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 .
Status of the Claims
Claims 16 and 19-37 are pending
Claims 22-24 and 32-33 are newly amended.
Claims 36 and 37 are newly added.
Upon further consideration, due to amendment of the claims, which establishes a genus/species relationship for the claimed recombinant polypeptide and homooligomer, the restriction requirement in regards to a recombinant polypeptide (claims 16 and 19-21) and the polynucleotide of the recombinant homooligomer (claim 25) has been withdrawn.
Claims and 26-35 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 09/18/2025.
Claims 16, 19-25 and 36-37 have been examined on their merits.
Withdrawn Objections & Rejections
The objections and rejections presented herein represent the full set of objections and rejections currently pending in the application. Any objections or rejections not specifically reiterated are hereby withdrawn.
The rejections of claims 22 and 23 under 35 U.S.C. 102(a)(1) as being anticipated by Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022) as evidenced by Hofmeyer et al. (Journal of Molecular Biology, 2013, on IDS 07/08/2022) are withdrawn due to amendment of the claims.
The rejection of claim 24 under 35 U.S.C. 103 as being unpatentable over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022) in view of Strong et al. (US20180117140A1, 2018) and Pucket (Chapter 23 in Protein-Protein Interactions, 2015) as evidenced by Hofmeyer et al. (Journal of Molecular Biology, 2013, on IDS 07/08/2022) is withdrawn due to amendment of the claims.
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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 16 and 19-21 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.
Claim 16 recites the limitation “the CCP6 domain of the C4BP alpha chain” in lines 2-3.
There is insufficient antecedent basis for either “the CCP6” or “the C4BP alpha chain” as these polypeptides have not been established in the claim. Amending the claim to “a CCP6” and “a C4BP alpha chain” would be ameliorative.
Claim 22 also recites the phrase “said polypeptide does not comprise” in line 4. Since claim 22 establishes a homologomer of at least six “recombinant polypeptides”, the limitation should read “said recombinant polypeptides do not comprise.”
Claim 23 likewise, recites “the CCP6” or “the C4BP alpha chain” without clear antecedent for a CCP6 or a C4BP alpha chain. It is noted, that since 23 depends on claim 22, clarification of these terms in claim 22 would ameliorate antecedent basis issues in claim 23.
Claim 23 likewise recites the phrase “said polypeptide does not comprise” in lines 3-4. Since claim 23 establishes a homologomer of at least seven “recombinant polypeptides”, the limitation should read “said recombinant polypeptides do not comprise.”
Claim 24, recites “wherein the polypeptide is the polypeptide consisting of” in lines 1-2. However, claim 1 establishes “A homooligomer of at least six recombinant polypeptides”. Therefore, claim 24 should read “wherein a said recombinant polypeptide of the homooligomer consists of.”
Claims 23 and 24 are also rejected under 35 USC 112(b) for their dependence on claim 22.
Appropriate clarification is required.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim 16 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited).
In regards to claim 16, Perramon discloses a C4BP isoform comprising six alpha chains which comprise the CCP6 domain polypeptide and lacks CCP1, CCP2, CCP3, CCP4, CCP5, CCP7, and CCP8 domains (and thus, is a recombinant polypeptide) (paragraphs [0024-0025]; claims 1, 3, 9). Perramon discloses that the C4BP isoform preserves the ability to form oligomers (paragraph [0031]).
In regards to an oligomerization domain, the instant specification (paragraph [0078]) broadly states, “The term ‘oligomerization domain’, as used herein, refers to a polypeptide domain having the property that polypeptides comprising said domain have a propensity to aggregate and form oligomers.”
Thus, because the C4BP isoform as taught by Perramon has the ability to (the property of) forming oligomers, it necessarily comprises a “oligomerization domain” as defined in the specification.
Therefore, Perramon discloses the invention as claimed.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 19, 22-23 and 25 are rejected under 35 U.S.C. 103 as being unpatentable over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited) in view of Strong et al. (US20180117140A1, 2018, previously cited).
In regards to claim 19 and 22, as above, Perramon teaches a C4BP isoform comprising six alpha chains which comprise the CCP6 domain polypeptide and lacks CCP1, CCP2, CCP3, CCP4, CCP5, CCP7, and CCP8 domains (and thus, is a recombinant polypeptide) (paragraphs [0024-0025]; claims 1, 3, 9). Perramon teaches that the C4BP isoform preserves the ability to form oligomers (paragraph [0031]).
In regards to an oligomerization domain, the instant specification (paragraph [0078]) broadly states, “The term ‘oligomerization domain’, as used herein, refers to a polypeptide domain having the property that polypeptides comprising said domain have a propensity to aggregate and form oligomers.”
Thus, because the C4BP isoform as taught by Perramon has the ability to (the property of) forming oligomers, it necessarily comprises a “oligomerization domain” (even if it is also the CCP6 domain itself) as defined in the specification.
As the C4BP isoform oligomerizes and comprises identical alpha chains (paragraphs 0024-0025, 0031], it is therefore also a homooligomer.
In regards to SEQ ID NO: 3, it is noted that this sequences comprises or consists of a CCP6 domain and a specific oligomerization domain.
In regards to this sequences, Perramon teaches an identical sequences corresponding to the sequences of the CCP6 domain (see SEQ ID NO: 1, paragraph [0029], sequences LCC . . . CGD; see also 20250929_104149_us-17-768-274-6.rag, BFS87735).
Perramon is silent as to the sequences of the specific oligomerization domain of SEQ ID NO: 3 ((sequences ETP . . . KEL).
However, the claimed oligomerization domain sequence was known in the art before the effective filing date.
Specifically, Strong teaches a C4BP multimerization (oligomerization) domain comprising sequences identical to those as in SEQ ID NO: 3 (see SEQ ID NO: 16, SEQ ID NO: 17, paragraphs [0059-0060]), sequences ETP . . . KEL; see also 20250929_104149_us-17-768-274-6.rai, RESULT 26).
Additionally, Applicant should note that that the successful cloning and sequencing of the cDNA encoding a known protein is obvious, and thus unpatentable, if (1) there was some suggestion or motivation in the prior art to clone the cDNA, and (2) there was a “reasonable expectation of success,” based on "detailed enabling methodology" in the prior art. Ex parte Kubin, 83 U.S.P.Q.2d (BNA) 1410 (B.P.A.I. 2007), aff'd, 561 F.3d 1351 (Fed. Cir. 2009).
In the instant case, a person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to the oligomerization domain (sequences ETP . . . KEL) because Strong indicates that the C4DP multimerization (oligomerization) domain is useful for engineering proteins that can be used to develop therapies and which provides stronger immune responses compared to other multimerization domains (paragraphs [0015, 0555]).
Furthermore, because, as above, Strong teaches that amino acids sequences that are identical to the claim sequence, because Strong teaches methods for engineering cells to express the C4DP multimerization domain sequence (such as with vectors) (paragraphs [0131-0132]), and because Perramon and Strong are in the same technical field of engineering proteins, it could have been done with predictable results and a reasonable expectation of success.
The homologomer as taught by Perramon and as modified by Strong would thus comprise or consist of SEQ ID NO: 3.
In regards to claim 23, Perramon teaches that the homooligomer may also comprise seven alpha chain chains, which as above, may comprise identical CCP6 domains lacking CCP1, CCP2, CCP3, CCP4, CCP5, CCP7, and CCP8, and which retains the ability to oligomerize, as discussed above (claim 9, paragraphs 0024-0025, 0031). As discussed above, the homooligomer as taught by Perramon and as modified by Strong would and comprise SEQ ID NO: 3.
In regards to claim 25, Perramon teaches a polypeptide of the homooligomer (paragraph [0033]).
Therefore, the combined teachings of Perramon and Strong render the invention unpatentable as claimed.
Claim 21 is rejected under 35 U.S.C. 103 as being unpatentable over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited) in view of Strong et al. (US20180117140A1, 2018, previously cited) and Pucket (Chapter 23 in Protein-Protein Interactions, 2015, previously cited).
Claim 24 is rejected under 35 U.S.C. 103 as being unpatentable over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited) in view of Strong et al. (US20180117140A1, 2018, previously cited) as applied to claim 22 above, and further in view of Pucket (Chapter 23 in Protein-Protein Interactions, 2015, previously cited).
In regards to claim 21, Perramon discloses claim 16 as discussed above.
In regards to claims 21 and 24, it is noted that difference between SEQ ID NO: 3 and SEQ ID NO: 6 is that SEQ ID NO: 6 also comprises a hexahistidine (often referred to by its commercial name, a 6xHis-tag).
However, a person of ordinary skill in the art would have been motivated to include a hexahistidine sequence because Pucket teaches that hexahistidine tags have unique properties such as small size, relatively low abundance of naturally occurring consecutive histidine repeat, and the ability to interact with immobilized metal cations to provide for the capture of proteins and protein complexes of interest (Abstract, p365; Introduction, p366).
Furthermore, because Perramon teaches that many applications have been developed utilizing terminal hexahistidine residues, because hexahistidine is a readily available commercial product for tagging recombinant proteins, and because Pucket teaches methods for transfecting cells with hexahistidine (Introduction, p367; Materials/Methods, p368-370), it could have been done with predictable results and a reasonable expectation of success.
The homooligomer as taught by Perramon and as modified by Strong and Pucket would therefore comprise SEQ ID NO: 6.
Therefore, the combined teachings of Perramon, Strong, and Pucket render the invention unpatentable as claimed.
Claim 36 is rejected under 35 U.S.C. 103 as being unpatentable over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited) in view of Strong et al. (US20180117140A1, 2018, previously cited) as evidenced by Hofmeyer et al. (Journal of Molecular Biology, 2013, on IDS 07/08/2022, previously cited) as applied to claim 22 above, and further in view of Chaudhari et al. (JMB, 1998).
In regards to claim 36, the homooligomer as taught by Perramon and as modified by Strong results in a protein that both comprises or consists of SEQ ID NO: 3 as discussed above.
In regards to an additional N-terminal methionine, as taught by Chaudhari, when recombinant proteins are expressed in E. coli, while typically, the N-terminal methionine is enzymatically removed, this does not always take place, and that about half of E. coli expressed proteins contain an extra N-terminal methionine residue (Introduction, p1180). A person of ordinary skill in the art would have been motivated to express a recombinant protein (such as the homoologomer as taught by Perramon) in E. coli in order to rapidly generate the protein. About half of the recombinant protein would naturally comprise an additional N-termal methionine. Furthemore, because Chaudhari teaches that recombinant proteins can be expressed in E. coli (which again, would result in a homologomer with an extra N-terminal methionine) (Introduction, p1180) it could have been done with predictable results and a reasonable expectation of success.
Therefore, the combined teachings of Perramon, Strong, and Chaudhari render the invention unpatentable as claimed.
Claim 20 is rejected under 35 U.S.C. 103 as being unpatentable over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited) in view of Strong et al. (US20180117140A1, 2018, previously cited), Pucket (Chapter 23 in Protein-Protein Interactions, 2015, previously cited), and Ting et al. (WO2010042654A2).
Claim 37 is rejected under 35 U.S.C. 103 as being unpatentable over Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited) in view of Strong et al. (US20180117140A1, 2018, previously cited) as applied to claim 22 above, and further in view of Pucket (Chapter 23 in Protein-Protein Interactions, 2015, previously cited) and Ting et al. (WO2010042654A2).
In regards to claims 20 and 37, in regards to SEQ ID NO: 7, it is noted that the difference between it and SEQ ID NO: 6 is an N-terminal secretory signal peptide (sequences MHP . . . VLG, which is further noted are the sequences of SEQ ID NO: 4). Thus, SEQ ID NO: 7 also comprises the same 6XHis-Tag, CCP6, and oligomerization domain as in SEQ ID NO: 6. It would have been prima facie obvious to modify the homooligomer of Perramon with these corresponding sequences as discussed above (see rejections of claims 21 and 24 as discussed above).
In regards to the secretory signal peptide, Ting teaches a human signal secretory protein with 100% identity with these claimed sequences (SEQ ID NO: 98, see Result 1, us-17-768-274-4.rag). Ting also teaches secretory signal peptides are useful for secretion in mammalian cells and are well documented (p15, lines 1-6). A person of ordinary skill in the art would have been motivated to include a signal secretory protein and specifically one with the corresponding sequences in order to promote secretion in human cells. Furthermore, because Ting teaches sequences with 100% identity, teaches that it can be used to promote secretion in human cells, and because Ting teaches that secretory signal peptides are well-documented, it could have been done with predictable results and a reasonable expectation of success.
Therefore, the combined teachings of Perramon, Strong, Pucket, and Ting render the invention unpatentable as claimed.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 16, 19, 22-23, and 25 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 5-12 and 15 of U.S. Patent No. 10,106,589 B2 in view of Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022) and Strong et al. (US20180117140A1, 2018).
Claims 21 and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 5-12 and 15 of U.S. Patent No. 10,106,589 B2 in view of Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022) and Strong et al. (US20180117140A1, 2018) as applied to claims 16 and 22 above, and further in view of Pucket (Chapter 23 in Protein-Protein Interactions, 2015, previously cited).
Claims 20 and 37 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 5-12 and 15 of U.S. Patent No. 10,106,589 B2 in view of Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022) and Strong et al. (US20180117140A1, 2018) as applied to claims 16 and 22 above, and further in view of Ting et al. (WO2010042654A2).
Claim 36 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 5-12 and 15 of U.S. Patent No. 10,106,589 B2 in view of Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022) and Strong et al. (US20180117140A1, 2018) as applied to claims 16 and 22 above, and further in view of Chaudhari et al. (JMB, 1998).
Although the conflicting claims of U.S. patent No. 10,106,589 are not identical to the currently prosecuted claims 16, 19, 22-23, and 25, they are not patently distinct from each other because said claims of both inventions are drawn to C4BP isoforms (recombinant polypeptides) comprising 6 or 7 alpha chains.
While the C4BP isoform of U.S. patent No. 10,106,589 does not require that the six alpha chains comprise the CCP6 domain without CCP1, CCP2, CCP3, CCP4, CCP5, CCP7, and CCP8 domains, a person of ordinary skill in the art would have been motivated to engineer a C4BP with a CCP6 domains in order specifically promote a tolerogenic state in monocyte-derived dendritic cells, as taught by Perramon (paragraphs [0007, 0020]). They would have been motivated to eliminate domains CCP1, CCP2, CCP3, CCP4, CCP5, CCP7, and CCP8 in order to avoid off-target binding or activation and improve specificity. Furthermore, because Perramon teaches a C4BP isoform comprising six or seven alpha chains which comprise the CCP6 domain (a polypeptide) and lacks CCP1, CCP2, CCP3, CCP4, CCP5, CCP7, and CCP8 domains (and thus, is a recombinant polypeptide) and comprise only identical CCP6 domains (and thus is a homooligomer) (paragraphs [0024-0025]; claims 1, 3, 9), it could have been done with predictable results and a reasonable expectation of success.
In regards to an oligomerization domain, a person of ordinary skill in the art would have been motivated to include an oligomerization domain in order to preserve the natural secondary structure of the C4BP complex, and because, as taught by Strong, the C4DP multimerization (oligomerization) domain is useful for engineering proteins that can be used to develop therapies and which provides stronger immune responses compared to other multimerization domains (paragraphs [0015, 0555]).
Furthermore, because Perramon teaches that recombinant C4BP isoforms preserves the ability to form oligomers (paragraph [0031]) and because Strong teaches that cells can be engineered to express a C4BP oligomerization domain (paragraphs [0131-0132]), it could have been done with predictable results and a reasonable expectation of success.
In regards to SEQ ID NO: 3, it is noted that this sequences comprises or consists of a CCP6 domain and a specific oligomerization domain.
In regards to this sequences, Perramon teaches an identical sequences corresponding to the sequences of the CCP6 domain (see SEQ ID NO: 1, paragraph [0029], sequences LCC . . . CGD; see also 20250929_104149_us-17-768-274-6.rag, BFS87735).
Perramon is silent as to the sequences of the specific oligomerization domain of SEQ ID NO: 3 ((sequences ETP . . . KEL).
However, the claimed oligomerization domain sequence was known in the art before the effective filing date.
Specifically, Strong teaches a C4BP multimerization (oligomerization) domain comprising sequences identical to those as in SEQ ID NO: 3 (see SEQ ID NO: 16, SEQ ID NO: 17, paragraphs [0059-0060]), sequences ETP . . . KEL; see also 20250929_104149_us-17-768-274-6.rai, RESULT 26).
Additionally, Applicant should note that that the successful cloning and sequencing of the cDNA encoding a known protein is obvious, and thus unpatentable, if (1) there was some suggestion or motivation in the prior art to clone the cDNA, and (2) there was a “reasonable expectation of success,” based on "detailed enabling methodology" in the prior art. Ex parte Kubin, 83 U.S.P.Q.2d (BNA) 1410 (B.P.A.I. 2007), aff'd, 561 F.3d 1351 (Fed. Cir. 2009).
In the instant case, a person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to the oligomerization domain (sequences ETP . . . KEL) because Strong indicates that the C4DP multimerization (oligomerization) domain is useful for engineering proteins that can be used to develop therapies and which provides stronger immune responses compared to other multimerization domains (paragraphs [0015, 0555]).
Furthermore, because, as above, Strong teaches that amino acids sequences that are identical to the claim sequence, because Strong teaches methods for engineering cells to express the C4DP multimerization domain sequence (such as with vectors) (paragraphs [0131-0132]), and because Perramon and Strong are in the same technical field of engineering proteins, it could have been done with predictable results and a reasonable expectation of success.
The homologomer as taught by Perramon and as modified by Strong would thus comprise or consist of SEQ ID NO: 3.
In regards to claims 21 and 24, in regards to SEQ ID NO: 6, it is noted that difference between SEQ ID NO: 3 and SEQ ID NO: 6 is that SEQ ID NO: 6 also comprises a hexahistidine (often referred to by its commercial name, a 6xHis-tag).
However, a person of ordinary skill in the art would have been motivated to include a hexahistidine sequence because Pucket teaches that hexahistidine tags have unique properties such as small size, relatively low abundance of naturally occurring consecutive histidine repeat, and the ability to interact with immobilized metal cations to provide for the capture of proteins and protein complexes of interest (Abstract, p365; Introduction, p366).
Furthermore, because Perramon teaches that many applications have been developed utilizing terminal hexahistidine residues, because hexahistidine is a readily available commercial product for tagging recombinant proteins, and because Pucket teaches methods for transfecting cells with hexahistidine (Introduction, p367; Materials/Methods, p368-370), it could have been done with predictable results and a reasonable expectation of success.
The homooligomer as taught by Perramon and as modified by Strong and Pucket would therefore comprise SEQ ID NO: 6.
In regards to claims 20 and 37, in regards to SEQ ID NO: 7, it is noted that the difference with SEQ ID NO: 6 is an N-terminal secretory signal peptide (sequences MHP . . . VLG, which is further noted are the sequences of SEQ ID NO: 4). Thus, SEQ ID NO: 7 also comprises the same 6XHis-Tag, CCP6, and oligomerization domain as in SEQ ID NO: 6. It would have been prima facie obvious to modify the homooligomer of Perramon with these corresponding sequences as discussed above.
In regards to the secretory signal peptide, Ting teaches a human signal secretory protein with 100% identity with these claimed sequences (SEQ ID NO: 98, see Result 1, us-17-768-274-4.rag). Ting also teaches secretory signal peptides are useful for secretion in mammalian cells and are well documented (p15, lines 1-6). A person of ordinary skill in the art would have been motivated to include a signal secretory protein and specifically one with the corresponding sequences in order to promote secretion in human cells. Furthermore, because Ting teaches sequences with 100% identity, teaches that it can be used to promote secretion in human cells, and because Ting teaches that secretory signal peptides are well-documented, it could have been done with predictable results and a reasonable expectation of success.
In regards to claim 36, in regards to an additional N-terminal methionine, as taught by Chaudhari, when recombinant proteins are expressed in E. coli, while typically, the N-terminal methionine is enzymatically removed, this does not always take place, and that about half of E. coli expressed proteins contain an extra N-terminal methionine residue (Introduction, p1180). A person of ordinary skill in the art would have been motivated to express a recombinant protein (such as the homoologomer as taught by Perramon) in E. coli in order to rapidly generate the protein. About half of the recombinant protein would naturally comprise an additional N-termal methionine. Furthemore, because Chaudhari teaches that recombinant proteins can be expressed in E. coli (which again, would result in a homologomer with an extra N-terminal methionine) (Introduction, p1180) it could have been done with predictable results and a reasonable expectation of success.
Response to Arguments
Applicant request rejoinder of at least claims 25-27 and 29-35 (Remarks, p6).
In regards to claims 16, 19-21 and 25, due to amendment of claims and overlapping scope (and therefore, have a genus/species relationship), the restriction requirement for these claims has been withdrawn. However, in regards to claims 26-27 and 29-35, while it is noted that these claims are amended, because are not a genus/species relationship, and the technical feature is not a special technical feature, withdrawal of the restriction requirement is premature at this time.
Applicant argues that the claims as amended are not anticipated by Perramon under 35 USC 102 (Remarks, p8).
Applicant’s arguments, see p8, filed 09/18/2025, with respect to the rejection of claims 22 and 23 under 35 USC 102(a)(1) have been fully considered and are persuasive. Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground(s) of rejection is made in view of Perramon et al. (EP3384923A1, published 10/10/2018, on IDS 08/08/2022, previously cited) in view of Strong et al. (US20180117140A1, 2018, previously cited) under 35 USC 103 as discussed above. Furthermore, claim 16 is anticipated by Perramon as discussed above.
Applicant argues that the claimed SEQ ID NO: 3 (corresponding to the C4BP isoform PRP6-HO7) provides unexpected results, specifically, that it has greater immunomodularity activity compared to the homooligomer of Perramon (Remarks, p9). Citing the Annex II of the Declaration under 37 CFR 1.132 filed 04/02/2026, Applicant argues that the oligomerization domain of SEQ ID NO: 2 (and particularly when the polypeptide sequence comprises SEQ ID NO: 3 is more effective in forming oligomers in the induction of a tolerogenic state (Remarks, p10). Applicant also argues SEQ ID NO: 2 has immunomodulatory activity while other oligomerization domains do not (Remarks, p10; citing Annex II).
Applicant’s arguments filed 04/02/2026 have been fully considered but are not found persuasive.
In regards to Applicant’s allegations of unexpected results, whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the “objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support.” In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range. In re Clemens, 622 F.2d 1029, 1036, 206 USPQ 289, 296 (CCPA 1980) (see MPEP 716.02(d)).
In the instant case, the claims do not require any specific result.
Furthermore, according to MPEP 716.02(a), not only must the evidence relied upon should establish “that the differences in results are in fact unexpected and unobvious and of both statistical and practical significance.” Ex parte Gelles, 22 USPQ2d 1318, 1319 (Bd. Pat. App. & Inter. 1992) (Mere conclusions in appellants’ brief that the claimed polymer had an unexpectedly increased impact strength “are not entitled to the weight of conclusions accompanying the evidence, either in the specification or in a declaration.”), but also, a greater than additive effect is not necessarily sufficient to overcome a prima facie case of obviousness because such an effect can either be expected or unexpected. Applicants must further show that the results were greater than those which would have been expected from the prior art to an unobvious extent, and that the results are of a significant, practical advantage. Ex parte The NutraSweet Co., 19 USPQ2d 1586 (Bd. Pat. App. & Inter. 1991) (Evidence showing greater than additive sweetness resulting from the claimed mixture of saccharin and L-aspartyl-L-phenylalanine was not sufficient to outweigh the evidence of obviousness because the teachings of the prior art lead to a general expectation of greater than additive sweetening effects when using mixtures of synthetic sweeteners.).
Applicant argues that a polypeptide comprising SEQ ID NO: 3 and not comprising any other CCPs would not have been obvious because Perramon does not suggest that oligomerization is even needed to preserve immunomodulatory activity (Remarks, p9). Specifically, Applicant argues that CCP6-based peptides that do not contain an oligomerization domain are still capable of preventing maturation of human Mo-DCs (Remarks, p9). In particular, Applicant argues that while Perramon teaches that peptides consisting of mutants of the CCP6 domain retain tolerogenic activity (citing the Declaration under 37 CFR 1.132 filed 04/02/2026), the instant application demonstrates that the CCP6 domain isolated without the oligomerization domain, and the homoologomer formed by seven oligomerization domains and lacking the CCP6 domain are not sufficient by themselves to retain immunomodulatory activity over Mo-macrophages or Mo-DCs (Remarks, p9). Thus, Applicant concludes that a person of ordinary skill in the art would never consider adding an oligomerization domain because it would have been considered unnecessary (Remarks, p10).
Applicant’s arguments filed 04/02/2026 have been fully considered but are not found persuasive.
In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., preserving immunomodulatory activity, tolerogenic activity, maturing Mo-DCs or Mo-macrophages) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
In regards to Applicant’s argument that the recombinant polypeptide as taught by Perramon does not contain an oligomerization domain, as discussed above, as broadly defined in the instant specification, “The term ‘oligomerization domain’, as used herein, refers to a polypeptide domain having the property that polypeptides comprising said domain have a propensity to aggregate and form oligomers” (paragraph [0078]).
Thus, because the C4BP isoform as taught by Perramon has the ability to (the property of) forming oligomers, it necessarily comprises a “oligomerization domain” as defined by the specification.
Furthermore, while Perramon may suggest that the CCP6 domain itself is sufficient for oligomerization (and is thus itself, an oligomerization domain as defined above), Perramon does not disallow modification to that domain, nor disallow the addition of an additional specific oligomerization domains.
Indeed, Perramon also teaches that “[A]n another embodiment, the functionally equivalent variant of the polypeptide comprising the CCP6 domain of the C4BP alpha chain is a fusion protein comprising a first region which comprises the CCP6 domain and a second region which comprises a polypeptide which does not form part of the C4BP alpha chain” (paragraph [0054]).
Thus, Perramon explicitly allows for additional components to the recombinant polypeptide.
Moreover, and critically, as declared by Applicant, “Perramon discloses assays demonstrating the immunomodulatory activity of the C4BP isoform lacking the beta C4BP(β-) (PRP-HO7) . . . the presently claimed homooligomer comprising SEQ ID NO: 3 (PRP6-H07)” (bolding added; see paragraph 6, Declaration under 37 CFR 1.132 filed 04/02/2026). Thus, as admitted by Applicant (who is noted is the same inventor as Perramon), the C4BP isoform as disclosed by Perramon in fact comprises the same “Hepta oligomerization” domain of the C4BPα domain (see Declaration, Results, 7th page).
Thus, the difference is in the “PRP6” domain (proline rich protein, which is part of the CCP6 domain, not the Hepta oligomerization domain.
However, as discussed above, Perramon explicitly discloses the sequences of the claimed CCP6 domain (see SEQ ID NO: 1, paragraph [0029], sequences LCC . . . CGD; see also 20250929_104149_us-17-768-274-6.rag, BFS87735). Additionally, as discussed above, a C4BP isoform comprising six alpha chains which comprise the CCP6 domain polypeptide and lacks CCP1, CCP2, CCP3, CCP4, CCP5, CCP7, and CCP8 domains (paragraphs [0024-0025]; claims 1, 3, 9).
Thus a “PRP6” domain is an embodiment envisioned by the disclosure of Perramon.
In regards to the specific oligomerization domain as in SEQ ID NO: 3, as discussed above, a person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to this specific oligomerization domain (sequences ETP . . . KEL; SEQ IDs NO: 16 or 17 of Strong) because Strong indicates that the C4DP multimerization (oligomerization) domain is useful for engineering proteins that can be used to develop therapies and which provides stronger immune responses compared to other multimerization domains (paragraphs [0015, 0555]).
Thus, a person of ordinary skill in the art would have been motivated to use the oligomerization domain of Strong because it is superior for therapeutic purposes to other multimerization domains.
Furthermore, because, as above, Strong teaches that amino acids sequences that are identical to the claim sequence, because Strong teaches methods for engineering cells to express the C4DP multimerization domain sequence (such as with vectors) (paragraphs [0131-0132]), and because Perramon and Strong are in the same technical field of engineering proteins, it could have been done with predictable results and a reasonable expectation of success.
In regards to Strong, Applicant argues that Strong’s teachings in regards to a C3BP multimerization (oligomerization) domain are general, that that SEQ ID NO: 16 is one of 33 recited oligomerization domains, and is thus, a non-finite list (Remarks, p11). Continuing, Applicant argues that because Strong teaches that the recited oligomerization domains can include modifications (such as N-terminal or C-terminal deletions) this results in thousands of possible sequences (Remarks, p11; footnote, p11).
Applicant’s arguments filed 04/02/2026 have been fully considered but are not found persuasive.
Despite Applicant’s assertion, recitation of 33 oligomerization domains is a finite list. Furthermore, SEQ ID NO: 2 (which is part of SEQ ID NO: 3) is a sequence entirely taught by Strong (SEQ ID NO: 16 which consists of ETP . . . KEL). Thus, while Strong may allow variation, the specific sequence was taught by Strong. Therefore, a person of ordinary skill in the art could have chosen the oligomerization domain of Strong, from finite number of identified, predictable solutions, with a reasonable expectation of success as required by MPEP 2143(I).
Continuing, in regards to Strong, Applicant argues that Strong relates to enhancement of B cell response to HIV antigens, and activation of the immune system, which is the opposite effect which is obtained by Applicant (Remarks, p11-12). On the other hand, Applicant argues that the tolerogenic response aims to prevent the immune system from reacting to harmless or self-antigens, leading to silencing of the immune system (Remarks, p12). Thus, Applicant argues that Strong actually teaches away from the instant invention, and as a result, there is no reasonable expectation of success when using the C4BP oligomerization domain (Remarks, p12).
Applicant’s arguments filed 04/02/2026 have been fully considered but are not found persuasive.
In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., silencing the immune system) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Specifically, the claims are not drawn to any specific use, but are generically drawn to a recombinant polypeptide.
Furthermore, even if the claims did require a specific use for silencing the immune system, while Strong may use C4b domains for treating HIV infection, since Strong does not suggest that domains of this proteins could not be used for other purposes, and therefore, does not criticize, discredit, or otherwise discourage the solution claimed, and therefore, Strong does not “teach away” from the use of a C4b oligomerization domain to promote tolerogenic activity (In re Fulton, 391 F.3d 1195, 1201, 73 USPQ2d 1141, 1146 (Fed. Cir. 2004). See also UCB, Inc. v. Actavis Labs, UT, Inc., 65 F.4th 679, 692, 2023 USPQ2d 448 (Fed. Cir. 2023).
Moreover, as evidenced by Serrano et al. (Frontiers in Immunology, published 04/40/2018), it was known in the art that C4b (specifically, the C4b(β-) isoform) has immunomodulatory activity and promotes tolerogenic responses (Title, Abstract, p1; Fig. 1, p5; Complement Components, p6). Thus, it was known in the art before the effective filing date that C4b has dual immune response.
Therefore, even if the claims required a specific tolerogenic effect, a person of ordinary skill in the art could have still used the C4b oligomerization domain of Strong with predictable results and a reasonable expectation of success.
Applicant argues that Pucket does not cure the deficiencies of Perramon and Strong (Remarks, p12).
Applicant’s arguments filed 04/02/2026 have been fully considered but are not found persuasive because Perramon and Strong are not deficient for the reasons discussed above.
In regards to the double-patenting rejections, Applicant argues that the rejections are flawed because Perramon is deficient and that a person of ordinary skill in the art would not have been motivated to add an oligomerization domain as discussed above (Remarks, p13). Applicant also argues that the rejections are flawed because, in regards to Strong, a person of ordinary skill in the art would not have considered an oligomerization domain for activating the immune system useful for suppressing it (Remarks, p13).
Applicant’s arguments filed 04/02/2026 have been fully considered but are not found persuasive.
In regards to Perramon, as discussed above, in regards to Applicant’s argument that the recombinant polypeptide as taught by Perramon does not contain an oligomerization domain, as discussed above, as broadly defined in the instant specification, “The term ‘oligomerization domain’, as used herein, refers to a polypeptide domain having the property that polypeptides comprising said domain have a propensity to aggregate and form oligomers” (paragraph [0078]).
Thus, because the C4BP isoform as taught by Perramon has the ability to (the property of) forming oligomers, it necessarily comprises a “oligomerization domain” as defined by the specification.
Furthermore, while Perramon may suggest that the CCP6 domain itself is sufficient for oligomerization (and is thus itself, an oligomerization domain as defined above), Perramon does not disallow modification to that domain, nor disallow the addition of an additional specific oligomerization domains.
Indeed, Perramon also teaches that “[A]n another embodiment, the functionally equivalent variant of the polypeptide comprising the CCP6 domain of the C4BP alpha chain is a fusion protein comprising a first region which comprises the CCP6 domain and a second region which comprises a polypeptide which does not form part of the C4BP alpha chain” (paragraph [0054]).
Thus, Perramon explicitly allows for additional components to the recombinant polypeptide.
In regards to the specific oligomerization domain as in SEQ ID NO: 3, as discussed above, a person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to this specific oligomerization domain (sequences ETP . . . KEL; SEQ IDs NO: 16 or 17 of Strong) because Strong indicates that the C4DP multimerization (oligomerization) domain is useful for engineering proteins that can be used to develop therapies and which provides stronger immune responses compared to other multimerization domains (paragraphs [0015, 0555]).
Thus, a person of ordinary skill in the art would have been motivated to use the oligomerization domain of Strong because it is superior for therapeutic purposes to other multimerization domains.
Furthermore, because, as above, Strong teaches that amino acids sequences that are identical to the claim sequence, because Strong teaches methods for engineering cells to express the C4DP multimerization domain sequence (such as with vectors) (paragraphs [0131-0132]), and because Perramon and Strong are in the same technical field of engineering proteins, it could have been done with predictable results and a reasonable expectation of success.
In response to Strong, in response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., silencing the immune system) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Specifically, the claims are not drawn to any specific use, but are generically drawn to a recombinant polypeptide.
Furthermore, even if the claims did require a specific use for silencing the immune system, while Strong may use C4b domains for treating HIV infection, since Strong does not suggest that domains of this proteins could not be used for other purposes, and therefore, does not criticize, discredit, or otherwise discourage the solution claimed, and therefore, Strong does not “teach away” from the use of a C4b oligomerization domain to promote tolerogenic activity (In re Fulton, 391 F.3d 1195, 1201, 73 USPQ2d 1141, 1146 (Fed. Cir. 2004). See also UCB, Inc. v. Actavis Labs, UT, Inc., 65 F.4th 679, 692, 2023 USPQ2d 448 (Fed. Cir. 2023).
Moreover, as evidenced by Serrano et al. (Frontiers in Immunology, published 04/40/2018), it was known in the art that C4b (specifically, the C4b(β-) isoform) has immunomodulatory activity and promotes tolerogenic responses (Title, Abstract, p1; Fig. 1, p5; Complement Components, p6). Thus, it was known in the art before the effective filing date that C4b has dual immune response.
Therefore, even if the claims required a specific tolerogenic effect, a person of ordinary skill in the art could have still used the C4b oligomerization domain of Strong with predictable results and a reasonable expectation of success.
Declaration under 37 CFR 1.132
Applicant declares that the claimed invention demonstrates unexpected results (paragraphs 5-6, 9-10; citing Figs 1-3 in Annex I and Annex II).
Specifically, Applicant declares that the claimed recombinant polypeptide comprising SEQ ID NO: 3, and no other CCP of the C4BP alpha chain have increased tolerogenic activity when forming homooligomers and that this was unexpected over Perrammon (paragraphs 5-6).
Additionally, Applicant declares that Annex II shows that the recombinant polypeptide is more effective when forming oligomers in the induction of a tolerogenic state when the oligomerization domain of SEQ ID NO: 2, and particularly when the polypeptide sequence is SEQ ID NO: 3 (paragraph 9).
The Declaration under 37 CFR 1.132 filed 04/02/2026 is insufficient to overcome the rejection of the claims based upon Perramon as set forth in the last Office action because they are not commensurate in scope with the claims.
In regards to Applicant’s allegations of unexpected results, whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the “objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support.” In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range. In re Clemens, 622 F.2d 1029, 1036, 206 USPQ 289, 296 (CCPA 1980) (see MPEP 716.02(d)).
In the instant case, the claims do not require any specific result. Specifically, the claims do not require or suggest any specific result in regards to the effect of the homooligomer on the induction of a tolerogenic state and are limited to SEQ ID NO: 3, not SEQ ID NO: 2. Furthermore, the evidence only provides evidence of a homooligomer with seven CCP6 subunits, while the claims more broadly are limited to six or seven subunits.
Moreover, it is noted that the results only compare individual components, β-chain oligomerization domain, or mouse α-chain oligomerization domain. However, the results do not compare other human α-chain oligomerization domain and do not suggest that the known oligomerization of Strong itself produces any specific effect.
In regards to the β-chain oligomerization domain, this would not be expected to produce a result because as evidenced by Serrano et al. (Frontiers in Immunology, published 04/40/2018), the C4b(β-) isoform, not the C4b(β+) isoform of C4b has immunomodulatory activity and promotes tolerogenic responses (Title, Abstract, p1; Fig. 1, p5; Complement Components, p6).
In regards to mouse α-chain oligomerization domain, this is the α-chain oligomerization domain of a different species, and therefore, would not expected to produce the same result.
In regards to the specific oligomerization domain as in SEQ ID NO: 3, as discussed above, a person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to this specific oligomerization domain (sequences ETP . . . KEL; SEQ IDs NO: 16 or 17 of Strong) because Strong indicates that the C4DP multimerization (oligomerization) domain is useful for engineering proteins that can be used to develop therapies and which provides stronger immune responses compared to other multimerization domains (paragraphs [0015, 0555]).
Thus, a person of ordinary skill in the art would have been motivated to use the oligomerization domain of Strong because it is superior for therapeutic purposes to other multimerization domains.
Furthermore, because, as above, Strong teaches that amino acids sequences that are identical to the claim sequence, because Strong teaches methods for engineering cells to express the C4DP multimerization domain sequence (such as with vectors) (paragraphs [0131-0132]), and because Perramon and Strong are in the same technical field of engineering proteins, it could have been done with predictable results and a reasonable expectation of success.
Thus, even if the claims did require a specific effect on tolerogenic activity, since the homooligomer of Perramon and as modified by Strong would have the same sequences, it would be expected to produce the same results.
Applicant declares that none of the cited documents disclose or suggest the recombinant polypeptide comprising SEQ ID NO: 3 (paragraph 10).
Applicant declares that Perramon discloses CCP6-based peptides that do not contain an oligomerization domain and are capable of maturing human Mo-DCs (pointing to paragraphs [0056-0059] of Perramon (paragraph 7). Relatedly, Applicant declares that while Perramon asserts that while the CCP6 domain retains tolerogenic activity, it alone, does not (pointing to Fig. 1 in Annex 1) (paragraphs 7-8).
Applicant declares that Perramon discloses peptides based on variants of the CCP6 domain but does not include an oligomerization domain (paragraph 8).
The Declaration under 37 CFR 1.132 filed 04/02/2026 is insufficient to overcome the rejection of the claims based upon Perramon as set forth in the last Office action because they are not commensurate in scope with the claims and do not establish facts which overcome the rejection as discussed above.
In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., preserving immunomodulatory activity, tolerogenic activity, maturing Mo-DCs or Mo-macrophages) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
In regards to Applicant’s argument that the recombinant polypeptide as taught by Perramon does not contain an oligomerization domain, as discussed above, as broadly defined in the instant specification, “The term ‘oligomerization domain’, as used herein, refers to a polypeptide domain having the property that polypeptides comprising said domain have a propensity to aggregate and form oligomers” (paragraph [0078]).
Thus, because the C4BP isoform as taught by Perramon has the ability to (the property of) forming oligomers, it necessarily comprises a “oligomerization domain” as defined by the specification.
Furthermore, while Perramon may suggest that the CCP6 domain itself is sufficient for oligomerization (and is thus itself, an oligomerization domain as defined above), Perramon does not disallow modification to that domain, nor disallow the addition of an additional specific oligomerization domains.
Indeed, Perramon also teaches that “[A]n another embodiment, the functionally equivalent variant of the polypeptide comprising the CCP6 domain of the C4BP alpha chain is a fusion protein comprising a first region which comprises the CCP6 domain and a second region which comprises a polypeptide which does not form part of the C4BP alpha chain” (paragraph [0054]).
Thus, Perramon explicitly allows for additional components to the recombinant polypeptide.
It is noted that Perramon is the same as an instant inventor. Thus, if paragraph [0054] of Perramon does not refer to a modification such as a specific oligomerization domain, then Applicant could declare that this is not an embodiment envisioned by the disclosure of Perramon.
In regards to the specific oligomerization domain as in SEQ ID NO: 3, as discussed above, a person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to this specific oligomerization domain (sequences ETP . . . KEL; SEQ IDs NO: 16 or 17 of Strong) because Strong indicates that the C4DP multimerization (oligomerization) domain is useful for engineering proteins that can be used to develop therapies and which provides stronger immune responses compared to other multimerization domains (paragraphs [0015, 0555]).
Thus, a person of ordinary skill in the art would have been motivated to use the oligomerization domain of Strong because it is superior for therapeutic purposes to other multimerization domains.
Furthermore, because, as above, Strong teaches that amino acids sequences that are identical to the claim sequence, because Strong teaches methods for engineering cells to express the C4DP multimerization domain sequence (such as with vectors) (paragraphs [0131-0132]), and because Perramon and Strong are in the same technical field of engineering proteins, it could have been done with predictable results and a reasonable expectation of success.
Conclusion
No claims are allowed.
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/JOSEPH PAUL MIANO/Examiner, Art Unit 1631
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