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 the Claims
1. Claims 1-26 are the original claims filed 8/26/2022. In the Preliminary Amendment of 8/26/2022, claims 1-25 are amended and claim 26 is canceled. In the Reply of 8/7/2025, claims 1-25 are amended. In the Response of 3/23/2026, claims 1-2, 9, 11-12, 14-15, and 18-25 are amended, and claims 3-8, and 17 are canceled. Claim 20 is amended in the claim set of 3/23/2026 but without an updated status identifier. To advance compact prosecution, the status identifier is amended for claim 20.
Claims 1-2, 9-16, 18-25 are all the claims.
The Office Action is final.
Priority
2. USAN 17/802,817, filed 08/26/2022, is a National Stage entry of PCT/EP2021/ 055068, International Filing Date: 03/01/2021, claims foreign priority to EP 20159913.1, filed 02/27/2020, claims foreign priority to EP 20206317.8, filed 11/06/2020.
Information Disclosure Statement
3. As of 4/10/2026, a total of two (2) IDS are filed: 8/26/2025; and 3/11/2026. The corresponding initialed and dated 1449 form is considered and of record.
Withdrawal of Objections
Claim Objections
4. The objection to Claims
b) claim 1 is amended to delete “has not received organ support
d) claims 11-12 are amended to recite “taken from said patient.”
e) claim 14 is amended to recite “of at least [10-7] 10-7 M.”
f) claim 15 is amended to recite “between 1 x 10-9 to 3 x 10-9”
g) claim 18 is amended to recite “
h) claim 19 is amended to to recite “…an ADM stabilizing antibody or fragment thereof that enhances the half-life for the retention time[)] of ADM in serum, blood, or plasma by at least 10%.”
i) claim 21 is amended to recite “…wherein said method further comprises administering
j) claim 22 is amended to recite
“…is a human monoclonal antibody or an antibody fragment thereof that binds to ADM , wherein the heavy chain comprises the sequences: CDR1: SEQ ID NO: 5 GYTFSRYW; CDR2: SEQ ID NO: 6 ILPGSGST; and CDR3: SEQ ID NO: 7 TEGYEYDGFDY, and wherein the light chain comprises the sequences: CDR1: SEQ ID NO: 8 QSIVYSNGNTY; CDR2: RVS; and CDR3: SEQ ID NO: 9 FQGSHIPYT.
k) claim 23 is amended to recite “a sequence selected from the group
m) claim 24 is amended to replace “…that is > 95% identical to it” with “…that is at least 95% identical.”
n) claim 1 is amended to recite “the N-terminus of ADM[:] of the sequence YRQSMNNFQGLRSFGCRFGTC (SEQ ID No. 4).”
o) claim 25 is amended to recite “the N-terminus of ADM[:] of the sequence YRQSMNNFQG (SEQ ID No. 25).
p) Claim 17 is canceled.
q) Claim 5 is canceled thus overcoming the objection under 37 CFR 1.75 as being a substantial duplicate of claim 1.
Withdrawal of Rejections
Claim Rejections - 35 USC § 112(b)
5. The rejection of Claims 4, 6, 9, 14-15, and 20 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite is moot for the canceled claims and withdrawn for the pending claims.
a) Claims 4 and 6 are canceled.
b) Claim 9 is amended to delete “in particular” and the phrase associated therewith.
c) Claims 14-15 are amended to delete the trademark/trade name “Biacore.”
d) Claim 20 is amended to delete the term “hADM 22-25.”
Objections Maintained
Specification
6. The objections to the disclosure because of informalities is maintained.
Applicants allege “The specification has been amended as requested in the Office Action to render the objections moot.” A bona fide search of all the documents filed in the IDS of 3/11/2026 and the Response of 3/26/2026 does not reveal a document containing the alleged amended specification. THE RESPONSE IS INCOMPLETE.
a) The disclosure is objected to because it contains two (2) instances of an embedded hyperlink and/or other form of browser-executable code, i.e., (https). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
b) The use of the term, i.e., BiaCore, Sulfolink, nanobody, 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.
c) The specification contains the peptide sequence “Ala-Ala-Ala-Ala” that is > 4 amino acids in length and required to be identified by sequence identifier (SEQ ID NO) pursuant to 37 CFR 1.821-1.825.
The objections are maintained.
Claim Objections
7. The objection to Claims
Applicants allege the claims have been amended as requested in the Office Action to render the claim objections moot by complying in every instance where the Office Action identified a requested change. THE RESPONSE IS INCOPLETE.
a) The objection to Claims
b) The objection to claim 9 is maintained. Amend claim 9 to recite “…wherein said shock [that] is selected from the group”.
l) Amend claim 23 to insert proper punctuation, i.e., a semi-colon, between the species of VH region and the species of VL region. Also include the term “or” between the penultimate and final species of the VH region and the VL region.
Rejections Maintained
Claim Rejections - 35 USC § 112(a)
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.
Written Description
8. The rejection of Claims
Applicants allege the claims require performing the claim product by process and whatever product results from that product by process is what is administered to the claimed patient class; product by process claiming offers an alternative to defining the structure of the subject matter being claimed; the specification includes specific examples walking one skilled in the art through the claim method steps and providing table 1 showing specific examples of antibodies derived from these process steps; MPEP § 2163(II)(A)(3)(a)(i) specifically addresses a situation where applicants use a product by process to in their claims which is supported by an example in the specification.
Response to Arguments
For the record, the claims are drawn to a method of treating shock (not to the genus of antibodies yielded by the process steps), wherein a product-by-process is incorporated into the body of the treatment claim. The claims are examined for the genus of products produced by the product-by-process steps that possess a structure/function correlation for the treatment of shock in a subject in need thereof so long as the generic anti-ADM antibody is administered “within 10 hours after the occurrence of shock” (claim 1) and that meet the structure/function requirements of claims 10-16, 18-21.
AS regards MPEP § 2163(II)(A)(3)(a)(i), Applicants do not identify the “situation” under the section that pertains to the instant fact scenario. Where the outstanding grounds are based on a lack of structure/function correlation for a therapeutic antibody, Applicants do not identify the “situation” where product-by-process steps are introduced into a method of treatment in order to satisfy a written description requirement for a therapeutic antibody having a treatment effect.
MPEP § 2163(II)(A)(3)(a):
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that inventor 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. Enzo Biochem, 323 F.3d at 964, 63 USPQ2d at 1613 (quoting the Written Description Guidelines, 66 Fed. Reg. at 1106, n. 49, stating that “if the art has established a strong correlation between structure and function, one skilled in the art would be able to predict with a reasonable degree of confidence the structure of the claimed invention from a recitation of its function”.). “Thus, the written description requirement may be satisfied through disclosure of function and minimal structure when there is a well-established correlation between structure and function.” Id.
Applicants’ response does not address the extensive legal and technical arguments presented in the Office Action of 9/23/2025 that address the complexity and unpredictability of identifying therapeutic antibodies. THE RESPONSE IS INCOMPLETE.
Detailed comments from the Office Action of 9/23/2025 excerpted as follows:
“Claim interpretation
Claim 1 is a generic claim and drawn to a method of treatment for a patient being in, having or with shock, comprising an anti-ADM antibody or fragment thereof that binds the peptide sequence region of SEQ ID NO: 4 of ADM and wherein the administration is contingent on the condition of the patient as follows: has suffered from shock for no longer than 10 hours at the starting point of treatment; has been admitted to an ICU no longer than 10 hours at the starting point of treatment; and/or has not received organ support or not longer than 10 hours of organ support at the starting point of treatment.
Claim 5 is a generic claim and drawn to a method of treatment a patient suffering from shock comprising an anti-ADM antibody or fragment thereof that binds the peptide sequence region of SEQ ID NO: 4 of ADM and wherein the administration is contingent on the condition of the patient as follows: within 10 hours after occurrence of shock in said patient; within 10 hours after admission of said patient to ICU; and /or before the patient has received organ support or within not longer than 10 hours of organ support.
“treatment”: the specification differentiates treatment (therapy) from prevention (prophylaxis)
[0327] Further preferred embodiments of the present invention relate to methods of therapy (e.g., treatment, curing, alleviating, improving, amelioration, etc.) or prevention of symptoms as defined in any of the foregoing embodiments comprising administering to a subject in need thereof the ADM antibody or an ADM antibody fragment or non-Ig-scaffold according to any of preceding embodiments. The subject is preferably a human.
The structural aspects of the anti-ADM antibody that are imbued with the alleged functionalized properties of the method claims are disclosed in Claims 22-24.
Otherwise, the claims are directed to methods of administering an antibody wherein the antibody is not defined by the critical regions of its primary structure (i.e., the CDR regions, or the heavy and light chain variable regions). Functional limitations are recited, including an explicit recitation that the antibody must bind ADM, and an implicit function that the antibody must inhibit or neutralize ADM in order to be therapeutically effective. Structural limitations other than amino acid sequence, including type of IgG1 Fc regions are recited. Therefore, all of the rejected claims read on methods of administering a genus of antibodies comprising less than the full complement of six CDR sequences much less even single domain antibodies. Additionally, the claims do not recite a structure for the recited antigen, ADM but for the N-terminal amino acids of SEQ ID NO: 4 or 25.
In summary, the claims recite a method of administering a genus of antibody products having (1) an explicitly recited functional feature of specifically binding any ADM protein and (2) an implied functional feature of inhibiting ADM such that the antibody products have the required activity in the therapeutic methods. However, the claims recite only minimal structural features or partial structural features for the genus of shock syndromes.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through establishment of a structure-function correlation (by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics) or through a sufficient description of a representative number of species. Either is considered sufficient to show the applicant was in possession of the claimed genus.
Regarding structure-function correlation, it is noted that one of skill in the art was aware that there is a lack of structure-function correlation in antibody molecules.
By the time the invention was made, it was well-established in the art that the formation of an intact antigen-binding surface on an antibody required the association of the complete heavy and light chain variable regions, 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 ((PTO-892) (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1). While this overall architecture is shared among antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure each antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level, even when the same antigen is bound (Edwards et al., J Mol Biol 334:103-118 (2003) (PTO-892); see also Marchalonis et al., Dev & Comp Immunol. 30:223-247 (2006) (PTO-892), summarized in Abstract and Conclusion.
Methods of preparing antibodies from a variety of species to a protein or peptide of interest were well-established in the art at the time the invention was made. But application of those methods to any given antibody was still a matter of trial-and-error testing, and the skilled person could not automatically predict which residues in the CDRs would be tolerant of mutations, or which amino acid substitutions would maintain antigen binding. Overall, at the time the invention was made, the level of skill for preparing antibodies and then selecting those antibodies with desired functional properties was high. For example, it is generally the case that absent the fundamental structure provided for by all six CDRs of a parental antibody in the context of appropriate VH and VL framework sequences, a person of ordinary skill cannot visualize or otherwise predict, what an antibody with a particular set of functional properties would look like structurally.
Moreover, persons of ordinary skill in the art have long since acknowledged that even minor changes in the amino acid sequences of the VH and VL, particularly in the CDRs, may dramatically affect antigen-binding function. Lippow, for example, teaches that a single point mutation in the CDR of a parent antibody led to as much as an eightfold improvement in binding affinity in the resulting mutant (p. 1172, left col., lines 7-8 from end of first full paragraph and Table 1a) (Lippow et al., “Computational design of antibody-affinity improvement beyond in vivo maturation,” Nature Biotechnology, 25(10):1171-1176 (2007) (PTO-892).
Sulea teaches that individual point mutations gave an improvement of one order of magnitude in binding affinity, which in turn, generated a 6-fold enhancement of efficacy at the cellular level (Abstract) (Sulea et al., “Application of Assisted Design of Antibody and Protein Therapeutics (ADAPT) improves efficacy of a Clostridium difficile toxin A single-domain antibody," Scientific Reports, 8(260):1-11 (2018) (PTO-892). Hasegawa et al. reports that a single amino acid substitution in the variable region was sufficient to alter the efficiency of biosynthesis and the variant antibody acquired stronger binding affinity to its antigen than the parent (Hasegawa et al., “Single amino acid substitution in LC-CDR1 induces Russell body phenotype that attenuates cellular protein synthesis through elF2a phosphorylation and thereby downregulates IgG secretion despite operational secretory pathway traffic,” MABS, VOL. 9, NO. 5, pp. 854-873 (2017) (PTO-892)). Altshuler teaches that generally, “CDR mutations should not involve residues that can play structural functions (form parts of the domain ‘internal core’, internal salt bridges, hydrogen bonds, etc.).” “Usually these are conservative residues, and any substitution of these residues causes decrease[s] in affinity” (Altshuler et al., “Generation of Recombinant Antibodies and Means for Increasing Their Affinity,” Biochemistry (Moscow), 75(13):1584-1605 (2010) at p. 1600, col. 1, para. 2, lines 1-5 (PTO-892). Accordingly, a person of ordinary skill in the art would have recognized that it was highly unpredictable that any of the CDRs or FRs could be modified to create an unlimited change in amino acids for both the CDRs and FRs of the claimed antibodies, without increasing, eliminating, or in some way altering antigen binding.
Summary of species disclosed in the specification
Applicant’s specification fully discloses one antibody clone, Adrecizumab (SEQ ID NOS: 22 HC)/23(LC); Claim 24), being effective shown by those data shown in Figures 1-7 as follows: the mortality rate over time in patients under Adrecizumab treatment compared to placebo when the treatment was administered between 0 and 10 hours after shock was diagnosed (FIG. 1A) and between 10 and 12.2 hours post shock (FIG. 1B); the changes of the SOFA Score when Adrecizumab treatment was administered within within 10 h after shock diagnosis (FIG. 2A) compared to treatment administered more than 10 h post shock diagnosis (FIG. 2B); the 28-day mortality rate over time in patients under Adrecizumab treatment compared to placebo when the treatment was administered between 0 and 0.344 days (8.3 hours) after ICU admission (FIG. 3A) and between 0.344 days and 29 days after ICU admission (FIG. 3B); the 90-day mortality rate over time in patients under Adrecizumab treatment compared to placebo when the treatment was administered between 0 and 0.344 days (8.3 hours) after ICU admission (FIG. 4A) and between 0.344 days and 29 days after ICU admission (FIG. 4B); the changes of the SOFA Score when Adrecizumab treatment was administered within 0.344 days after ICU admission (FIG. 5A) compared to treatment administered more than 0.344 days post ICU admission (FIG. 5B); the mean fluid balance on day 7 after start of treatment, when Adrecizumab treatment was administered 0.344 days after ICU admission (FIG. 6A) compared to treatment administered more than 0.344 days post ICU admission (FIG. 6B); and the mean fluid balance on day 7 after start of treatment, when Adrecizumab treatment was administered within 10 hours after shock diagnosis (FIG. 7A) compared to treatment administered more than 10 hours after shock diagnosis (FIG. 7B).
Are the disclosed species representative of the claimed genus?
It is asserted that the disclosed species are not representative of the claimed genus because the claims encompass anti-ADM antibodies and variations thereof for any anti-ADM antibody. The genus of all possible anti-ADM antibodies encompassed by the claims would be structurally distinct but unpredictable whether the structure/function correlation was met for binding to ADM much less the treatment effect on the shocked patient.
The disclosed species includes Adrecizumab. Neither the specification nor the prior art provides guidance as to what structural changes can be made to the parent sequences and still predictably arrive at an antibody that binds ADM. The disclosed species therefore does not represent the claimed genus.
Has Applicant provided a common structure sufficient to visualize the genus?
Applicant has not provided a common structure sufficient to visualize the genus of all possible functional variants. While the disclosure provides the amino acid sequences of the HC and LC for Adrecizumab, there is no alignment between these and other ADM binders that might show similarities among their linear structures.
While the prior art contains disclosure as to the structural features of several anti- ADM antibodies, it is unclear what structural features these antibodies need to share in order to maintain binding affinity and stability. Even in 2021, therapeutic antibodies are still not understood well enough to allow researchers to predict with certainty what modifications can be made to a primary antibody sequence such that binding is maintained. “[T]he major test of understanding is whether the changes associated with antibody maturation can be predicted with any reasonable accuracy, and whether there is sufficient information for developing therapeutic antibodies,” Vajda et al., “Progress toward improved understanding of antibody maturation,” Current Opinion in Structural Biology, 67 pp. 226-231 (2021 (PTO 892)) at p. 226, col. 2, lines 20-24.
As recently as 2020, researches were still speculating as to how to reliably identify further putative binders from antibody sequence data, see, e.g., Marks et al., “How repertoire data are changing antibody science,” J. Biol. Chem. 295(29) 9823-9837 (2020 (PTO 892)), acknowledging that “there is a vast amount of the antibody sequence space that remains unknown,” p. 9831, col. 2, para. 2.
Even though the protein sequence of ADM was known in the art, this would not have translated into knowledge of the genus of antibodies that could possibly engage it. Computational and machine learning approaches for sequence-based prediction of paratope-epitope interactions are accumulating, but “it remains unclear whether antibody-antigen binding is predictable” (Akbar et al., Cell Reports 34, 108856, Mar. 16, 2021 at p. 2, col. 2, para. 2 (PTO 892)). The current state of the art continues to work toward finding an effective and efficient prediction tool for reliably assigning antibody structure based on known target epitopes. See e.g., Lo et al., “Conformational epitope matching and prediction based on protein surface spiral features,” BMC Genomics volume 22, Article number: 116 (2021 (PTO 892)) (disclosing new algorithms that calculate physicochemical properties, such as polarity, charge or the secondary structure of residues within the targeted protein sequences, and then applying quantitative matrix analyses or machine-learning algorithms to predict linear and conformational epitopes).
It is asserted that neither the specification nor the state of art at the time of filing disclosed structural features common to the members of the genus for reliably assigning different antibody structures based on sequence data for one antibody clone, Adrecizumab, which would support the premise that the inventors possessed the full scope of the claimed invention.”
The rejection is maintained.
Claim Rejections - 35 USC § 103
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 (i.e., changing from AIA to pre-AIA ) 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.
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, 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.
9. The rejection of Claims Finding Phase II Clinical Trial to Investigate the Safety, Tolerability and Efficacy of ADRECIZUMAB in Patients With Septic Shock and Elevated Adrenomedullin”; posted 2017-03-21; ‘758) is moot for the canceled claims and maintained for the pending claims.
Applicants allege claims 1 and 2 as amended to recite administration of the anti-ADM antibody, ADRECIZUMAB, to occur within 10 hours and 9 hours, respectively, after the occurrence of shock, is what confers unexpected results over the cited art with a surprisingly beneficial therapeutic effect. Figure 1B, example 2 and p. 93 of the specification are relied on to substantiate the allegation.
Response to Arguments
Applicants’ admission of record is that “unexpected results” and “surprisingly beneficial therapeutic effect” are found with ADRECIZUMAB. None of the rejected claims recite the VH/VL CDR1-3 or VH/VL domains that comprise ADRECIZUMAB or functional variants thereof. None of the generic antibodies of the product-by-process step in the method invention are known to yield unexpected results” and “surprisingly beneficial therapeutic effect”.
Applicants comments and the Laterre reference teaching post-shock administration of drugs for “a time window of 12 hours” is a practicality in the industry.
Examples under the decision of KSR, 550 U.S. at 418, 82 USPQ2d at 1396 to support a conclusion of obviousness include
“Obvious to try” – choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success.
Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention- the teaching of within 12 hours is for a finite and limited number of intervals between the onset of shock the administration of an anti-ADM antibody. Herein the claims are not drawn to ADRECIZUMAB, so the POSA would not have been precluded from changing the interval by no less than two to three hours in administering the generic anti-ADM antibody.
The rejection is maintained.
10. The rejection of Claims 2019-06-18; ‘531) is moot for the canceled claims and maintained for the pending claims.
Applicants allege claims 1 and 2 as amended to recite administration of the anti-ADM antibody, ADRECIZUMAB, to occur within 10 hours and 9 hours, respectively, after the occurrence of shock, is what confers unexpected results over the cited art with a surprisingly beneficial therapeutic effect. Figure 1B, example 2 and p. 93 of the specification are relied on to substantiate the allegation.
Response to Arguments
Applicants’ admission of record is that “unexpected results” and “surprisingly beneficial therapeutic effect” are found with ADRECIZUMAB. None of the rejected claims recite the VH/VL CDR1-3 or VH/VL domains that comprise ADRECIZUMAB or functional variants thereof. None of the generic antibodies of the product-by-process step in the method invention are known to yield unexpected results” and “surprisingly beneficial therapeutic effect”.
Applicants comments and the Laterre reference teaching post-shock administration of drugs for “a time window of 12 hours” is a practicality in the industry.
Examples under the decision of KSR, 550 U.S. at 418, 82 USPQ2d at 1396 to support a conclusion of obviousness include
“Obvious to try” – choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success.
Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention- the teaching of within 12 hours is for a finite and limited number of intervals between the onset of shock the administration of an anti-ADM antibody. Herein the claims are not drawn to ADRECIZUMAB, so the POSA would not have been precluded from changing the interval by no less than two to three hours in administering the generic anti-ADM antibody.
The rejection is maintained.
Double Patenting
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.
11. The provisional rejection of Claims 1-25 on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6, 10, 18-19, 22-26, and 28 of copending Application No. 17/801,108 (reference US 20230104578) is moot for the canceled claims and maintained for the pending claims.
Applicants request to “to delay substantively addressing the full scope of distinctions between the current claims and these claims until at least one application's claims are indicated as being allowable” is granted.
Applicants comment that “unexpected results demonstrated by the claims of the current application and discussed above are sufficient to render all of the double patenting rejections moot” is indecipherable. The breadth and scope of the claimed invention, not the claims per se, have not been demonstrated by intrinsic nor extrinsic evidence to substantiate unexpected results for the universe of anti-ADM antibodies that meet the structure/ function requirements.
The rejection is maintained.
12. The provisional rejection of Claims 1-25 on the ground of nonstatutory double patenting as being unpatentable over claims 25-28 of copending Application No. 17/802,799 (reference application no. 20230193348) is moot for the canceled claims and maintained for the pending claims.
Applicants request to “to delay substantively addressing the full scope of distinctions between the current claims and these claims until at least one application's claims are indicated as being allowable” is granted.
Applicants comment that “unexpected results demonstrated by the claims of the current application and discussed above are sufficient to render all of the double patenting rejections moot” is indecipherable. The breadth and scope of the claimed invention, not the claims per se, have not been demonstrated by intrinsic nor extrinsic evidence to substantiate unexpected results for the universe of anti-ADM antibodies that meet the structure/ function requirements.
The rejection is maintained.
13. The provisional rejection of Claims 1-25 on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6, 8, 14, 19-25, and 27 of copending Application No. 19/099,348 (NOT YET TO PUBLISH) is moot for the canceled claims and maintained for the pending claims.
Applicants request to “to delay substantively addressing the full scope of distinctions between the current claims and these claims until at least one application's claims are indicated as being allowable” is granted.
Applicants comment that “unexpected results demonstrated by the claims of the current application and discussed above are sufficient to render all of the double patenting rejections moot” is indecipherable. The breadth and scope of the claimed invention, not the claims per se, have not been demonstrated by intrinsic nor extrinsic evidence to substantiate unexpected results for the universe of anti-ADM antibodies that meet the structure/ function requirements.
The rejection is maintained.
14. The provisional rejection of Claims 1-25 on the ground of nonstatutory double patenting as being unpatentable over the claims to the following family of cases that are drawn to identical VH/CDR1-3 and VLCDR1-3 as well as the HC/LC that comprise the Adrecizumab antibody is moot for the canceled claims and maintained for the pending claims.
Applicants request to “to delay substantively addressing the full scope of distinctions between the current claims and these claims until at least one application's claims are indicated as being allowable” is granted.
Applicants comment that “unexpected results demonstrated by the claims of the current application and discussed above are sufficient to render all of the double patenting rejections moot” is indecipherable. The breadth and scope of the claimed invention, not the claims per se, have not been demonstrated by intrinsic nor extrinsic evidence to substantiate unexpected results for the universe of anti-ADM antibodies that meet the structure/ function requirements.
The rejection is maintained.
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Conclusion
15. No claims are allowed.
16. THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
17. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LYNN A. BRISTOL whose telephone number is (571)272-6883. The examiner can normally be reached Mon-Fri 9 AM-5 PM.
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, Wu Julie can be reached at 571-272-5205. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
LYNN ANNE BRISTOL
Primary Examiner
Art Unit 1643
/LYNN A BRISTOL/Primary Examiner, Art Unit 1643
Prosecution Insights