DETAILED ACTION
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 .
Applicant’s remarks, filed 8/6/2026, are acknowledged and entered into the record. Applicants amended claims 1, 6, 8, 11-12, 15-18, 20 and 22-23, canceled claims 9-10, 13-14, 19, 21 and 27-32, and withdrew claims 33-38, in the remarks of 8/6/2026.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. The present application claims benefit under 35 U.S.C. 119(e) to U.S. Provisional application 63/381,245, filed 10/27/2022.
Election/Restrictions
Applicant’s election without traverse of Group I, encompassing claims 1-26, in the reply filed on 8/6/2026 is acknowledged. Claims 27-38 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Groups II and III, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 8/6/2026. Applicants subsequently canceled claims 9-10, 13-14, 19 and 21 of elected Group I and claims 27-32 of Group II.
Status of Claims
Claims 1-8, 11-12, 15-18, 20, 22-26 and 33-38 are pending, claims 33-38 are withdrawn, claims 1-8, 11-12, 15-18, 20, 22-26 are being examined on the merits.
Claim Objections
Claim 8 is objected to because of the following informalities:
Claim 8, lines 7 and 10 recite a “myc-myc-hexahistag”. There should be a space between the “myc-myc-hexahis” and “tag”, as this is not one word.
Claim 8, lines 9, 12 and 14 recite “less than 1 nM less than 0.5 nM”. There should be a comma, or a conjugate between the two listed alternatives. For example, “less than 1 nM or less than 0.5 nM”.
Claim 8, lines 18 and 20 recite “or less than 1 nM, or less as measured”. The extra “or less” is believed to be a typo.
Claim 8, lines 17 and 19 recite “with a IC50 of with a IC50 of”. There is a typographical duplicate of the same phrase.
Appropriate correction is required.
Claim 20 is objected to because of the following informalities: Claim 20(f) recites “having an amino acid sequence SEQ ID NO: 60”. The claim is missing “of” before “SEQ ID NO: 60”. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
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.
Claims 1-8, 15-18 and 23-26 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 applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Independent claims 1, 6, 15 and 23 recite an anti-ACVR1 antibody, or antigen-binding fragment thereof, wherein the antibody comprises three HCDRs of SEQ ID NO: 46 and three LCDRs of SEQ ID NO: 54. However, the claims do not explicitly define the residues of the VH and/or VL full length sequences which correspond to the claimed CDRs. It is known in the art that various numbering schemes define the CDRs of an antigen binding domain differently. The specifications describe this scenario (specs., pg. 8, para. 0041); whereby it states that individual CDRs of an antibody are each independently determined according to one of the Kabat, Chothia, or AbM numbering schemes, or by structural analysis of the multispecific molecule, whereby the structural analysis identifies residues in the variable regions predicted to make contact with an epitope region (para. 0088). As numerous numbering systems exist, and more schemes may be introduced or modified in the future, whereby each scheme defines the CDR residues differently, it is indefinite to describe the CDRs by “any definition known in the art”; as the types of numbering schemes known in the art is open-ended and subject to change. Importantly, claims 1, 6, 15 and 23 do not claim the antibody by the full VH and VL sequences of SEQ ID NOs: 46 and 54, respectively; if this were the case, the necessary residues of the CDRs are present regardless of which number scheme is applied. Instead, claims 1, 6, 15 and 23 attempt to limit the claimed antibody solely by the CDRs of the full VH and VL sequences; therefore the CDR residues must be explicitly defined. The skilled artisan, attempting to determine the limitations of the claim, must know what residues of the full VH or VL constitute the necessary and required CDRs that meet the limitations of the claims. As different numbering schemes are known in the art, and the different numbering schemes, applied to the various VH and VL sequences listed in the claims, would result in different amino acid sequences for the claimed CDRs, it is unclear what the necessary structural limitations of the antibody of the claims are. The metes and bounds of the claimed structures are unclear, therefore claims 1, 6, 15 and 23 are rejected for indefiniteness. Further, as claims 2-5, 7-8, 16-18 and 24-26 depend from claims 1, 6, 15 or 23, but fail to rectify the indefiniteness issue by defining the claimed structures, claims 2-5, 7-8, 16-18 and 24-26 are also rejected for indefiniteness.
Claims 11, 15-18, 20 and 23 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 applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 11, 15-17, 20 and 23 recite a binding molecule comprising a domain “having an amino acid sequence of SEQ ID NO:”. Use of the terminology “an amino acid sequence” reads on as little as 1-3 amino acids (i.e. a sub-sequence) of any of the claimed sequences. That is, the claims do not require the full length sequence identifiers, it is not close-ended and defined by the recited SEQ ID NOs; rather, that any 1-3 consecutive amino acid residues constitute “an amino acid sequence of”. Thus, for example in claim 11, where the claim recites a HCDR1 domain having an amino acid sequence of SEQ ID NO: 48, it is unclear which amino acid residues of SEQ ID NO: 48 are required, as all that is claimed is an amino acid sequence of SEQ ID NO: 48. This is repeated for the HCDRs 1-3 and LCDRs 1-3 of claims 11 and 20; such that it is unclear what amino acid residues are required from the listed SEQ ID NOs. Similarly, claims 15-17 each recite “an amino acid sequence of SEQ ID NO:” 46 or 54. Thus, it is unclear what sub-sequence of amino acids are required from the listed SEQ ID NOs. As the structure of the CDRs or the VH/VL of the antibody is unclear with regard to how the required amino acid sequences are defined, the metes and bounds of the claims are unclear. Further, the use of “having an amino acid sequence” presents indefiniteness issues. The claimed domains must either “comprise” the recited amino acid sequence, whereby it may also have additional amino acids, or “consist of”, or “consist essentially of”, whereby the claimed sequences cannot have additional amino acids. That is, “comprising” is open-ended and “consisting of” is closed-ended and definite (see MPEP section 2111.03). Using the term “having” does not make clear whether the domains may comprise, or must consist of, the relative amino acid sequences. Thus, claims 11, 15-17, 20 and 23 are rejected for indefiniteness. As claim 18 depends from rejected claim 15, but fails to rectify the indefiniteness issues, claim 18 is also rejected. It is suggested that applicants use definitive language such as “comprising the amino acid sequence of SEQ ID NO”, when referencing the required amino acid sequences that encode the domains of the claimed product.
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.
Claims 15-17 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made, of the specific subject matter claimed. 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. See also MPEP Section 2163.
Claim 15 recites an anti-ACVR1 antibody comprising a VH (i.e. HCVR) comprising three HCDRs 1-3 and a VL (i.e. LCVR) comprising three LCDRs 1-3, wherein the VH comprises an amino acid sequence 90% or 95% identical to SEQ ID NO: 46, or comprising up to 12 amino acid substitutions, and wherein the VL comprises an amino acid sequence 90% or 95% identical to SEQ ID NO: 54, or comprising up to 10 amino acid substitutions. Claim 15 is independent, and while it requires the VH and the VL to comprise any corresponding CDRs 1-3, it does not define the CDR sequences that are required. Rather it defines the VH and VL on the basis of SEQ ID NOs: 46 and 54 respectively, whereby the VH or VL may be 90% identical. Thus, the broadest reasonable interpretation is to a genus of anti-ACVR1 antibodies comprising a VH >90% identical to SEQ ID NO: 46 and a VL >90% identical to SEQ ID NO: 54, and wherein the substitutions may occur within the CDR domains of the VH or VL. Thus, the claim is drawn to a genus of anti-ACVR1 antibodies with unidentified HCDRs and LCDRs. The VH of SEQ ID NO: 46 is 124 amino acids in length; thus allowing for up to 12 amino acid residue substitutions, at any location, with any alternative amino acid. Similarly, the VL of SEQ ID NO: 54 is 107 amino acids in length; thus allowing for up to 10 amino acid residue substitutions, at any location, with any alternative amino acid. Thus, for example, the number of possible combinations of the VH is determined by the formula N x 19A/((N-A)/A), whereby N is the total sequence length, 19 represents the alternative amino acids available for substitution at each residue, and A is the number of residues that may be substituted. Thus, the scope of the VH, alone, encompasses 29 x 1015 alternative variants. It is clear that the claims encompass a vast number of alternative embodiments, comprising a sub-genus of either the VH of SEQ ID NO: 46 or the VH of SEQ ID NO: 54, with no guidance as to which residues may be substituted, or with which amino acids, and wherein the substitutions may occur anywhere within any of the CDRs of each variable domain, such that the sub-genus of variant embodiments comprise unidentified CDR sequences.
In support of the claimed genus of variants, the specifications disclose 3 anti-ACVR1 antibodies, REGN 5166, REGN 5167 and REGN 5168. REGN 5168 is the species comprising the VH of SEQ ID NO: 46 and the VL of SEQ ID NO: 54. The VH of REGN 5166 (SEQ ID NO: 14) is only 60% similar in sequence to the VH of SEQ ID NO: 46, comprising 47 different amino acid residues. The VH of REGN 5167 is only 48% similar in sequence to the VH of SEQ ID NO: 46, comprising 81 different amino acid residues. Thus, when looking at the VH alone, neither REGN 5166 or 5167 are within the scope of the genus of variants of claim 15; neither species teaches a common structure to SEQ ID NO: 46, or where specific residues may be substituted. Thus, the specifications provide no guidance as to which residues may be substituted, or with which alternative amino acids. When determining representative examples in the art, it is important to consider whether there is evidence of a singular shared structural feature which imparts the defining property of the claimed genus, and which would necessarily be present in every species of the claimed genus. In this case, no CDRs are defined which are necessarily present in all variant species. Neither REGN 5166 or 5167 share a common structural feature to REGN 5168, which comprises the VH of SEQ ID NO: 46 and the VL of SEQ ID NO: 54. Applicants do not reduce to practice any embodiments of the variants of the claimed sequences, having 90-99% sequence identity in either the VH or the VL to instant SEQ ID NOs: 46 and 54, respectively.
It is known in the art that the antigen binding domain of an antibody requires the 6 complementarity determining regions (CDR) of the heavy and light chains, whereby the 3 CDRs of the heavy chain and the 3 CDRs of the light chain are structurally inter-dependent in forming the unique binding pocket of the antibody paratope region; and thus the CDRs constitute critical aspects of the antibody paratope and ultimately impart the paratope-epitope binding functionality with regard to specificity and affinity (for review see MacCallum et al., 1996). However, the structure-to-function correlation continues to be highly unpredictable. For example, Chen et al., (1992) teaches that a single amino acid substitution in the VH CDR2 of PC-specific T15 antibody could increase, decrease or ablate binding the target antigen (abstract, Fig. 3), and this occurred in an unpredictable manner based on which residue was mutated. Similarly, a single point mutation in the heavy chain CDR3 region of the high affinity anti-VEGF antibody G6.31, could in some cases enhance, or otherwise completely ablate binding to the target antigen, and this also occurred in an unpredictable manner (Koenig et al., PNAS, 2017). That is, only screening each mutation individually provided insight as to the resulting changes in functionality. In some cases this extends even beyond the CDRs. Within the framework regions, Koenig et al. (PNAS, 2017) teaches that various amino acid point mutations can increase or decrease binding or neutralization capacity. Some amino acid residues are more tolerant to substitution, while other “conserved” residues are less tolerant, such that a single amino acid substitution may defunctionalize the antibody (pg. E487, Fig. 1). Thus, while antibodies share certain characteristics such as Fc regions or hinge regions, these regions are not correlated with the binding function of the antibody. Conversely, the hyper-variable regions, comprising the complementary set of 6 CDRs, are well established in the art as the portion of the binding regions which impart the specificity of the antibody; and yet, there is no way to look at an amino acid sequence and envision, a priori, whether the combination of six CDRs will bind a particular epitope, even when the CDRs are highly related, without teachings of the basic shared amino acid residues that are sufficient to impart functional binding across all variants. Further, even when provided with several related antibodies that bind the desired target, this does not represent the astronomical and potentially unknowable breadth of all possible amino acid sequences which will result in the desired binding properties. This is exemplified by the Court decision in Abbvie (Abbvie v Janssen 759 F.3d 1285 (Fed. Cir. 2014)), where Abbvie developed over 200 antibodies that shared 99.5% identity in the variable regions (pg. 7) and which bound the target, but in no way allowed one to envisage the unique structure of Centocor’s antibodies which bound the same target but shared only 50% sequence similarity (see table on pg. 11). Thus, when claiming a genus of antibodies based on their binding to a common target, the representative examples must cover the full scope of structural variabilities which encompass all species variants that would bind the target.
Moreover, the decision arrived at in Amgen v. Sanofi, 872, F.3d 1367 (Fed. Cir. 2017) supports expanded analysis of whether a claim drawn to an antibody being specific for an epitope, even a specific epitope, permits an applicant to pursue all possible antibodies that are capable of being produced against such an epitope. That is, “disclosure of an antigen fully characterized by its structure, formula or physical properties does not, without more, provide adequate written description of an antibody claimed by its binding affinity to that antigen” (Amgen v. Sanofi, 872, F.3d 1367 (Fed. Cir. 2014)).
Section 2163(II)(A)(3)(a)(ii) of the MPEP states that the written description for a claimed genus may be satisfied through either a) a representative number of species, or b) disclosed correlation between function and structure. Here the applicants do not provide any variants of the selected species, in which mutations were made, which were reduced to practice; nor do they identify the shared structural properties of the CDR residues that would define the genus beyond the desired functionality. Currently the essential property of binding the extracellular domain of ACVR1 is imparted by the single, specific set of CDR sequences that have been reduced to practice. Specifically, the physical features (or amino acid residues encoding said features) which impart the property of binding the same epitope of ACVR1 should be disclosed. Further, a description of the type and number of amino acid residue substitutions that may be made at such identified positions within the sequence, that result in “at least 90%” sequence identity to a selected sequence, would be essential in determining the degree of variability that may be allotted in total sequence identity. This lack of definition complicates the determination of the boundaries of the claimed genus with regard to which, as of yet unidentified, species variants (antibodies with a VH or a VL domain which is at least 90% to instant SEQ ID NOs: 46 and 54, respectively) would be anticipated, a priori, by one skilled in the art, to fall within the scope of the claims. Without the identification of the necessary shared structural properties of all species variants that fall within the scope of the genus, it may be that antibody species with < 90% sequence identity (such as REGN 5166 or 5167) would still bind ACVR1, or conversely, that antibodies with > 90% sequence identity would not bind ACVR1.
In view of this uncertainty and the lack of a representative number of examples of the claimed genus, claim 15 is rejected for lack of adequate written description support.
Claims 16-17 are also rejected as they are dependent on rejected claim 15 but fail to rectify the issue of indefiniteness. Specifically, claims 16-17 limit the species variants to those comprising either a VH with 100% sequence identity to SEQ ID NO: 46 or a VL with 100% sequence identity to SEQ ID NO: 54, but not both. Thus, each of claims 16-17 encompass a second variable domain which may comprise a genus of alternative domains, which have not been described. As the 6 corresponding CDRs of the VH and the VL are required to impart the binding specificity and affinity of the anti-ACVR1 antibodies, and claims 16-17 leave one of the VH or VL as undefined with respect to the CDRs, the claims lack descriptive support for possession of a genus of variants which will maintain binding to ACVR1. Thus, claims 16-17 are also rejected for lack of descriptive support. Claim 18 resolves the issue of unidentified substitutions within the CDRs, as no substitutions are allowed, but fails to define the requisite CDRs to which the antibody of claim 15 is limited; thus claim 18 remains rejected for indefiniteness under U.S.C. 35 112(b), as described above.
Claim Rejections - 35 USC § 112
Claims 24-25 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made, of the specific subject matter claimed. 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. See also MPEP Section 2163.
Claims 24-25 are rejected as lacking adequate descriptive support for possession of a genus of antibodies or antigen-binding fragments that i) compete for binding to ACVR1 with the antibody of claim 1, or ii) binds to the same epitope (of human ACVR1) as the antibody or antigen-binding fragment thereof of claim 1. In support of the claimed genus, the specifications disclose the antibodies REGN 5166 or 5167. Neither REGN 5166 or 5167 share structural similarity with the claimed antibody (REGN 5168 of claim 1) of the invention.
The art of antibody structure, regarding the structure/function relationship which imparts the target epitope specificity and binding affinity of any particular antibody species, is described above. Moreover, the decision arrived at in Amgen v. Sanofi, 872, F.3d 1367 (Fed. Cir. 2017) supports expanded analysis of whether a claim drawn to an antibody being specific for an epitope, even a specific epitope, permits an applicant to pursue all possible antibodies that are capable of being produced against such an epitope. Specifically, “disclosure of an antigen fully characterized by its structure, formula or physical properties does not, without more, provide adequate written description of an antibody claimed by its binding affinity to that antigen,” (Amgen v Sanofi, 872, F.3d 1367 (Fed. Cir. 2017)). Thus emphasizing that claimed antibodies must be described by their structure, which is congruent with their claimed function; and when claiming a genus of variants, there must be a shared structural feature which imparts the desired functional properties and which is necessarily shared across all variant species. Presently, the claimed genus of antibodies (of claims 24-25) are only defined by functional properties, but no specific structure is recited. Specifically, the physical features (or amino acid residues presenting said features) which impart the property of binding the same ACVR1 epitope should be disclosed. Further, a description of the type and number of amino acid residue substitutions that may be made at such identified positions within the sequence would be essential in determining the degree of variability that may be allotted in structural identity across variant species of the “competing” variant anti-ACVR1 antibodies. This lack of definition complicates the determination of the boundaries of the claimed genus with regard to which, as of yet unidentified, species variants would be anticipated by one skilled in the art to fall within the scope of the claims. Without identification of the necessary shared structural properties of all species variants that fall within the scope of the genus, it is difficult to determine that the applicants have possession of an adequate representative number of species to support the scope of the claimed genus. Instead, applicants seem to be claiming conceptual antibodies, that have yet to be invented, based solely on desired functionality, without providing any guidance as to the basic shared structural features that are necessary for one of skill in the art to produce variants which maintain said functionality.
“The purpose of the written description requirement is to ‘ensure that the scope of the
right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s
contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli
Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D.
Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description
requirement, the 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. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir.
1991). See also MPEP 2163.04. Otherwise, the “claims merely recite a description of the
problem to be solved while claiming all solutions to it and … cover any compound later actually
invented and determined to fall within the claim’s functional boundaries- leaving it to the
pharmaceutical industry to complete an unfinished invention.” Ariad Pharmaceuticals, Inc. v. Eli
Lilly and Co., 598 F.3d 1336, 1353 (Fed. Cir. 2010).
Applicants have not described a representative number of species of the claimed invention of a genus of alternative antibodies which bind to the same epitope, or compete for binding with, the anti-ACVR1 antibody of claim 1. Applicants have not described the necessary structure of any of the claimed “competing” antibodies. Thus applicants fail to show they had possession of the claimed genus. Claims 24-25 are rejected for lack of adequate written description.
Allowable Subject Matter
Anti-ACVR1 antibodies comprising the HCDRs 1-3 of instant SEQ ID NOs: 48, 50 and 52, respectively, and the LCDRs 1-3 of instant SEQ ID NOs: 56, 58 and 60, respectively, have been searched and are free of the prior art. Similarly, an anti-ACVR1 antibody comprising the VH and VL domains of instant SEQ ID NOs: 46 and 54, respectively, is also free of the prior art.
Claims 12 and 22, which each recite wherein the antibody comprises a VH and VL comprising the sequences of instant SEQ ID NOs: 46 and 54, with 100% sequence identity, are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Conclusion
No claims are allowed. Claims 1-8, 11, 15-18, 20, 23-26 are rejected; claims 12 and 22 are objected to.
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/JAMES RYLAND MELCHIOR/Examiner, Art Unit 1644
/NELSON B MOSELEY II/Primary Examiner, Art Unit 1642
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