DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant's amendment and remarks, filed 12/29/25, are acknowledged.
Claims 1, 11, 14-16, 26, 29-30 have been amended.
Claims 1, 4-9, 11-16, 19-24, 26-33 are pending.
Claims 32-33 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
Claims 1, 4-9, 11-16, 19-24, 26-31 are being acted upon.
This application contains sequence disclosures that are encompassed by the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR § 1.821(a)(1) and (a)(2). However, this application fails to comply with the requirements of 37 CFR §§ 1.821 through 1.825 for the reason(s) set forth below:
The claims fail to disclose the SEQ ID NOS for the amino acid sequences in Claim 5-6. The specification on page 5, 31-32 is objected to in that it also fails to disclose the SEQ ID Nos for the same sequences as in claims 5-6. Amendment to recite the corresponding SEQ ID Nos. from the sequence listing, i.e. SEQ ID NO 1, 19-33, is required. Additionally, the substitute specification, filed 8/1/25 incorrectly identifies SEQ ID NO: 39-42 (as the 12/10/21 sequence listing only has 38 sequences). The sequences identified as SEQ ID NO: 39-42 in the substitute specification and the present claims correspond to SEQ ID NO: 34-37 of the sequence listing. Amendment to replace SEQ ID NO: 39-42 with SEQ ID NO: 34-37 in the claims and specification would be remedial.
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 1, 4-9, 11-16, 19-24, 26-31 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 1 is indefinite in the recitation that the chimeric polypeptide sequence includes “a vascular endothelial growth factor (VEGF-A) and (VEGF-D)”. The fact that both VEGF-A and VEGF-D appear in parenthesis makes the claim unclear. While a parenthetical can be used to define an abbreviation for a term, the claim does not appear to do so. For example, if the claim were to recite a vascular endothelial growth factor A (VEGF-A) and a vascular endothelial growth factor D (VEGF-D) or a vascular endothelial growth factor (VEGF)-A and VEGF-D, it would be clear that the parenetical portion is defining an abbreviation. However, It appears that claim 1 may be intended to encompass any VEGF, with the parenthetical “(VEGF-A) and (VEGF-D)” being merely exemplary. This is particularly the case given the dependent claims which specify that the sequence includes a VEGF selected from VEGF-A and VEGF-D. In other words, either claim 1 intends to encompass any VEGF, or if claim 1 intends to require VEGF-A and VEGF-D, the dependent claims fail to further limit claim 1. Claim 1 is also indefinite in the recitation that the polypeptide includes “a” VEGF-A, for example. Does the claim mean a VEGF-A polypeptide ( i.e. full length VEG-A, see page 18 of the specification). Do the claim mean a VEGF-A sequence, a portion of VEGF-A? The scope of the claims is unclear and indefinite. For the purposes of examination, the claim is being interpreted as requiring a VEGF-A amino acid sequence and a VEGF-D amino acid sequence.
Claim 14 recites a specific amino acid sequence, which the claim identifies as SEQ ID NO: 38. However, SEQ ID NO: 38 does not correspond to the claimed sequence, and the scope of the claim is unclear and indefinite. Does it require the recited sequence, or would it encompass SEQ ID NO: 38, which is a different sequence. Amendment to refer to SEQ ID NO: 36, which corresponds to the sequence shown in claim 14, would be remedial.
Claims 20-21 recites the limitation "the first linker" in line 1. There is insufficient antecedent basis for this limitation in the claims.
Claim 29 is indefinite in the recitation that the chimeric protein “initially” has the amino acid sequence of SEQ ID NO: 36. Do the claims require SEQ ID NO: 36, or is the claim meant to encompass fragments thereof that can be derived form an “initial “ sequence. The claim is unclear and indefinite. Claim 29 is also indefinite and unclear in the recitation of a “synthetic protein chimeric synthetic protein” in line 2.
Claims 29-30 recite the limitation "the synthetic protein" or “the chimeric synthetic protein” in lines 1-2. There is insufficient antecedent basis for this limitation in the claim.
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.
Claims 7-9 and 22-24 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. Claims 7-8 and 22-23 recite that the chimeric polypeptide sequences includes a VEGF sequence, or a VEGF sequence selected from VEGF-A, VEGF-B, VEGF-C, and VEGF-D. However, claims 1 and 16 recites a VEGF-A and a VEGF-D, i.e. the claims already requires a VEGF-A and VEGF-D sequence, and therefore claims 7-8 and 22-23 fail to further limit claims 1 and 16, from which they depend. Claims 9 and 24 recite that the chimeric polypeptide includes a first VEGF domain and a second VEGF domain, and are included to the extent that claims 1 and 16 would appear to require at least a portion of VEGF-A and VEGF-D, i.e. a first and second VEGF “domain” and therefore claims 9 and 24 do not further limit the claims. 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.
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(s) 1, 4-5, 7-9, 15-16, 19-20, 22-24, and 31 is/are rejected under 35 U.S.C. 102(a)(1) as anticipated by US 20140248302.
The ‘302 publication teaches a recombinant (i.e. synthetic) chimeric protein comprising a cholera toxin B protein a SSG linker and a first VEGF-A domain and a second VEGF domain (see Fig 28, in particular). Said second VEGF domain (derived from VEGF-C) comprises the amino acid sequence TNTFFKPPCV, which is a sequence identical to residues found VEGF-D (see VEGF-D of SEQ ID NO: 18 in the instant application). Thus, the chimeric protein of the ‘302 publication comprises a chimeric polypeptide sequence that includes a VEGF-A sequence and a VEGF-D sequence, a linker, and a CTB protein and is within the scope of the instant claims. Claims 15 is included since the chimeric protein above comprises a portion of sequence from SEQ ID NO: 37 (the CTB sequence), which would be “an” amino acid sequence from SEQ ID NO: 37 (amendment to recite “the” amino acid sequence of SEQ ID NO: 37, would overcome the rejection of claim 15). The ’302 publication teaches an immunogenic composition comprising said protein and an adjuvant (see paragraph 174, in particular).
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.
Claim(s) 1, 4-9, 11-13, 15-16, 19-24, 26-28, and 31 is/are rejected under 35 U.S.C. 103 as obvious over US 2016/0095910, in view of US 2010/0216702 and evidenced by GenBank accession ABG56901.1, 2016.
The ‘910 publication teaches a synthetic chimeric protein comprising an immunogenic carrier protein sequence of SEQ ID NO: 1 that comprises a portion of cholera toxin B (for example residues IERMKTLR, as evidenced by GenBank ABG56901.1, i.e. an immunogenic polypeptide sequence of CTB). The ‘910 publication also teaches that the chimeric protein can further include a linker to attach a growth factor, and one or more of a full length growth factors selected from IGF-1, IGF-2, FGF1, FGF2, TGF-α, TGF-β, VEGF-A, VEGF-B, VEGF-C, VEGF-D, PDGF, NGF, EGF, HGF, BMP's, PDL1 and IL's 1-6. (see paragraphs 21-22, 38, and the claims, in particular). The ’910 publication also teaches an embodiment wherein the synthetic chimeric protein further comprises growth factor sequences, which can be VEGF-A and VEGF-C (i.e. a chimeric polypeptide having a first and second VEGF domain) linked to said carrier protein (See page 7, in particular).
Although the ‘910 publication does not explicitly teach a combination of full length VEGF-A and VEGF-D, it would be obvious to do so. For example, the ‘702 publication, teaches that VEGF-C and VEGF-D are homolog polypeptides that act as specific ligands for the same receptors, and that VEGF-A can be fused to VEGF-B, VECF-C, or VEDG-F D to form a chimera (see paragraphs 8, 49 and 17, in particular). Thus, one could simply substitute VEGF-D in the chimeric polypeptide of the ‘910 publication for VEGF-C, since they are technical equivalents.
Furthermore, selecting from the specifically recited options that can be included in the chimeric polypeptide would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. A person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense (see KSR International Co. V. Telefex Inc 82 USPQ2d 1385).
Regarding claim 6, the ‘910 discloses using a linker of claim 6 in an exemplary chimeric polypeptide (see Fig. 13, in particular). Selecting from the disclosed linkers would be obvious and involve choosing amount a finite number of predictable options.
Regarding claims 11 and 26, including a full length VEGF-A and VEGF-D, as made obvious by the cited references, would have the sequences of SEQ ID NO: 34 and 35 of the instant application. See, the ‘702 publication, which teaches VEGF-A exists as isoforms of different lengths, i.e. 121, 145, 148, 165, amino acids. All of the VEGF-A isoforms comprise SEQ I DNO: 35 of the instant application. Thus, it would be obvious that when using the VEGF-A full length polypeptide in the chimeric polypeptides of the ‘910 publication, that one could select one of the known, wild-type VEGF-isoforms (as taught in the ‘702 publication) and that any of these would comprise SEQ ID NO: 35 of the instant application. publication). Likewise, the ‘702 publication teaches that wild type VEGF-D has a sequence of SEQ ID NO: 52, which comprises SEQ ID NO: 34 of the instant application. Thus, it would be obvious that when selecting full length VEGF-D, as suggested in the ‘910 publication, it would comprise SEQ ID NO: 34 of the instant application. Furthermore, full length VEGF-A and VEGF-D, as made obvious above, would bind to VEGF1-3 receptors. Claims 15 is included since the proteins above would comprise SEQ ID NO: SEQ ID NO: 34 and 35 of the instant claims, which would be “an” amino acid sequence from SEQ ID NO: 37 (amendment to recite “the” amino acid sequence of SEQ ID NO: 37 would overcome the rejection of claim 15).
Applicant’s arguments filed 12/29/25 have been fully considered, but they are not persuasive.
Applicant argues that the ‘910 publication teaches modifying CTB subunit, but not fusing the subunit to chimeric synthetic proteins, as presently claimed.
The ‘910 publication teaches immunogenic chimeric polypeptides comprising SEQ ID NO: 1,, a linker, and a second sequence including one or more of the following full length growth factors IGF-1, IGF-2, FGF1, FGF2, TGF-β, VEGF-A, VEGF-B, VEGF-C, VEGF, D, PDGF, NGF, EGF, HGF, BMP's, and IL's 1-6. Said SEQ ID NO: 1 comprises IERMKTLR, which as noted above is a portion of cholera toxin B. Thus, the proteins of the ‘910 publication comprise “a polypeptide sequence including an immunogenic polypeptide sequence of a CTB protein” as recited in the instant claims.
Applicant argues that merely providing a broad list of possible elements does not render any specific combination obvious. Applicant argues that the ‘910 publication discloses a laundry list of growth factors and cytokines, with no guidance to select VEGF-A and VEGF-D from the list. Applicant argues that the ‘702 publication does not cure this defect, since the it discloses the use of VEGF-receptor antagonists that are modified VEGF-analogs with mutations, which are structurally different that the claimed VEGF molecules.
The ’910 publication teaches a recombinant chimeric protein comprising carrier protein comprise a portion of cholera toxin B (for example residues IERMKTLR), a linker, and at least one or more additional polypeptide sequences, wherein the polypeptides include a full length of one or more of the following: IGF-1, IGF-2, FGF1, FGF2, TGF-α, TGF-β, VEGF-A, VEGF-B, VEGF-C, VEGF, D, PDGF, NGF, EGF, HGF, BMP's, PDL1 and IL's 1-6. Selecting from the combinations that could be made from this defined list would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. A person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense (see KSR International Co. V. Telefex Inc 82 USPQ2d 1385).
Additionally, as noted above, the ’910 publication also teaches a specific example of using VEGF-A and VEGF-C (i.e. a chimeric polypeptide having a first and second VEGF domain) linked to said carrier protein (See page 7, in particular). One could also simply substitute VEGF-C with VEGF-D in said polypeptide, since VEGF-C and VEGF-D are technical equivalents (see the ‘702 publication, which teaches that VEGF-C and VEGF-D are homolog polypeptides that act as specific ligands for the same receptors, and that VEGF-A can be fused to VEGF-B, VECF-C, or VEDG-F D to from a chimera (see paragraphs 8, 49 and 17, in particular).
Furthermore, the ‘702 is not relied upon for its analogs, but rather for its disclosure of naturally occurring, wild type VEGF polypeptides sequence isoforms. For example, the ‘702 publication teaches VEGF-A exists as isoforms of different lengths, i.e. 121, 145, 148, 165, amino acids. All of the VEGF-A isoforms comprise SEQ ID NO; 35 of the instant application. Thus, it would be obvious that when using the VEGF-A full length polypeptide in the chimeric polypeptides of the ‘910 publication, that one could select one of the known, wild-type VEGF-isoforms (as taught in the ‘702 publication) and that any of these would comprise SEQ ID NO: 35 of the instant application. Likewise, the ‘702 publication teaches that wild type VEGF-D has a sequence of SEQ ID NO: 52, which comprises SEQ ID NO: 34 of the instant application. Thus, it would be obvious that when selecting full length VEGF-D, as suggested in the ‘910 publication, it would comprise SEQ ID NO: 34 of the instant application.
Claim(s) 1, 4-5, 7-9, 11-13, 15-16, 19-20, 22-24, 26-28, and 31 is/are rejected under 35 U.S.C. 103 as obvious over US 20140248302, in view of US 2010/0216702.
The teachings of the ‘302 publication are described above. The ‘302 publication also teaches a recombinant (i.e. synthetic) chimeric protein comprising more than one different growth factor sequence (i.e. a chimeric sequence), a linker, and a cholera toxin B protein (see paragraphs 13-16, 18, 46, 125, in particular). The ‘302 publication also teaches that the chimeric protein can include one or more of a full length IGF-1, IGF-2, FGF1, FGF2, TGF-α, TGF-β, VEGF-A, VEGF-B, VEGF-C, VEGF-D, PDGF, NGF, EGF, HGF, BMP's, PDL1 and IL's 1-6. (see claims and paragraph 18, in particular). Although the ‘302 publication does not explicitly disclose a combination of full length VEGF-A and VEGF-D, it would be obvious to combine these elements, since doing so would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. A person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense (see KSR International Co. V. Telefex Inc 82 USPQ2d 1385).
In addition, the ‘702 publication, teaches that VEGF-C and VEGF-D are homologous polypeptides that act as specific ligands for the same receptors, and that VEGF-A can be fused to VEGF-B, VECF-C, or VEDG-F D to form a chimera (see paragraphs 8, 49 and 17, in particular). Thus, one could simply substitute VEGF-D in the chimeric polypeptide of the ‘302 publication for VEGF-C, since they are technical equivalents.
Regarding claims 11 and 26, including a full length VEGF-A and VEGF-D, as made obvious by the cited references, would have the sequences of SEQ ID NO: 34 and 35 of the instant application. See, the ‘702 publication, which teaches VEGF-A exists as isoforms of different lengths, i.e. 121, 145, 148, 165, amino acids. All of the VEGF-A isoforms comprise SEQ ID NO: 35 of the instant application. Thus, it would be obvious that when using the VEGF-A full length polypeptide in the chimeric polypeptides of the ‘302 publication, that one could select one of the known, wild-type VEGF-isoforms (as taught in the ‘702 publication) and that any of these would comprise SEQ ID NO: 35 of the instant application. publication). Likewise, the ‘702 publication teaches that wild type VEGF-D has a sequence of SEQ ID NO: 52, which comprises SEQ ID NO: 34 of the instant application. Thus, it would be obvious that when selecting full length VEGF-D, as suggested in the ‘302 publication, it would comprise SEQ ID NO: 34 of the instant application. Furthermore, full length VEGF-A and VEGF-D, as made obvious above, would bind to VEGF1-3 receptors. Claims 15 is included since the proteins above would comprise SEQ ID NO: SEQ ID NO: 34 and 35 of the instant claims, which would be “an” amino acid sequence from SEQ ID NO: 37 (amendment to recite “the” amino acid sequence of SEQ ID NO: 37 would overcome the rejection of claim 15).
Applicant’s arguments filed 12/29/25 have been fully considered, but they are not persuasive.
Applicant argues that the claims are not obvious for the same reasons set forth above.
The claims stand rejected for the same reasons set forth above.
Claims 6 and 21 are rejected under 35 U.S.C. 103(a) as being unpatentable over US 20140248302 and US 2010/0216702, as applied to claims 1, 4, 16, and 20 above, and further in view of US 2016/0095910.
The combined teachings of the ‘302 and ‘702 publications are discussed above.
They do not explicitly teach the linker of claim 6 or 21.
The ‘910 discloses using a linker of claim 6 and 21 in an exemplary chimeric polypeptide for linking immunogenic polypeptide carriers to a growth factor polypeptide (see Fig. 13, in particular).
Therefore, it would have been obvious to a person of ordinary skill in the art at the time the invention was made to apply the teachings of the ‘910 publication, to chimeric polypeptide made obvious by the ‘302 and ‘702 publications. Doing so would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. A person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense (see KSR International Co. V. Telefex Inc 82 USPQ2d 1385).
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 1, 4-9, 11-13, 15-16, 19-24, 26-28, and 31 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 10,736,948, or claims 1-9 of U.S. Patent No. 11,419,923, or claims 1-9 of 12,433,939 in view of US 2010/0216702 and 8,173,613.
The patents claim a synthetic protein comprising an immunogenic polypeptide comprising CT-B and EGF and one or more additional growth factors (i.e.. a chimeric polypeptide), and a linker having SSG. The patents claim a immunogenic composition comprising said protein and an adjuvant The patents claim that the polypeptide can include more than one additional growth factor, and that a growth factor can be selected from VEGF-A and VEGF-D. It would be obvious to use VEGF-A and D sequences as the growth factors as choosing among a finite predictable options, or based on the teachings of the ‘702 publication would be obvious for the same reasons set forth above. Additionally, regarding the linker of claim 6, the ‘613 patent teaches a linker comprising the linker of claim 6 (see SEQ ID NO: 15) and choosing from known linker sequences for use in chimeric polypeptides would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. Furthermore, the use of the polypeptide as an immunogenic composition with an adjuvant would be obvious based on the ‘910 publication. Furthermore, VEGF-A and VEGF-D, as made obvious above, would bind to VEGF1-3 receptors. Claims 15 is included to the extent they encompass subsequences, such as VEGF-A or CT-B, for the same reasons set forth above.
Claims 1, 4-9, 11-13, 15-16, 19-24, 26-28, and 31 are rejected on the ground of nonstatutory double patenting as being unpatentable over the claims U.S. Patent Nos. 9,902,760, or 11,198,716, or 12,030,920, in view of 2016/0095910 and US 2010/0216702.
The patents claim a synthetic protein comprising an immunogenic polypeptide comprising CT-B and on or more growth factors selected from VEGF-A and VEGF-D (i.e. a chimeric polypeptide), and a linker having SSG. Additionally, as noted above, the ‘910 publication teaches a linker sequence of claims 6 and 21 for use in chimeric polypeptides would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. Furthermore, the use of the polypeptide as an immunogenic composition with an adjuvant would be obvious based on the ‘910 publication. It would be obvious to use VEGF-A and D sequences as the growth factors since the ‘910 publication teaches they can be used as growth factors for linking to CT-B like polypeptides for creating immunogenic compositions with an adjuvant. Furthermore, selecting the claimed VEGF-A and D sequences as taught by the ‘702 publication would be obvious for the same reasons set forth above. Furthermore, VEGF-A and VEGF-D, as made obvious above, would bind to VEGF1-3 receptors. Claim 15 is included to the extent they encompass fragments, such as VEGF-A, for the same reasons set forth above.
Applicant argues that the ‘910 publication and ‘702 publication are deficient for the same reason set forth above.
The claims stand rejected for the same reasons set forth above.
No claim is allowed.
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Amy E. Juedes
Patent Examiner
Technology Center 1600
/AMY E JUEDES/Primary Examiner, Art Unit 1644