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 .
Election/Restrictions
Claims 16-35 are pending.
Claims 22, 25-27 and 32-33 are newly amended.
Applicant’s election without traverse of Group II, claims 22-24 in the reply filed on 09/18/2025 is acknowledged.
Claims 16-21 and 25-35 withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim.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 22-24 have been examined on their merits.
Claim Rejections - 35 USC § 112
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 22-24 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 22 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.
Claims 22 and 23 are rejected 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).
In regards to claim 22, 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]). As evidenced by Hofmeyer, it is well-established in the art that the C4BP complex forma at the site of alpha chain oligomerization domains (Fig. 1, p1302; Fig. 2, p1306). Thus, a person of ordinary skill in the art would have recognized that the C4BP isoforms, as disclosed by Perramon comprise an oligomerization domain. As the C4BP isoform oligomerizes and comprises identical alpha chains (paragraphs 0024-0025, 0031], it is therefore a homooligomer.
In regards to claim 23, Perramon discloses 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).
Therefore, Perramon anticipates 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.
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) 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).
Perramon anticipates claim 22 as discussed above.
In regards to claim 24, in regards to SEQ ID NO: 6, Perramon explicitly teaches 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 oligomerization domain (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: 6 (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).
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.
Perramon does not explicitly teach that the C4DP isoform comprises six consecutive terminal histidine residues (a hexahistidine, or 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.
Therefore, the combined teachings of Perramon, Strong, and Pucket 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 22-23 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).
Although the conflicting claims of U.S. patent No. 10,106,589 are not identical to the currently prosecuted claims 22-23, they are not patently distinct from each other because said claims of both inventions are drawn to C4BP isoforms 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 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.
According to MPEP 2112.01,
“Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977)”.
Furthermore, “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). Continuing, “When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not” Id.
Claims 22-24 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), Strong et al. (US20180117140A1, 2018), and Pucket (Chapter 23 in Protein-Protein Interactions, 2015).
As discussed above, although the conflicting claims of U.S. patent No. 10,106,589 are not identical to the currently prosecuted claims 22-24, they are not patently distinct from each other because said claims of both inventions are drawn to C4BP isoforms 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 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: 6, in regards to the sequences of the CCP6 domain, Perramon teaches 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).
In regards to the C4BP oligomerization domain, Strong teaches a C4BP multimerization (oligomerization) comprising sequences identical to those as in SEQ ID NO: 6 (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).
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 CCP6 domain in order specifically promote a tolerogenic state in monocyte-derived dendritic cells, as taught by Perramon.
A person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to the oligomerization domain 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, both Perramon and Strong teach that amino acids sequences that are identical to the claimed sequences and because Perramon C4DP isoforms engineering engineered to preserve C4DP oligomerization, it could have been done with predictable results and a reasonable expectation of success.
In regards to the six consecutive terminal histidine residues (a hexahistidine, or often referred to by its commercial name, a 6xHis-tag), 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.
According to MPEP 2112.01,
“Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977)”.
Furthermore, “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). Continuing, “When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not” Id.
Claims 22-23 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 13-14, and 16 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) .
Although the conflicting claims of U.S. patent No. 10,106,589 are not identical to the currently prosecuted claims 22-23, they are not patently distinct from each other because said claims of both inventions are drawn to C4BP isoforms comprising the CCP6 region of the alpha-chain.
While the C4BP isoform of U.S. patent No. 10,106,589 does not require that 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 six or seven CCP6 domains because Perramon teaches that CCP6 domain specifically promotes tolerogenic state in monocyte-derived dendritic cells (paragraphs [0007, 0020])., and multiple repeating domains would be expected to increase this effect.
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.
According to MPEP 2112.01,
“Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977)”.
Furthermore, “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). Continuing, “When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not” Id.
Claims 22-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 13-14, and 16 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), Strong et al. (US20180117140A1, 2018), and Pucket (Chapter 23 in Protein-Protein Interactions, 2015).
Although the conflicting claims of U.S. patent No. 10,106,589 are not identical to the currently prosecuted claims 22-24, they are not patently distinct from each other because said claims of both inventions are drawn to C4BP isoforms comprising the CCP6 region of the alpha-chain.
While the C4BP isoform of U.S. patent No. 10,106,589 does not require that 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 six or seven CCP6 domains because Perramon teaches that CCP6 domain specifically promotes tolerogenic state in monocyte-derived dendritic cells (paragraphs [0007, 0020])., and multiple repeating domains would be expected to increase this effect.
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 Strong Perramon discloses that recombinant C4BP isoforms preserves the ability to form oligomers (paragraph [0031]), and therefore, must comprise the C4BP oligomerization domain, 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: 6, in regards to the sequences of the CCP6 domain, Perramon teaches 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).
In regards to the C4BP oligomerization domain, Strong teaches a C4BP multimerization (oligomerization) comprising sequences identical to those as in SEQ ID NO: 6 (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).
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 CCP6 domain in order specifically promote a tolerogenic state in monocyte-derived dendritic cells, as taught by Perramon.
A person of ordinary skill in the art would have been motivated to clone the cDNA corresponding to the oligomerization domain 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 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 the six consecutive terminal histidine residues (a hexahistidine, or often referred to by its commercial name, a 6xHis-tag), 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.
According to MPEP 2112.01,
“Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977)”.
Furthermore, “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). Continuing, “When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not” Id.
Conclusion
No claims are allowed.
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/JOSEPH PAUL MIANO/Examiner, Art Unit 1631