 7-9, “wherein the CSF marker for amyloid is CSF Ab1-42, the CSF marker for tau is CSF phosphor-tau, and the CSF marker for neurodegeneration is total tau and/or the imaging marker for amyloid is amyloid imaging, for tau is tau imaging and/or for neurodegeneration is magnetic resonance imaging (MRI0 or fluorodeoxyglucose positron emission tomography (PET)” as in claims 10-11 (see p. 791, abstract; p. 793-798.) Mattsson teaches that the change percentage in NfL level compared to baseline NfL in MCI is ~3-15% and in AD dementia is ~7-20% (see figure 2 and Table3). Mattsson teaches that the neuronal axonal damage (i.e. neurodegeneration) is associated with AD optionally mild-to-moderate AD, pre-symptomatic AD and/or mild cognitive impairment due to AD as in claim 21 (see p. 761 abstract).
DIAN-TU-NCT04623242 teaches methods for treating AD comprising intravenously or subcutaneously administering to a patient in need there an anti-human Ab1-42 antibody, Gantenerumab (RO4909832) at an initial dose of 225 mg or begins at 450 mg every four weeks, 675mg, 900mg or 1200mg every four weeks (p. 135-143; p. 150 table 5) or Solanezumab (LY2062430) at 800mg or 1600mg every four weeks (see p.212-222, table 5). DIAN-TU-NCT04623242 teaches that the increased NfL level in patients with mild cognitive impairment (MCI) and AD dementia compared to the baseline is decreased in the MCI and AD patients treated with the anti-human Ab1-42 antibody, and that the levels of free Aβ42, tau, and phosphorylated tau are also decreased levels in the MCI and AD patients treated with the anti-human Ab1-42 antibody, Gantenerumab (RO4909832) or Solanezumab (LY2062430) (see p.120; p. 210-211; p. 213-214). DIAN-TU-NCT04623242 teaches that the increased NfL level in the plasma or CSF in the patients with MCI and AD dementia correlated with baseline CSF biomarkers (low Aβ42, high total tau, and high phosphorylated tau levels), magnetic resonance imaging measures, low fluorodeoxyglucose–positron emission tomography uptake, and poor cognitive performance (see p. 8-9; p. 27-31; p. 44-45). DIAN-TU-NCT04623242 teaches that patients are positive for amyloid, and optionally negative or positive for tau and/or neurodegeneration based on a CSF marker, plasma marker or an imaging marker as in claims 7-9 and that the CSF marker for amyloid is CSF Ab1-42, the CSF marker for tau is CSF phosphor-tau, and the CSF marker for neurodegeneration is total tau and/or the imaging marker for amyloid is amyloid imaging, for tau is tau imaging and/or for neurodegeneration is magnetic resonance imaging (MRI0 or fluorodeoxyglucose positron emission tomography (PET) as in claims 10-11 (see p. 27-31; p. 44-45; p.70-80). DIAN-TU-NCT04623242 teaches that the neuronal axonal damage is associated with AD optionally mild-to-moderate AD, pre-symptomatic AD and/or mild cognitive impairment due to AD as in claim 21 (see p.27-31).
A person of ordinary skill in the art would have recognized that selecting and applying the known decreased level of NfL including at least 10%, 20%, 30% or 50% decrease, the known decreased level of pTau217, the known decrease level of free Ab1-42 in the plasma or CSF of the patients after treatment with the anti-human Ab1-42 antibody compared with the levels of NfL, pTau217 and free Ab1-42 in the plasma or CSF of the patient prior to the treatment and the known technique disclosed by Weston, Mattsson and DIAN-TU-NCT04623242 to the Groves’ method would have yielded the predictable result of decreasing the level of NfL including at least 10%, 20%, 30% or 50% decrease, decreasing the level of pTau217 and decreasing the level of free Ab1-42 in the plasma or CSF of the patients after treatment with the anti-human Ab1-42 antibody compared with the levels of NfL, pTau217 and free Ab1-42 in the plasma or CSF of the patient prior to the treatment.
Using and including the known decreased level of NfL including at least 10%, 20%, 30% or 50% decrease, the known decreased level of pTau217, the known decrease level of free Ab1-42 in the plasma or CSF of the patients after treatment with the anti-human Ab1-42 antibody compared with the levels of NfL, pTau217 and free Ab1-42 in the plasma or CSF of the patient prior to the treatment disclosed by Weston, Mattsson and DIAN-TU-NCT04623242 in the Groves’ method would provide an improvement and better treatment based on measuring and monitoring the decreased level of NfL, the decreased level of pTau217 and the decreased level of free Ab1-42 in the plasma or CSF of the patients after treatment with the anti-human Ab1-42 antibody compared with the levels in the plasma or CSF of the patient prior to the treatment, and expand application of the Groves’ method, and would increase patient’s satisfaction with treatment of AD using an human Ab1-42 antibody including the anti-human Ab1-42 Abet0380 antibody or the anti-human Ab1-42MEDI1814 antibody.
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to select and apply the known decreased level of NfL including at least 10%, 20%, 30% or 50% decrease, the known decreased level of pTau217, the known decrease level of free Ab1-42 in the plasma or CSF of the patients after treatment with the anti-human Ab1-42 antibody compared with the levels of NfL, pTau217 and free Ab1-42 in the plasma or CSF of the patient pre-treatment with the antibody to the method of Groves and yield the predictable result of decreasing the level of NfL including by at least 10%, 20%, 30% or 50% decrease in the patient compared with the level of NfL in the patient pre-treatment with the antibody, or decreasing the level of pTau217 compared to pre-treatment or the level of free Ab1-42 compared to pre-treatment and/or increasing the level of total Ab1-42 compared to pre-treatment.
Double Patenting
13. The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 5-7 of U.S. Patent No. 9834598, claims 9-12 of U.S. Patent No. 10662239, claims 14-17 of U.S. Patent No.11286297, claims 10-12 U.S. Patent No. 12098191, claims 17-20 U.S. Patent No. 12344664 in view of Weston et al. (2017), Mattsson et al. (2019) and DIAN-TU-NCT04623242 (2019).
Claims 5-7 of US9834598 (the ‘598 patent), claims 9-12 of US10662239 (the ‘239 patent), claims 14-17 of US11286297 (the ‘297 patent), claims 10-12 US12098191 (the ‘191 patent) or claims 17-20 US12344664 (the ‘664 patent) claim a method of treating a human or animal subject having an amyloidosis associated with amyloid beta, the method comprising administering to the subject an anti-human Ab1-42 antibody including MEDI1814 and Abet0380 antibody wherein the anti-human Ab1-42 antibody comprises (i) a VH comprising the Abet0380 set of HCDRs, wherein the amino acid sequences of the Abet0380 HCDRs are HCDR1 SEQ ID NO: 525, HCDR2 SEQ ID NO: 526, and HCDR3 SEQ ID NO: 527, or comprising the Abet0380 set of HCDRs with one or two amino acid mutations, and (ii) a VL domain comprising the Abet0380 set of LCDRs, wherein the amino acid sequences of the Abet0380 LCDRs are LCDR1 SEQ ID NO: 534 LCDR2 SEQ ID NO: 535, and LCDR3 SEQ ID NO: 536, or comprising the Abet0380 set of LCDRs with one or two amino acid mutations.
While the claims of the ‘598, the ‘239, the ‘297, the ‘191 or the ‘664 patent do not explicitly recite the limitation “teach that the anti-human Ab1-42 antibody decreases the level of NfL in the patient compared with the level of NfL in the patient pre-treatment with the antibody in in the plasma or CSF as in claims 3-4, by at least 10%, 20%, 30% or 50% as in claim 5 or decreases the level of pTau217 compared to pre-treatment as in claim 22 or the level of free Ab1-42 compared to pre-treatment and/or increases the level of total Ab1-42 compared to pre-treatment as in claim 23, Weston, Mattsson and DIAN-TU-NCT04623242 teach these limitations and provide motivation and an expectation of success for the reasons set forth above. Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to select and apply the known decreased level of NfL including at least 10%, 20%, 30% or 50% decrease, the known decreased level of pTau217, the known level of free Ab1-42 in the plasma or CSF of the patient treated with the anti-human Ab1-42 antibody compared with the levels of NfL, pTau217 and ree Ab1-42 in the plasma or CSF of the patient pre-treatment with the antibody and the technique disclosed by Weston, Mattsson and DIAN-TU-NCT04623242 to the method of the ‘598, the ‘239, the ‘297, the ‘191 or the ‘664 patent and yield the predictable result of decreasing the level of NfL including by at least 10%, 20%, 30% or 50% decrease in the patient compared with the level of NfL in the patient pre-treatment with the antibody, or decreasing the level of pTau217 compared to pre-treatment or the level of free Ab1-42 compared to pre-treatment and/or increasing the level of total Ab1-42 compared to pre-treatment.
Double Patenting
14. Claims 1-24 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 15-17 of copending Application No. 17/535059, claims 1-31 of copending Application No.18/260125, claims 1,7-16, 19-21, 32-33, 38-39, 73-74 of copending Application No. 18/549803, claims 57-60 of copending Application No. 18/604668, claims 15-19 of copending Application No. 18/628082, claims 26-119 of copending Application No. 18/705490, claims 26-119 of copending Application No. 18/705493, claims 26-30 of copending Application No. 18/705500 or claim 24 of copending Application No. 19/221202 in view of Weston et al. (2017), Mattsson et al. (2019) and DIAN-TU-NCT04623242 (2019).
Claims 15-17 of 17/535059 (the ‘059 Application), claims 1-31 of 18/260125 (the ‘125 Application), claims 1,7-16, 19-21, 32-33, 38-39, 73-74 of 18/549803 (the ‘803 Application), claims 57-60 of 18/604668 (the ‘668 Application), claims 15-19 of 18/628082 (the ‘082 Application), claims 26-119 of 18/705490 (the ‘490 Application), claims 26-119 of 18/705493 (the ‘493 Application), claims 26-30 of 18/705500 (the ‘500 Application) or claim 24 of 19/221202 (the ‘202 Application) claim a method of treating a human or animal subject having an amyloidosis associated with amyloid beta, the method comprising administering to the subject an anti-human Ab1-42 antibody including MEDI1814 and Abet0380 antibody wherein the anti-human Ab1-42 antibody comprises (i) a VH comprising the Abet0380 set of HCDRs, wherein the amino acid sequences of the Abet0380 HCDRs are HCDR1 SEQ ID NO: 525, HCDR2 SEQ ID NO: 526, and HCDR3 SEQ ID NO: 527, or comprising the Abet0380 set of HCDRs with one or two amino acid mutations, and (ii) a VL domain comprising the Abet0380 set of LCDRs, wherein the amino acid sequences of the Abet0380 LCDRs are LCDR1 SEQ ID NO: 534 LCDR2 SEQ ID NO: 535, and LCDR3 SEQ ID NO: 536, or comprising the Abet0380 set of LCDRs with one or two amino acid mutations.
While the claims of the ‘059, the ‘125, the ‘803, the ‘668, the ‘082, the ‘490, the ‘493, the ‘500 or the ‘202 Application do not explicitly recite the limitation “teach that the anti-human Ab1-42 antibody decreases the level of NfL in the patient compared with the level of NfL in the patient pre-treatment with the antibody in in the plasma or CSF as in claims 3-4, by at least 10%, 20%, 30% or 50% as in claim 5 or decreases the level of pTau217 compared to pre-treatment as in claim 22 or the level of free Ab1-42 compared to pre-treatment and/or increases the level of total Ab1-42 compared to pre-treatment as in claim 23, Weston, Mattsson and DIAN-TU-NCT04623242 teach these limitations and provide motivation and an expectation of success for the reasons set forth above. Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to select and apply the known decreased level of NfL including at least 10%, 20%, 30% or 50% decrease, the known decreased level of pTau217, the known level of free Ab1-42 in the plasma or CSF of the patient treated with the anti-human Ab1-42 antibody compared with the levels of NfL, pTau217 and ree Ab1-42 in the plasma or CSF of the patient pre-treatment with the antibody disclosed by Weston, Mattsson and DIAN-TU-NCT04623242 to the method of the ‘059, the ‘125, the ‘803, the ‘668, the ‘082, the ‘490, the ‘493, the ‘500 or the ‘202 Application, and yield the predictable result of decreasing the level of NfL including by at least 10%, 20%, 30% or 50% decrease in the patient compared with the level of NfL in the patient pre-treatment with the antibody, or decreasing the level of pTau217 compared to pre-treatment or the level of free Ab1-42 compared to pre-treatment and/or increasing the level of total Ab1-42 compared to pre-treatment.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
15. NO CLAIM IS ALLOWED.
Sequence alignment
VH
SEQ ID NO:7(Abet0380) 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGRGLEWVSVIGKTNENIAY 60
SEQ ID NO:9(MEDI1814) 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
SEQ ID NO:7(Abet0380) 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
SEQ ID NO:9(MEDI1814) 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
SEQ ID NO:7(Abet0380) 121 VTVSS 125
SEQ ID NO:9(MEDI1814) 121 VTVSS 125
VL
SEQ ID NO:8(Abet0380) 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
SEQ ID NO:10(MEDI1814) 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
SEQ ID NO:8(Abet0380) 61 FSASNSGHTATLTISGTQATDEADYYCSSQDTVTRVFGGGTKLTVL 106
SEQ ID NO:10(MEDI1814) 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
16. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
US10662239 (under the ODP rejection) teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:1-SEQ ID NO:2-SEQ ID NO:3
Sequence 398, US/15793510
Patent No. 10662239
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-302
CURRENT APPLICATION NUMBER: US/15/793,510
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 398
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380
Query Match 88.7%; Score 193.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 YQTMW--------------VIGKTNENIAYADSVKG------------------------ 22
||||| |||||||||||||||||
Db 31 YQTMWWVRQAPGRGLEWVSVIGKTNENIAYADSVKGRFTISRDNSKNTLYLQMNSLRAED 90
Qy 23 --------EWMDHSRPYYYYGMDV 38
||||||||||||||||
Db 91 TAVYYCAREWMDHSRPYYYYGMDV 114
SEQ ID NO:9
Sequence 524, US/15793510
Patent No. 10662239
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-302
CURRENT APPLICATION NUMBER: US/15/793,510
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/15793510
Patent No. 10662239
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-302
CURRENT APPLICATION NUMBER: US/15/793,510
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US11286297 (under the ODP rejection) teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:1-SEQ ID NO:2-SEQ ID NO:3
Sequence 398, US/16864439
Patent No. 11286297
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-303
CURRENT APPLICATION NUMBER: US/16/864,439
CURRENT FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 398
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380
Query Match 88.7%; Score 193.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 YQTMW--------------VIGKTNENIAYADSVKG------------------------ 22
||||| |||||||||||||||||
Db 31 YQTMWWVRQAPGRGLEWVSVIGKTNENIAYADSVKGRFTISRDNSKNTLYLQMNSLRAED 90
Qy 23 --------EWMDHSRPYYYYGMDV 38
||||||||||||||||
Db 91 TAVYYCAREWMDHSRPYYYYGMDV 114
SEQ ID NO:9
Sequence 524, US/16864439
Patent No. 11286297
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-303
CURRENT APPLICATION NUMBER: US/16/864,439
CURRENT FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SESQ ID NO:10
Sequence 533, US/16864439
Patent No. 11286297
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-303
CURRENT APPLICATION NUMBER: US/16/864,439
CURRENT FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US12098191 (under the ODP rejection) teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:1-SEQ ID NO:2-SEQ ID NO:3
Sequence 398, US/17673449
Patent No. 12098191
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-304
CURRENT APPLICATION NUMBER: US/17/673,449
CURRENT FILING DATE: 2022-02-16
PRIOR APPLICATION NUMBER: 16/864,439
PRIOR FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 398
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380
Query Match 88.7%; Score 193.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 YQTMW--------------VIGKTNENIAYADSVKG------------------------ 22
||||| |||||||||||||||||
Db 31 YQTMWWVRQAPGRGLEWVSVIGKTNENIAYADSVKGRFTISRDNSKNTLYLQMNSLRAED 90
Qy 23 --------EWMDHSRPYYYYGMDV 38
||||||||||||||||
Db 91 TAVYYCAREWMDHSRPYYYYGMDV 114
SEQ ID NO:9
equence 524, US/17673449
Patent No. 12098191
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-304
CURRENT APPLICATION NUMBER: US/17/673,449
CURRENT FILING DATE: 2022-02-16
PRIOR APPLICATION NUMBER: 16/864,439
PRIOR FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/17673449
Patent No. 12098191
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-304
CURRENT APPLICATION NUMBER: US/17/673,449
CURRENT FILING DATE: 2022-02-16
PRIOR APPLICATION NUMBER: 16/864,439
PRIOR FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US12344664 (under the ODP rejection) teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:1-SEQ ID NO:2-SEQ ID NO:3
Sequence 398, US/18604668
Patent No. 12344664
GENERAL INFORMATION
APPLICANT: MedImmune Limited (en)
TITLE OF INVENTION: ANTIBODIES TO AMYLOID BETA (en)
FILE REFERENCE: 137266-5011-US01
CURRENT APPLICATION NUMBER: US/18/604,668
CURRENT FILING DATE: 2024-03-14
NUMBER OF SEQ ID NOS: 577
SEQ ID NO 398
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
organism = Homo sapiens
Query Match 88.7%; Score 193.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 YQTMW--------------VIGKTNENIAYADSVKG------------------------ 22
||||| |||||||||||||||||
Db 31 YQTMWWVRQAPGRGLEWVSVIGKTNENIAYADSVKGRFTISRDNSKNTLYLQMNSLRAED 90
Qy 23 --------EWMDHSRPYYYYGMDV 38
||||||||||||||||
Db 91 TAVYYCAREWMDHSRPYYYYGMDV 114
SEQ ID NO:9
Sequence 524, US/18604668
Patent No. 12344664
GENERAL INFORMATION
APPLICANT: MedImmune Limited (en)
TITLE OF INVENTION: ANTIBODIES TO AMYLOID BETA (en)
FILE REFERENCE: 137266-5011-US01
CURRENT APPLICATION NUMBER: US/18/604,668
CURRENT FILING DATE: 2024-03-14
NUMBER OF SEQ ID NOS: 577
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
organism = Homo sapiens
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/18604668
Patent No. 12344664
GENERAL INFORMATION
APPLICANT: MedImmune Limited (en)
TITLE OF INVENTION: ANTIBODIES TO AMYLOID BETA (en)
FILE REFERENCE: 137266-5011-US01
CURRENT APPLICATION NUMBER: US/18/604,668
CURRENT FILING DATE: 2024-03-14
NUMBER OF SEQ ID NOS: 577
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..106
QUALIFIERS: mol_type = protein
organism = Homo sapiens
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US20150299299 teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:9
US-14-435-520-524
(NOTE: this sequence has 6 duplicates in the database searched)
Sequence 524, US/14435520
Publication No. US20150299299A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/14435520
Publication No. US20150299299A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: ABETA-100WO1
CURRENT APPLICATION NUMBER: US/14/435,520
CURRENT FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US20180105585 teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:9
Sequence 524, US/15793510
Publication No. US20180105585A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-302
CURRENT APPLICATION NUMBER: US/15/793,510
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 479, US/15793510
Sequence 533, US/15793510
Publication No. US20180105585A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-302
CURRENT APPLICATION NUMBER: US/15/793,510
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US20190262327 teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:9
Sequence 524, US/16085180
Publication No. US20190262327A1
GENERAL INFORMATION
APPLICANT: ASTRAZENECA AB
TITLE OF INVENTION: COMBINATION OF A BACE INHIBITOR AND AN ANTIBODY OR ANTIGEN-BINDING FRAGMENT FOR THE TREATMENT OF A D
TITLE OF INVENTION: ISORDER ASSOCIATED WITH THE ACCUMULATION OF AMYLOID BETA
FILE REFERENCE: 1848081-0002-090-301
CURRENT APPLICATION NUMBER: US/16/085,180
CURRENT FILING DATE: 2018-09-14
PRIOR APPLICATION NUMBER: PCT/EP2017/056180
PRIOR FILING DATE: 2017-03-15
PRIOR APPLICATION NUMBER: US 62/308,698
PRIOR FILING DATE: 2016-03-15
NUMBER OF SEQ ID NOS: 648
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
NAME/KEY: source
OTHER INFORMATION: /note="Abet0380-GL"
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/16085180
Publication No. US20190262327A1
GENERAL INFORMATION
APPLICANT: ASTRAZENECA AB
TITLE OF INVENTION: COMBINATION OF A BACE INHIBITOR AND AN ANTIBODY OR ANTIGEN-BINDING FRAGMENT FOR THE TREATMENT OF A D
TITLE OF INVENTION: ISORDER ASSOCIATED WITH THE ACCUMULATION OF AMYLOID BETA
FILE REFERENCE: 1848081-0002-090-301
CURRENT APPLICATION NUMBER: US/16/085,180
CURRENT FILING DATE: 2018-09-14
PRIOR APPLICATION NUMBER: PCT/EP2017/056180
PRIOR FILING DATE: 2017-03-15
PRIOR APPLICATION NUMBER: US 62/308,698
PRIOR FILING DATE: 2016-03-15
NUMBER OF SEQ ID NOS: 648
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
NAME/KEY: source
OTHER INFORMATION: /note="Abet0380-GL"
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US20210009665 teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:9
Sequence 524, US/16864439
Publication No. US20210009665A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-303
CURRENT APPLICATION NUMBER: US/16/864,439
CURRENT FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/16864439
Publication No. US20210009665A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-303
CURRENT APPLICATION NUMBER: US/16/864,439
CURRENT FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: US 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US20220251181 teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:9
Sequence 524, US/17673449
Publication No. US20220251181A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-304
CURRENT APPLICATION NUMBER: US/17/673,449
CURRENT FILING DATE: 2022-02-16
PRIOR APPLICATION NUMBER: 16/864,439
PRIOR FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/17673449
Publication No. US20220251181A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited
TITLE OF INVENTION: Antibodies to Amyloid Beta
FILE REFERENCE: 1848081-0002-094-304
CURRENT APPLICATION NUMBER: US/17/673,449
CURRENT FILING DATE: 2022-02-16
PRIOR APPLICATION NUMBER: 16/864,439
PRIOR FILING DATE: 2020-05-01
PRIOR APPLICATION NUMBER: 15/793,510
PRIOR FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: 14/435,520
PRIOR FILING DATE: 2015-04-14
PRIOR APPLICATION NUMBER: PCT/EP2013/071567
PRIOR FILING DATE: 2013-10-15
PRIOR APPLICATION NUMBER: 61/713996
PRIOR FILING DATE: 2012-10-15
NUMBER OF SEQ ID NOS: 578
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
OTHER INFORMATION: Abet0380-GL
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US20240294619 teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:9
Sequence 524, US/18604668
Publication No. US20240294619A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited (en)
TITLE OF INVENTION: ANTIBODIES TO AMYLOID BETA (en)
FILE REFERENCE: 137266-5011-US01
CURRENT APPLICATION NUMBER: US/18/604,668
CURRENT FILING DATE: 2024-03-14
NUMBER OF SEQ ID NOS: 577
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
organism = Homo sapiens
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/18604668
Publication No. US20240294619A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited (en)
TITLE OF INVENTION: ANTIBODIES TO AMYLOID BETA (en)
FILE REFERENCE: 137266-5011-US01
CURRENT APPLICATION NUMBER: US/18/604,668
CURRENT FILING DATE: 2024-03-14
NUMBER OF SEQ ID NOS: 577
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..106
QUALIFIERS: mol_type = protein
organism = Homo sapiens
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
US20250304670 teaches anti-Abeta antibody comprising a VH and a VL wherein the VH comprises the amino acid sequence of SEQ ID NO:524 which is 100% identical to instant SEQ ID NO:9 and the VL comprises the amino acid sequence of SEQ ID NO:533, which is 100% identical to instant SEQ ID NO:10 (see the sequence alignment below).
SEQ ID NO:9
Sequence 524, US/19221202
Publication No. US20250304670A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited (en)
TITLE OF INVENTION: ANTIBODIES TO AMYLOID BETA (en)
FILE REFERENCE: 137266-5011-US02
CURRENT APPLICATION NUMBER: US/19/221,202
CURRENT FILING DATE: 2025-05-28
NUMBER OF SEQ ID NOS: 577
SEQ ID NO 524
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
organism = Homo sapiens
Query Match 100.0%; Score 674; Length 125;
Best Local Similarity 100.0%;
Matches 125; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASMGNFNYQTMWWVRQAPGKGLEWVSVIGKTNENIAY 60
Qy 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREWMDHSRPYYYYGMDVWGQGTL 120
Qy 121 VTVSS 125
|||||
Db 121 VTVSS 125
SEQ ID NO:10
Sequence 533, US/19221202
Publication No. US20250304670A1
GENERAL INFORMATION
APPLICANT: MedImmune Limited (en)
TITLE OF INVENTION: ANTIBODIES TO AMYLOID BETA (en)
FILE REFERENCE: 137266-5011-US02
CURRENT APPLICATION NUMBER: US/19/221,202
CURRENT FILING DATE: 2025-05-28
NUMBER OF SEQ ID NOS: 577
SEQ ID NO 533
LENGTH: 106
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..106
QUALIFIERS: mol_type = protein
organism = Homo sapiens
Query Match 100.0%; Score 556; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYELTQPPSVSVSPGQTASITCSGHNLEDKFASWYQQKPGQSPVLVIYRDDKRPSGIPER 60
Qy 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSASNSGHTATLTISGTQAMDEADYYCSSQDTVTRVFGGGTKLTVL 106
17. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHANG-YU WANG whose telephone number is (571)272-4521. The examiner can normally be reached on Monday-Thursday, 7:00am-5:00pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached on 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see https://ppair-my.uspto.gov/pair/PrivatePair. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Chang-Yu Wang
January 14, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675