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
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on February 7, 2025 has been entered.
RESPONSE TO AMENDMENT
Status of Application/Amendments/claims
3. Applicant’s amendment filed February 7, 2025 is acknowledged. Claims 1-11, 16, 18, 22 and 25 are canceled. Claim 33 is amended. Claims 12-15, 17, 19-21, 23-24, 26-34 are pending in this application. Election was made without traverse in the reply filed on 4/11/22.
4. Claims 12-15, 17, 19-21, 23-24 and 26-34 are under examination with respect to Alzheimer-type dementia and anti-PD-1 antibody in this office action.
5. Applicant’s arguments filed on February 7, 2025 have been fully considered but they are not deemed to be persuasive for the reasons set forth below.
Specification
6. The disclosure is objected to because of the following informalities: The use of the term “LEAF(TM)” “Aricept (R)” “Metolose (R)”(p.40), “MILLIPORE” (p. 41), 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Claim Rejections/Objections Withdrawn
7. The rejection of claim 33 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite is withdrawn in response to Applicant’s amendment to the claim.
The rejection of claims 19-21, 23 and 27-34 under 35 U.S.C. 103 as being unpatentable over Eisenbach-Schwartz et al. (US9394365; also published as WO2015136541) in view of Kondo et al. (Curr. Protoc. Immunol., 2010; 89:12.16.1-2.16.12) and Kaneda’263 (US2009/0082263) is withdrawn in response to Applicant’s arguments on p. 17-20 of the response and paragraphs 10-13 and 17-18 of the declaration filed 02/07/2025.
The rejection of claims 12-15, 17, 24 and 26 under 35 U.S.C. 103 as being unpatentable over Kaneda’263 (US2009/0082263) is withdrawn in response to Applicant’s arguments on p. 17-20 of the response and paragraphs 10-13 and 17-18 of the declaration filed 02/07/2025.
Claim Rejections/Objections Maintained
In view of the amendment filed on February 7, 2025, the following rejections are maintained.
Duplicate Claims
8. Applicant is advised that should claim 27 be found allowable, claim 32 will be objected to under 37 CFR 1.75 as being a substantial duplicate thereof; and should claim 33 be found allowable, claim 34 will be objected to under 37 CFR 1.75 as being a substantial duplicate thereof. When two claims in an application are duplicates or else are so close in content that they both cover the same thing, despite a slight difference in wording, it is proper after allowing one claim to object to the other as being a substantial duplicate of the allowed claim. See MPEP § 608.01(m).
New Grounds of Rejection Necessitated by the Amendment
The following rejections are new grounds of rejections necessitated by the amendment filed on February 7, 2025.
Claim Rejections - 35 USC § 112
9. 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.
Claims 12-15, 17, 19-21, 23-24 and 26-34 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 increasing the spontaneous alteration rate in the Y-maze test and increasing the response latency in the passive avoidance test in mice by intraperitoneal administration of LEAF™ purified anti-mouse CD279 anti-PD-1 antibody (from BioLegend) alone or in combination with subcutaneous administration of HVJ-E to the mice followed by injection with beta-amyloid compared to a vehicle control or single administration of HVJ-E or anti-PD-1 antibody or increasing the spontaneous alternation and spontaneous alternation rate in the Y-maze test in mice by intranasal administration of HVJ-E to the mice followed by injection with beta-amyloid compared to a vehicle control, does not reasonably provide enablement for a method for treating cognitive impairment with accumulation of a prionoid, comprising administering a Sendai virus envelope as active ingredient and wherein neither a nucleic acid or an agent is encapsulated in the Sendai virus envelope, or in combination with an immune checkpoint inhibitor that is an anti-PD-1 antibody or ant-PD-L1 antibody with no defined structures, and wherein the cognitive impairment with accumulation of a prionoid is selected from Alzheimer-type dementia, mild cognitive impairment (MCI) and cerebral amyloid angiopathy and wherein the immune checkpoint inhibitor is not encapsulated in the Sendai virus envelope 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.
“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 12-15, 17, 24 and 26 are drawn to a method for treating cognitive impairment with accumulation of a prionoid, the method comprising administering a Sendai virus envelope (HVJ-E) as active ingredient to a patient in need thereof, wherein the prionoid is amyloid beta, wherein neither a nucleic acid nor an agent is encapsulated in the Sendai virus envelope, and wherein the cognitive impairment with accumulation of a prionoid is any one selected from Alzheimer-type dementia, mild cognitive impairment (MCI) and cerebral amyloid angiopathy.
Claims 19-21, 23-24 and 27-34 are drawn to a method for treating cognitive impairment with accumulation of a prionoid, the method comprising administering a Sendai virus envelope (HVJ-E) in combination with an immune checkpoint inhibitor to a patient in need thereof, wherein the prionoid is amyloid beta, wherein the immune checkpoint inhibitor is an anti-PD-1 antibody or an anti-PD-L1 antibody, wherein the cognitive impairment with accumulation of a prionoid is any one selected from Alzheimer-type dementia, mild cognitive impairment (MCI) and cerebral amyloid angiopathy, and wherein the immune checkpoint inhibitor is not encapsulated in the Sendai virus envelope.
The instant invention is based on findings: i based on the Y-maze test (the number of spontaneous alternation, spontaneous alternation rate), the group administered with the combination of anti-PD-1 antibody (i.e. LEAF™ purified anti-mouse CD279 anti-PD-1 antibody from BioLegend) and HVJ-E exhibited a higher spontaneous alteration rate compared to the vehicle control or single administration of HVJ-E or anti-PD-1 antibody (figure 2); ii) based on the passive avoidance test (response latency), the anti-PD-1 antibody group and the HVJ-E+anti-PD-1 antibody combined application group exhibited a significantly higher effect compared to the vehicle control, and the response latency of the HVJ-E+anti-PD-1 antibody combined application group was significantly different from that of the HVJ-E single administration group (figure 3); and iii) based on the Y-maze test, the HVJ-E intranasal administration group exhibited significantly higher spontaneous alternation and spontaneous alternation rate as compared to the vehicle control group.
Based on Applicant’s own admission, the combination of intranasal administration of HVJ-E and intraperitoneal administration of anti-PD-1 antibody was not significantly different from the vehicle control group and the effect of combined application of HVJ-E and the anti-PD-1 antibody was different between intranasal administration and subcutaneous administration (see p.60-61).
Based on the specification, Applicant is enabled for increasing the spontaneous alteration rate in the Y-maze test and increasing the response latency in the passive avoidance test in mice injected with amyloid-beta by subcutaneous administration of HVJ-E, or intranasal administration of HVJ-E or subcutaneous administration of HVJ-E and intraperitoneal administration of a structurally and functionally defined anti-PD-1 antibody obtained from BioLegend as compared to a vehicle control.
However, the specification provides insufficient guidance to enable a skilled artisan to practice the full scope of the claimed invention without undue experimentation because:
i) based on Applicant’s own admission, the combination of intranasal administration of HVJ-E and intraperitoneal administration of anti-PD-1 antibody was not significantly different from the vehicle control group and the effect of combined application of HVJ-E and the anti-PD-1 antibody was different between intranasal administration and subcutaneous administration (see p.60-61).
ii) the specification provides no structural and functional relationship or correlation between the LEAF™ purified anti-mouse CD279 anti-PD-1 antibody (from BioLegend) and other structurally and functionally undefined anti-PD-1 antibodies or anti-PD-L1 antibodies.
Thus, it is unpredictable whether other administration routes would result in the same effects as shown in the examples. It is also unpredictable what other structurally and functionally undefined anti-PD-1 antibodies or anti-PD-L1 antibodies are and whether other structurally and functionally undefined anti-PD-1 antibodies or anti-PD-L1 antibodies can be used in the claimed method because 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 an antibody with the claimed binding activity or features, the antibody must comprise all 6 CDRs with defined sequences or structures in order to maintain the claimed antigen binding specificity and affinity. However, no such information is provided by the specification.
Moreover, even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al. (Proc. Natl. Acad. Sci. USA 1982 Vol. 79: page 1979). Rudikoff et al teach that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. Applicant fails to teach what structures/amino acid sequences are for the claimed anti-PD-1 antibodies or anti-PD-L1. The specification provides no identification of any particular portion of the structure that must be conserved.
In addition, the art recognizes that fully developed animal models for neurodegenerative disease are still lacking especially for Alzheimer’s disease (AD) because the complexity of the disease and deficiency of characterized cognition (see p. 403, abstract. Anger. Neurotoxicology 1991. 12: 403-13, cited previously). Each type of AD animal models only reflects part of pathogenesis of AD. 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, cited previously). 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, cited previously). 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 fails to provide sufficient guidance to enable one of skill in the art to practice the full scope of the invention without undue experimentation because Applicant fails to teach what other cognitive abilities or impairment are. Applicant is enabled for increasing the spontaneous alteration rate in the Y-maze test and increasing the response latency in the passive avoidance test in mice injected with amyloid-beta by subcutaneous administration of HVJ-E, or intranasal administration of HVJ-E or subcutaneous administration of HVJ-E and intraperitoneal administration of a structurally and functionally defined anti-PD-1 antibody obtained from BioLegend as compared to a vehicle control.
However, the animal behavioral tests do not reflect all of the human cognitive abilities. Based on the definition found on the website Answers.com/topic/cognition, cognitive ability is the ability relating to the process of acquiring knowledge by using reasoning, intuition or perception and cognition is a mental processes that are involved in the acquisition and use of knowledge, including sensation, perception, attention, learning, memory, language, thinking, and reasoning (see definition of cognition and cognitive ability on Answers.com/topic/cognition retrieved on March 7, 2007). However, Applicant fails to teach what other cognitive abilities are decreased or impaired in recited Alzheimer-type dementia, mild cognitive impairment (MCI) and cerebral amyloid angiopathy and can be treated by administration of HVJ-E or in combination with a structurally and functionally undefined anti-PD-1 antibody or anti-PD-L1 antibody. A skilled artisan cannot contemplate whether other forms of impairment of cognitive abilities can be treated.
Therefore, in view of the breadth of the claims, the lack of guidance in the specification, the limited working 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 claimed invention as it pertains to a method for treating cognitive impairment by administration of HVJ-E or in combination with a structurally and functionally undefined anti-PD-1 antibody or anti-PD-L1 antibody.
Claim Rejections - 35 USC § 112
10. Claims 19-21, 23 and 27-34 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 19-21, 23 and 27-34 encompass using a genus of anti-PD-1 antibody and a genus of anti-PD-L1 antibody for treating cognitive impairment with accumulation of prionoid that is amyloid b.
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. The specification fails to provide sufficient description as to what structures or sequences for the claimed anti-PD-1 and anti-PD-L1 antibodies or their corresponding heavy chain, light chain, variable regions, or H/LCDRs1-3 are in order to generate antibodies with the claimed binding ability or features and what sequences can be changed or not changed in order to have the claimed binding ability or features.
As an initial matter, Applicant has provided no structures or sequences sufficiently detailed to show that he/she was in possession of the claimed invention as a whole. There was also no known or disclosed correlation between the required function (i.e. binding to PD-1 or PD-L1) and any particular structure or sequence.
Applicant has not disclosed sufficient species for the broad genus of anti-PD-1 antibodies and the broad genus of anti-PD-L1 antibodies.
The specification only discloses intraperitoneal administration of LEAF™ purified anti-mouse CD279 anti-PD-1 antibody (batch number: B203991, BioLegend) alone or in combination with subcutaneous administration of HVJ-E to animals followed by injection with beta-amyloid. The specification discloses that i) based on Y-maze test (spontaneous alternation rate), the group administered with the combination of anti-PD-1 antibody and HVJ-E exhibited a higher spontaneous alteration rate as compared to the vehicle control or single administration of HVJ-E or anti-PD-1 antibody; ii) based on passive avoidance test (response latency), the group administered with the combination of anti-PD-1 antibody and HVJ-E exhibited a higher effect as compared to the vehicle control and significantly different from that of the HVJ-E single administration group; and iii) based on the Y-maze test, the HVJ-E intranasal administration group exhibited significantly higher spontaneous alternation and spontaneous alternation rate as compared to the vehicle control group.
It is noted that based on Applicant’s own admission, the combination of intranasal administration of HVJ-E and intraperitoneal administration of anti-PD-1 antibody was not significantly different from the vehicle control group and the effect of combined application of HVJ-E and the anti-PD-1 antibody was different between intranasal administration and subcutaneous administration (see p.60-61).
However, the specification fails to demonstrate that Applicant is in possession of using the claimed genus of anti-PD-1 antibodies and anti-PD-L1 antibodies recited in instant claims because the claims are not limited to the use of the LEAF™ purified anti-mouse CD279 anti-PD-1 antibody (from BioLegend) set forth above but also encompass other structurally and functionally undefined anti-PD-1 antibodies and anti-PD-L1 antibodies; and the specification provides no structural and functional relationship or correlation between the LEAF™ purified anti-mouse CD279 anti-PD-1 antibody (from BioLegend) and other structurally and functionally undefined anti-PD-1 antibodies or anti-PD-L1 antibodies including those recited on p. 35-36 of the instant specification.
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.
Furthermore, the Fed. Cir.’s decision in Amgen confirmed that post-filing disclosures may be informative in establishing the size of the claimed genus. In this case, there are numerous disclosures of novel antibodies that were published after applicants’ filing date and are not fairly described in it, and their sequences are not taught or suggested by the instant specification, and the instant application provides no structure at all for comparison. The specification’s general reference to anti-PD-1 antibodies or anti-PD-L1 antibodies does not clearly suggest any particular sequences that can be used in order to result in the claimed anti-PD-1 antibodies or anti-PD-L1 antibodies. 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. In order to generate an antibody with the claimed binding activity or features, the antibody must comprise all 6 CDRs with defined sequences or structures in order to maintain the claimed antigen binding specificity and affinity. However, no such information is provided by the specification.
Applicant fails to teach what structures/amino acid sequences are for the claimed anti-PD-1 antibodies or anti-PD-L1. The specification provides no identification of any particular portion of the structure that must be conserved. The instant specification fails to provide sufficient descriptive information, such as definitive structural or functional features of the claimed genus of anti-PD-1 antibodies or anti-PD-L1 antibodies used in the claimed method. There is no description of the conserved regions which are critical to the function of the claimed genus. There is no description of the sites at which variability may be tolerated and there is no information regarding the relation of the structure of other antibodies containing structurally and functionally undefined sequences to the function of the antibodies recited in the claims. Furthermore, the prior art does not provide compensatory structural or correlative teachings sufficient to enable one of skill to isolate and identify what other anti-PD-1 antibodies or anti-PD-L1 antibodies containing structurally and functionally undefined sequences might be. Since the common characteristics/features of other anti-PD-1 antibodies or anti-PD-L1 antibodies containing structurally and functionally undefined sequences 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 using the claimed genus of anti-PD-1 antibodies or anti-PD-L1 antibodies in the claimed method.
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 anti-PD-1 antibodies or anti-PD-L1 antibodies, 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 and Centocor v. Abbott, 636 F.3d1341 (Fed. Cir. 2011) and AbbVie v. Janssen, 759 F.3d 1285 (Fed. Cir.2014). One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483.
Therefore, the claimed method has 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.
Conclusion
11. NO CLAIM IS ALLOWED.
12. 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.
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Chang-Yu Wang
December 16, 2025
/CHANG-YU WANG/Primary Examiner, Art Unit 1675