DETAILED ACTION
Notice of Pre-AIA or AIA Status
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. The amendments and remarks filed 4/14/2026 are acknowledged. Claims 1-7, 9-16, 21 and 23 are amended. Claims 1-16, 21, 23 and 31-32 are pending and under examination.
Withdrawn Rejections
3. The rejection of claims of 1, 2, 4 and 23 for under 35 U.S.C 112(b) as set forth at page 3 of the previous Office action (mailed 01/14/2025) is withdrawn in view of the amended claims
(received 04/14/2026).
4. The rejection of claims 1, and 6 under 35 U.S.C 112(a) regarding written description as set forth at pp. 3-11 of the previous Office action (mailed 01/14/2025) is withdrawn in view of the amended claims (received 04/14/2026).
5. The rejection of claims 1-7, 9-16, 21, 23, 31, and 32 are rejected under 35 U.S.C § 102(a)(1) as being anticipated by Rosenthal, et al. (US Patent No. US 10,316,081 B2, hereinafter "Rosenthal") is withdrawn as arguments have been fully considered and are persuasive
6. The rejection of claims 1-16, 21, 23, 31, and 32 rejected under 35 U.S.C § 102(a)(1) as being anticipated by Annexon, et al. (Annexon Biosciences Reports Top-line Phase lb Results for Novel Clq Inhibitor ANX007 in Glaucoma available Oct 9, 2019), is withdrawn as arguments have been fully considered and are persuasive. Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground(s) of rejection of Claims 1-16, 21, 23, and 31-32 are rejected under 35 U.S.C 103 as being obvious over Annexon, et al. (Annexon Biosciences Reports Top-line Phase 1b Results for Novel C1q Inhibitor ANX007 in Glaucoma. (https://ir.annexonbio.com/node/6131/pdf available Oct 9, 2019).
7. The rejection of claims 1-16, 21, 23, 31, and 32 rejected under 35 U.S.C § 102(a)(1) as allegedly anticipated by Yednock, et al. (Patent Application Publication No: US 2017/0152309 A1), is withdrawn as arguments have been fully considered and are persuasive. Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground(s) of rejection of claims 1-16, 21, 23, 31, and 32 rejected under 35 U.S.C § 103 as being obvious over Yednock, et al. (Patent Application Publication No: US 2017/0152309 A1)
Maintained Rejections
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
8. Claims 2 and 4 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends
The rejection is maintained for the reason of record (page 11, Office action mailed 14 January 2026) and for the reasons discussed below. For convenience, the rejection is repeated herein:
Claim 1 recites the CDR’s for the light chain and heavy chain of the antibody. Claim 2 and 4 further recite heavy and light chains, however, the light and heavy chains are at least about 95% homologous. Having about 95% homologous amino acid sequence of the heavy and light chain is broader than what is recited in claim 1 and fails to further limit the claim. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Applicant’s Arguments
Applicant’s arguments (pp. 5-6, remarked received 14 April 2026) have been fully considered but are not found to be persuasive for the following reasons.
Applicant argues that the claim 1 defined the antibody by the required six CDR sequences. Applicant argues that claim 2 and 4 depend from claim 1 and do not broaden the claim, rather specify a further limitation wherein the light chain variable domain and heavy chain variable domain comprise an amino acid sequence with at least 95% sequence identify of the recited amino acid sequence.
Response to Arguments
This has been fully considered but is not found to be persuasive for the following reasons. Claims 2 and 4 broadly encompass the anti-C1q antibody light and heavy chain variable domain comprising an amino acid sequence with at least 95% sequence identity to SEQ ID NO: 4, 35-38 (light chain) and SEQ ID NO: 8 and 31-34 (heavy chain). This would represent a large pool of variant polypeptides that must have similar functional activity. A variance of 5%, for example, in the polypeptide set forth in SEQ ID NO: 4 that is 107 amino acids in length translates into 5 residues that may be added, deleted, substituted, or otherwise mutated anywhere throughout the entire length of the 107 residue amino acid polypeptide. There is no limit in the claims, as written, that the variance be contiguous. Moreover, there is no limitation stating that the substitution, for example, be a conservative substitution. As a result, there are potentially thousands of variant permutations that could be made and still maintain a variance of 95%. Hence, claim 2 and 4 do not further limit claim 1. Accordingly, the rejection is maintained.
New Rejections
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
9. Claims 2 and 4 is 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 MPEP states that the purpose of the written description requirement is to ensure that the inventor had possession, as of the filing date of the application, of the specific subject matter later claimed. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention.”
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, disclosure of drawings, or by disclosure of relevant identifying characteristics, for example, 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, sufficient to show the Applicants were in possession of the claimed genus.
The instant claims are drawn to the method of claim 1, wherein the antibody or antigen-binding fragment thereof comprises a light chain variable domain comprising an amino acid sequence with at least 95% sequence identity to the amino acid sequence selected from any one of SEQ ID NO: 4 and 35-38; wherein the antibody or antigen-binding fragment thereof comprises a heavy chain variable domain comprising an amino acid sequence with at least 95% sequence identity to the amino acid sequence selected from any one of SEQ ID NO: 8 and 31-34.
The specification teaches in some embodiments, the antibody comprises a light chain variable domain comprising an amino acid sequence with at least about 95% homology to the amino acid sequence selected from SEQ ID NO: 4 and 35-38. The specification further teaches in some embodiments, the antibody comprises a heavy chain variable domain comprising an amino acid sequence with at least about 95% homology to the amino acid sequence selected from SEQ ID NO: 8 and 31-34.
The claims encompass a genus of anti-C1q antibody that are not adequately described. Although the claims are inclusive of the anti-C1q antibody comprising the amino acid sequence of SEQ ID NO: 4, 8, and 31-38, the claims also broadly encompass chimeric molecule complexes comprising variants of SEQ ID NO: 4, 8, and 31-38 that are at least 95% identical to the full-length amino acid sequence. This would represent a large pool of variant polypeptides that must have similar functional activity. A variance of 5%, for example, in the polypeptide set forth in SEQ ID NO: 31 that is 121 amino acids in length translates into 6 residues that may be added, deleted, substituted, or otherwise mutated anywhere throughout the entire length of the 121 residue amino acid polypeptide. There is no limit in the claims, as written, that the variance be contiguous. Moreover, there is no limitation stating that the substitution, for example, be a conservative substitution. As a result, there are potentially thousands of variant permutations that could be made and still maintain a variance of 95%. Applicants have not described which domain or portions of SEQ ID NO: 4, 8, and 31-38 that are critical to the function of the protein. The specification provides limited guidance regarding which amino acids can be modified in the genus of polypeptides, while maintaining any given function. Therefore, these structures (i.e., sequence variants and fragments) are claimed only be their functional characteristics and the specification fails to provide sufficient correlation between the claimed functional characteristics and the necessary structural components (i.e., critical domains within the sequences).
Accordingly, the specification does not define any structural features commonly possessed by the members of the genus, because, while the description of an ability of the claimed protein may generically describe the protein’s function, it does not describe the protein itself. A definition by function does not suffice to define the genu because it is only an indication of what the protein does, rather than what it is; therefore, it is only a definition of a useful result rather than a definition of what achieves the result. In addition, because the genus of chimeric molecule complexes is highly variable (i.e., each complex would necessarily have a unique structure, See MPEP 2434), the generic description of the heterodimer is insufficient to describe the genus, Further, given the highly diverse nature of proteins, even one of skill in the art cannot envision the structure of the chimeric molecule complex only by knowing its functional characteristics. Thus, the specification does not provide substantive evidence for possession of this large and variable genus, encompassing a potentially massive number of chimeric molecule complexes claimed only by a functional characteristic and/or partial structure.
A biomolecule sequence described only by a functional characteristic, without any known or disclosed correlation between that function and the structure of the sequence, normally is not sufficient identifying characteristics for written description purposes, even when accompanied by a method of obtaining the agent. The specification does not adequately describe the correlation between the chemical structure and function of the genus, such as structural domains or motifs that are essential and distinguish members of the genus from those excluded. Thus, the genus of antibodies has no correlation between their structure and function.
Furthermore, Applicants have not shown possession of a representative number of species that have the claimed function(s). The claims generically recite anti-C1q antibody. While the specification clearly sets forth a correlation between the anti-C1q antibody comprising SEQ ID NO: 4, 8, and 31-38, and the functions of treating ocular disease, this correlation does not appear to be clearly present in the breadth of the claims. As noted above, the claims are not limited to the disclosed anti-C1q antibody comprising SEQ ID NO: 4, 8, and 31-38, and broadly encompass anti-C1q antibody comprising variants and fragments of SEQ ID NO: 4, 8, and 31-38. Thus, the genus has substantial variation because of the numerous alternatives and combinations permitted. There is no description of the structure common to the members of the genus such that one of skill in the art can visualize or recognize the members of the genus. Therefore, only a single species has been described and this is not considered to be representative of the breadth of the genus.
MPEP §2163 states that for a generic claim, the genus can be adequately described if the disclosure presents a sufficient number of representative species that encompass the genus. If the genus has a substantial variance (as in the instant case), the disclosure must describe a sufficient variety of species to reflect the variation within that genus. Although the MPEP does not define what constitutes a sufficient number of representative species, the courts have indicated what does not constitute a representative number to adequately describe a broad genus. The courts determined that the disclosure of two chemical compounds within a subgenus did not describe that subgenus (e.g., see In re Gostelli, 872, F. 2d at 1012, 10 USPQ2d at 1618).
Further, the disclosure of only one or two species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure “indicates that the patentee has invented species sufficient to constitute the genu[us].” See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) ("[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated.") (MPEP 2163). “A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when… the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.” In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004).
Accordingly, the specification also does not provide adequate written description to identify the broad genus of the claimed, claimed only be a function characteristic(s) and not structures per se, because inter alia, it does not describe a sufficient number and/or a sufficient variety of representative species to reflect the breadth and variation within the claimed genus. Consequently, based on the lack of information within the specification, there is evidence that a representative number and a representative variety of the numerous heterodimers had not yet been identified and thus, the specification represents little more than a wish for possession. Therefore, one of skill in the art would not conclude that Applicant was in possession of the broad and highly variable genus of heterodimers claimed only by a partial structure and functional characteristic(s).
Vas-Cath Inc. v. Mahurkar, 19 U5PQ2d 1111, makes clear that
"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.)
With the exception of an anti-C1q antibody comprising SEQ ID NO: 4, 8, and 31-38, the skilled artisan cannot envision the detailed chemical structure of the encompassed polypeptides, 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 for isolating it. The nucleic acid and/or protein itself is required. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481,1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence.
University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404. 1405 held that:
...To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines Inc., 107 F.3d 1565,1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) (" [T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2d 1966.
In Ariad Pharrns., Inc. v. Eh Lilly & Co., 598 F.3d 1336,1351 (Fed. Cir. 2010), the court held that a “sufficient description of a genus ... requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can 'visualize or recognize’ the members of the genus." Ariad, 598 F.Bd at 1350. “[A]n adequate written description requires a precise definition, such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other materials,” Id. Although “functional claim language can meet the written description requirement when the art has established a correlation between structure and function," "merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genu and showing that one has invented a genus and not just a species.”Id.
Furthermore, regardless whether a compound is claimed per se or a method is claimed that entails the use of the compound, the inventor cannot lay claim to that subject matter unless he can provide a description of the compound sufficient to distinguish infringing compounds from non-infringing compounds, or infringing methods from non-infringing methods. Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920-23, 69 USPQ2d 1886, 1890-93 (Fed. Cir. 2004).
Protein chemistry is probably one of the most unpredictable areas of biotechnology. Consequently, the effects of sequence dissimilarities upon protein structure and function cannot be predicted. Bowie et al. (Science, 1990, 247:1306-1310) teach that an amino acid sequence encodes a message that determines the shape and function of a protein and that it is the ability of these proteins to fold into unique three-dimensional structures that allows them to function and carry out the instructions of the genome and further teaches that the problem of predicting protein structure from sequence data and in turn utilizing predicted structural determinations to ascertain functional aspects of the protein is extremely complex (column 1, page 1306). Bowie et al. further teach that while it is known that many amino acid substitutions are possible in any given protein, the position within the protein's sequence where such amino acid substitutions can be made with a reasonable expectation of maintaining function are limited. Certain positions in the sequence are critical to the three dimensional structure/function relationship and these regions can tolerate only conservative substitutions or no substitutions at all (column 2, page 1306). The sensitivity of proteins to alterations of even a single amino acid in a sequence are exemplified by Burgess et al. (J. Cell Biol. 111:2129-2138,1990) who teach that replacement of a single lysine residue at position 118 of acidic fibroblast growth factor by glutamic acid led to the substantial loss of heparin binding, receptor binding and biological activity of the protein and by Lazar et al. (Mol. Cell. Biol., 8:1247-1252,1988) who teach that in transforming growth factor alpha, replacement of aspartic acid at position 47 with alanine or asparagine did not affect biological activity while replacement with serine or glutamic acid sharply reduced the biological activity of the mitogen. These references demonstrate that even a single amino acid substitution will often dramatically affect the biological activity and characteristics of a protein.
Additionally, Whisstock et al. (Quarterly Reviews in Biophysics. 36(3):307-340, 2007) teach that the prediction of protein function from sequence and structure is a difficult problem (See abstract). Although many families of proteins contain homologues with the same function, homologous proteins often have different functions as the sequences progressively diverge (See page 309). Whisstock et al. teach that assigning a function to an amino acid sequence based upon similarity becomes significantly more complex as the similarity between the sequence and a putative homologue falls. Whisstock et al. teach that while it is hopeful that similar proteins will share similar functions, substitution of a single, critically placed amino acid in an active-site may be sufficient to alter a protein’s role fundamentally (See pages 321-323). Given not only the teachings of Bowie et al., Lazar et al. and Burgess et al. but also the limitations and pitfalls of assigning a function to an amino acid sequence based upon similarity as taught by Whisstock, the claimed proteins could not be predicted. Therefore, the state of the art supports that even the skilled artisan requires guidance on the critical structures of the agent per se and thereby does not provide adequate written description support for which structural features of any given polypeptide would predictably retain their functional activities.
Accordingly, one of skill in the art would conclude that the claimed invention encompasses a plurality of polypeptides defined solely in terms of their function that may not have the biological functions recited in the claims. Based on the teachings of the instant specification and the prior art, one of skill in the art would not conclude that Applicant was in possession of the claimed genus of agents.
While “examples explicitly covering the full scope of the claim language” typically will not be required, a sufficient number of representative species must be included to “demonstrate that the patentee possessed the full scope of the [claimed] invention.” Lizardtech v. Earth Resource Mapping, Inc., 424 F.3d 1336, 1345, 76 USPQ2d 1724, 1732 (Fed. Cir. 2005).
In the absence of sufficient recitation of distinguishing characteristics, the specification does not provide adequate written description of the claimed genus. One of skill in the art would not recognize from the disclosure that the applicant was in possession of the genus. Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features (see, Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 927, 69 USPQ2d 1886, 1895 (Fed. Cir. 2004); accord Ex Parte Kubin, 2007-0819, BPAI 31 May 2007, opinion at p. 16, paragraph 1). 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).
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).
Claim Rejections - 35 USC § 103
9. In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
10. Claims 1-16, 21, 23, and 31-32 are rejected under 35 U.S.C 103 as being obvious over Annexon, et al. (Annexon Biosciences Reports Top-line Phase 1b Results for Novel C1q Inhibitor ANX007 in Glaucoma. (https://ir.annexonbio.com/node/6131/pdf available Oct 9, 2019).
The instant claims are drawn to a method of treating an ocular disease in a human patient, comprising administering to the patient a composition comprising about 1 mg to about 10 mg of an anti-C1q antibody via intravitreal injection.
Annexon, et al. teach ANX007, which is an monoclonal antibody antigen-binding fragment (Fab) which inhibits C1q formulated for intravitreal administration to treat glaucoma and geographic atrophy which is well-tolerated at all dose levels for at least 4 weeks, as recited in instant claims 1, 6, 7, 23, 31 and 32.
Regarding instant claims 1, 2, 3, 4, 5, and 8 that recite “wherein the antibody comprises a light chain variable domain comprising an HVR-L1 having the amino acid sequence of SEQ ID NO: 5, an HVR-L2 having the amino acid of SEQ ID NO: 6, and an HVR-L3 having the amino acid of SEQ ID NO: 7; and a heavy chain variable domain comprising an HVR-H1 having the amino acid sequence of SEQ ID NO: 9, an HVR-H2 having the amino acid of SEQ ID NO: 10, and an HVR-H3 having the amino acid of SEQ ID NO: 11 (instant claim 1)”, “wherein the antibody comprises a light chain variable domain comprising an amino acid sequence with at least about 95% homology to the amino acid sequence selected from SEQ ID NO: 4 and 35-38 and wherein the light chain variable domain comprises an HVR-L1 having the amino acid sequence of SEQ ID NO: 5, an HVR-L2 having the amino acid of SEQ ID NO: 6, and an HVR-L3 having the amino acid of SEQ ID NO: 7 (instant claim 2)”, “wherein the light chain variable domain comprising an amino acid sequence selected from SEQ ID NO: 4 and 35-38 (instant claim 3)”, “wherein the antibody comprises a heavy chain variable domain comprising an amino acid sequence with at least about 95% homology to the amino acid sequence selected from SEQ ID NO: 8 and 31-34 and wherein the heavy chain variable domain comprises an HVR-H1 having the amino acid sequence of SEQ ID NO: 9, an HVR-H2 having the amino acid of SEQ ID NO: 10, and an HVR-H3 having the amino acid of SEQ ID NO: 11 (instant claim 4)”, “wherein the heavy chain variable domain comprising an amino acid sequence selected from SEQ ID NO: 8 and 31-34 (instant claim 5)”, and “wherein the Fab fragment comprises a heavy chain Fab fragment of SEQ ID NO: 39 and a light chain Fab fragment of SEQ ID NO: 40 (instant claim 8)”, such structures would be inherent properties of ANX007, because Annexon, et al. teach administering the same antibody (ANX007), at multiple dosages to the same patient population and therefore, the prior method would necessarily possess the same results claimed by the Applicant. Annexon, et al. teach the monoclonal antibody antigen-biding fragment anti-C1q that accumulates on photoreceptor cell synapses with normal age or disease that may lead to aberrant synapse removal and neuronal loss in disease. Annexon, et al. further teach ANX007 is designed to potently bind and inhibit C1q and all downstream components of the classical complement cascade, including C3 and C5, but to not interfere with the normal function of C3 and C5 as part of other complement pathways. Instant specification teaches the anti-C1q antibody disclosed are potent inhibitors of C1q and recognize complement factor C1q and/or C1q in the C1 complex of the classical complement activation pathway (page 34, line 15). Instant specification further teaches the antibody recognizes C1q, showing no binding to the other complement components (C3b and C5) (page 6, line 15). It is well settled that “[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer." Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable (emphasis added); see In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977). In In re Crish, 393 F.3d 1253, 1258, 73 USPQ2d 1364, 1368. Additionally, "Products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present.
Based on the application disclosure on page 56, line 9, optimization is reasonable of dosages and dosage administration as different dosages are recited in instant claims 1, 9-16, 21 and 23. The time of dosage and measuring clinical endpoints can clearly be a result effective parameter that a person having ordinary skill in the art would routinely optimize. Optimization of parameters is a routine practice that would be obvious for a person of ordinary skill in the art to employ. It would have been customary for an artisan of ordinary skill to determine the optimal amount of each ingredient, i.e., the dosage and dosing regimen, needed to achieve the desired results. The principle of law states from MPEP §§ 2144.05: "The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages," (see In re Peterson, 315 F.3d at 1330, 65 USPQ2d at 1382). Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation," (See In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955)).
Applicant’s arguments
Applicant’s arguments (page 6, remarks received 04/14/2026) have been fully considered but are not found persuasive for the following reasons.
Applicant argues that the specific dosage of 1 mg to 10 mg of anti-C1q Fab fragment is not disclosed.
Response to Arguments
This has been fully considered but is not found to be persuasive for the follow reasons. The rejection has been adjusted to be under the statutory basis of 35 U.S.C 103, to which fully supports the rejection under optimization of parameters as stated in the about new rejection.
11. Claims 1-16, 21, 23, and 31-32 are rejected under rejected under 35 U.S.C 103 as being anticipated over Yednock, et al. (Patient Application Publication No: US 2017/0152309 A1, issued 06/1/2017).
Yednock, et al. teach an antibody fragment that binds to C1q, with the heavy chain variable domain comprising SEQ ID NO:1 (claim 1), that is 100% duplicate with the instant heavy variable domain comprising instant SEQ ID NO: 9, 10, and 11. Yednock, et al. teach the antibody fragment that binds to C1q, with the light chain variable domain comprising SEQ ID NO: 2 (paragraph 18), that is 100% duplicate with the instant light variable domain comprising instant SEQ ID NO: 5, 6, and 7. Yednock, et al. further teach a method of treating or preventing a disease by comprising administering antibody Fab fragment (claim 37) via an intravitreal administration (paragraph 222) , and such disease are defined as glaucoma, age-related macular degeneration (AMD), and geographic atrophy (paragraph 29). This recites the limitations of instant claims 1, 6, 7, 31 and 32.
Yednock, et al. teach an antibody fragment that binds to C1q, with the heavy chain variable domain comprising SEQ ID NO:1 (claim 1), that is 100% duplicate with the instant heavy variable domain comprising instant SEQ ID NO: 9, 10, and 11 of instant claim 1.
Yednock, et al. SEQ ID NO: 1 is 100% duplicate with instant SEQ ID NO: 9:
Query Match 100.0%; Score 67; Length 229;
Best Local Similarity 100.0%;
Matches 10; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GYHFTSYWMH 10
||||||||||
Db 26 GYHFTSYWMH 35
Yednock, et al. SEQ ID NO: 1 is 100% duplicate with instant SEQ ID NO: 10:
Query Match 100.0%; Score 91; Length 229;
Best Local Similarity 100.0%;
Matches 17; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 VIHPNSGSINYNEKFES 17
|||||||||||||||||
Db 50 VIHPNSGSINYNEKFES 66
Yednock, et al. SEQ ID NO: 1 is 100% duplicate with instant SEQ ID NO: 11:
Query Match 100.0%; Score 63; Length 229;
Best Local Similarity 100.0%;
Matches 12; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ERDSTEVLPMDY 12
||||||||||||
Db 99 ERDSTEVLPMDY 110
Yednock, et al. teach the antibody fragment that binds to C1q, with the light chain variable domain comprising SEQ ID NO: 2 (paragraph 18), that is 100% duplicate with the instant light variable domain comprising instant SEQ ID NO: 5, 6, and 7 on instant claim 1.
Yednock, et al. SEQ ID NO: 2 is 100% duplicate with instant SEQ ID NO: 5:
Query Match 100.0%; Score 52; Length 214;
Best Local Similarity 100.0%;
Matches 11; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RASKSINKYLA 11
|||||||||||
Db 24 RASKSINKYLA 34
Yednock, et al. SEQ ID NO: 2 is 100% duplicate with instant SEQ ID NO: 6:
Query Match 100.0%; Score 32; Length 214;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SGSTLQS 7
|||||||
Db 50 SGSTLQS 56
Yednock, et al. SEQ ID NO: 2 is 100% duplicate with instant SEQ ID NO: 7:
Query Match 100.0%; Score 52; Length 214;
Best Local Similarity 100.0%;
Matches 9; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QQHNEYPLT 9
|||||||||
Db 89 QQHNEYPLT 97
Yednock, et al. teach the antibody Fab fragment comprising a light chain of amino acid sequence provided in SEQ ID NO: 2, which is at least 95% (100% for instant SEQ ID NO: 37) homologous to the amino acid sequence of the light chain variable domain of instant SEQ ID NO: 35-38.
Yednock, et al. teach the antibody Fab fragment comprising a heavy chain of amino acid sequence provided in SEQ ID NO: 1, which is at least 95% (100% for instant SEQ ID NO: 33) homologous to the amino acid sequence of the light chain variable domain of instant SEQ ID NO: 31-34.
Yednock, et al. SEQ ID NO: 2 is 95.5% duplicate with instant SEQ ID NO: 35:
Query Match 95.5%; Score 533; Length 214;
Best Local Similarity 96.3%;
Matches 103; Conservative 1; Mismatches 3; Indels 0; Gaps 0;
Qy 1 DVQITQSPSYLAASLGERATINCRASKSINKYLAWYQQKPGKTNKLLIYSGSTLQSGIPA 60
||||||||| |:|||||||||||||||||||||||||||||| ||||||||||||||||
Db 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
Qy 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
Yednock, et al. SEQ ID NO: 2 is 98.6% duplicate with instant SEQ ID NO: 36:
Query Match 98.6%; Score 546; Length 214;
Best Local Similarity 99.1%;
Matches 106; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKANKLLIYSGSTLQSGIPA 60
||||||||||||||||||||||||||||||||||||||||||| ||||||||||||||||
Db 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
Qy 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
Yednock, et al. SEQ ID NO: 2 is 100% duplicate with instant SEQ ID NO: 37:
Qy 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
Qy 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
Yednock, et al. SEQ ID NO: 2 is 99.5% duplicate with instant SEQ ID NO: 38:
Query Match 99.5%; Score 552; Length 214;
Best Local Similarity 98.1%;
Matches 105; Conservative 2; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DIQLTQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
|:|:||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
Qy 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIK 107
Yednock, et al. SEQ ID NO: 1 is 96.6% duplicate with instant SEQ ID NO: 31:
Qy 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
Qy 61 NEKFESKATITVDKSTSTAYMQLSSLTSEDSAVYYCAGERDSTEVLPMDYWGQGTSVTVS 120
||||||: |||||||||||||:|||| |||:||||||||||||||||||||||||:||||
Db 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
Qy 121 S 121
|
Db 121 S 121
Yednock, et al. SEQ ID NO: 1 is 99.4% duplicate with instant SEQ ID NO: 32:
Qy 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
Qy 61 NEKFESRATITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
||||||| ||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
Qy 121 S 121
|
Db 121 S 121
Yednock, et al. SEQ ID NO: 1 is 100% duplicate with instant SEQ ID NO: 33:
Qy 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
Qy 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
Qy 121 S 121
|
Db 121 S 121
Yednock, et al. SEQ ID NO: 1 is 99.5% duplicate with instant SEQ ID NO: 34:
Qy 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVRQAPGQGLEWIGVIHPNSGSINY 60
|||||||||||||||||||||||||||||||||||||:||||||||||||||||||||||
Db 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
Qy 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
Qy 121 S 121
|
Db 121 S 121
Yednock, et al. teach the Fab fragment comprising amino acid sequence of SEQ ID NO: 2 which is 100% identical to instant SEQ ID NO: 39 and 40.
Yednock, et al. SEQ ID NO: 2 is 100% duplicate with instant SEQ ID NO: 39:
Query Match 100.0%; Score 1205; Length 229;
Best Local Similarity 100.0%;
Matches 229; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVQSGAELKKPGASVKVSCKSSGYHFTSYWMHWVKQAPGQGLEWIGVIHPNSGSINY 60
Qy 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NEKFESRVTITVDKSTSTAYMELSSLRSEDTAVYYCAGERDSTEVLPMDYWGQGTTVTVS 120
Qy 121 SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS 180
Qy 181 SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT 229
|||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT 229
Yednock, et al. SEQ ID NO: 2 is 100% duplicate with instant SEQ ID NO: 40:
Query Match 100.0%; Score 1108; Length 214;
Best Local Similarity 100.0%;
Matches 214; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DVQITQSPSSLSASLGERATINCRASKSINKYLAWYQQKPGKAPKLLIYSGSTLQSGIPA 60
Qy 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIKRTVAAPSVFIFPP 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLEPEDFAMYYCQQHNEYPLTFGQGTKLEIKRTVAAPSVFIFPP 120
Qy 121 SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT 180
Qy 181 LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 214
||||||||||||||||||||||||||||||||||
Db 181 LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 214
Yednock, et al. teach dosage of the antibody will depend on the treatment, route of administration, the nature of the therapeutics, sensitivity of the patient to the therapeutics, etc. A clinician can determine the maximum safe dose for an individual, depending on the route of administration. Utilizing ordinary skill, the competent clinician will be able to optimize the dosage of a particular therapeutic composition in the course of routine clinical trials (paragraph 182).
Based on the application disclosure on page 56, line 9, optimization is reasonable of dosages and dosage administration as different dosages are recited in instant claims 1, 9-16, 21 and 23. The time of dosage and measuring clinical endpoints can clearly be a result effective parameter that a person having ordinary skill in the art would routinely optimize. Optimization of parameters is a routine practice that would be obvious for a person of ordinary skill in the art to employ. It would have been customary for an artisan of ordinary skill to determine the optimal amount of each ingredient, i.e., the dosage and dosing regimen, needed to achieve the desired results. The principle of law states from MPEP §§ 2144.05: "The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages," (see In re Peterson, 315 F.3d at 1330, 65 USPQ2d at 1382). Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation," (See In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955)).
Applicant’s arguments
Applicant’s arguments (page 9, remarks received 04/14/2026) have been fully considered but are not found persuasive for the following reasons.
Applicant argues that the specific dosage of 1 mg to 10 mg of anti-C1q Fab fragment is not disclosed. It is understood that applicant argues that optimization of parameters is an obviousness argument, not an anticipation argument under 35 U.S.C 102.
Response to Arguments
This has been fully considered but is not found to be persuasive for the follow reasons. The rejection has been adjusted to be under the statutory basis of 35 U.S.C 103, to which fully supports the rejection under optimization of parameters as stated above.
Conclusion
12. No claims are allowed.
13. Any inquiry concerning this communication or earlier communications from the examiner should be directed to Syed J Abbas whose telephone number is (571)272-0015. The examiner can normally be reached M-Th, 9:00AM-4:00PM.
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/SYED J ABBAS/Examiner, Art Unit 1674
/VANESSA L. FORD/Supervisory Patent Examiner, Art Unit 1674
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