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 .
Response to Amendment
The amendment filed 17 July 2026 is acknowledged. Claims 1, 38-41 are amended. Claims 10 and 15 are newly cancelled.
Claim Status
Claims 1, 4, 8, 19-21, 24, 28, 38-42, 44, 46, 50-51, and 53 are pending and under examination in the instant office action.
Withdrawal of Objections
The objection to claim 1 for the recitation of “comprising a characteristic” is withdrawn in view of Applicant’s arguments that “comprising a characteristic” is synonymous with “characterized by” a characteristic (Remarks 7/17/2026 p. 6).
The objections to claims 38-40 for informalities is withdrawn in view of the amendments to the claims.
Withdrawal of Rejections
The rejection of claim 41 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite is withdrawn in view of the amendments to the claims.
The rejection of claims 1, 4, 8, 10, 15, 19-21, 24, 28, 38-42, 44, 46, 50-51, and 53 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is withdrawn in view of the amendments to the claims.
The rejection of claims 1, 4, 8, 10, 15, 19-21, 24, 28, 38-42, 44, 46, 50-51, and 53 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph for scope of enablement is withdrawn in view of the amendments to the claims.
The rejections of claims 10 and 15 are moot in view of the cancellation of the claims.
Double Patenting- Maintained
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, 8, 19-21, 24, 28, 38-42, 44, 46, 50-51, and 53 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 26 of U.S. Patent No. 11555078 (Of record, IDS dated 6/28/2023). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of '078 make obvious the instant claims as evidenced by as evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 published 28 July 2013 (PTO-892 dated 1/20/2026).
Regarding claims 1, 10, and 15, claims 1-26 of the ‘078 patent teach a polypeptide complex according to Formula I: A2-A1-L1-P1-H1 wherein A1 comprises a first antigen recognizing molecule that binds to an effector cell antigen, wherein A1 comprises an anti-CD3 binding molecule comprising complementary determining regions (CDRs) heavy and light chain SEQ ID NOs: 1-6; P1 comprises a peptide that binds to A1 of a particular formula as recited; wherein L1 comprises a linking moiety that connects A1 to P1 and is a substrate for a tumor specific protease; H1 comprises a half-life extending molecule; and A2 comprises a second antigen recognizing molecule that binds to PSMA (claim 1), wherein the polypeptide complex comprises the amino acid sequences according to SEQ ID NO: 72 and SEQ ID NO: 73 which are identical to instant SEQ ID NO: 1 and 2 as shown below:
Query Match 100.0%; Score 3414; Length 645;
Best Local Similarity 100.0%;
Matches 645; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSY 60
Qy 61 ADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLV 120
Qy 121 TVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQ 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 TVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQ 180
Qy 181 LVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 LVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYA 240
Qy 241 DSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 DSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTV 300
Qy 301 SSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPG 360
Qy 361 QAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGG 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 QAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGG 420
Qy 421 TKLTVLGGGGSDIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWYQQKTGKVPKFLIY 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 TKLTVLGGGGSDIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWYQQKTGKVPKFLIY 480
Qy 481 EASTLQSGVPSRFSGGGSGTDFTLTISSLQPEDVATYYCQNYNSAPFTFGPGTKVDIKRT 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 EASTLQSGVPSRFSGGGSGTDFTLTISSLQPEDVATYYCQNYNSAPFTFGPGTKVDIKRT 540
Qy 541 VAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSK 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 VAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSK 600
Qy 601 DSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 645
|||||||||||||||||||||||||||||||||||||||||||||
Db 601 DSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 645
Query Match 100.0%; Score 1199; Length 226;
Best Local Similarity 100.0%;
Matches 226; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVQLVESGGGVVQPGRSLRLSCAASGFAFSRYGMHWVRQAPGKGLEWVAVIWYDGSNKYY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVESGGGVVQPGRSLRLSCAASGFAFSRYGMHWVRQAPGKGLEWVAVIWYDGSNKYY 60
Qy 61 ADSVKGRFTISRDNSKNTQYLQMNSLRAEDTAVYYCARGGDFLYYYYYGMDVWGQGTTVT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTQYLQMNSLRAEDTAVYYCARGGDFLYYYYYGMDVWGQGTTVT 120
Qy 121 VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL 180
Qy 181 QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC 226
||||||||||||||||||||||||||||||||||||||||||||||
Db 181 QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC 226
The claims of ‘078 do not explicitly teach the characteristics:(a) at least one disulfide bond formed by a pair of cysteine residues in the first chain or the second chain or by a pair of cysteine residues in the first chain and the second chain; (b) a secondary structure composition comprising a P-sheet or a random coil; (c) at least one pyroglutamine in the second chain; (d) a melting temperature (Tm) between of about 65 °C to about 85 °C when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0 mg/mL in a buffer comprising 10 mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3 (e) a far UV circular dichroism peak at a wavelength between 190 nm and 205 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.1mg/mL in 10mM potassium phosphate buffer pH 7.0; (f) a far UV circular dichroism dip at a wavelength between 210 nm and 220 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.lmg/mL in 10mM potassium phosphate buffer pH 7.0; or (g) a near UV circular dichroism peak at a wavelength between 250 nm and 300 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0mg/mL in a buffer comprising 10mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3, the claims of the ‘078 patent are silent. However, each of the properties a)-g) are inherent properties of the polypeptide complex consisting of SEQ ID NO: 1 and 2, because a protein with the same primary structure would be expected to have the same secondary structure, tertiary structure, and post-translational modifications provided it is made in a mammalian cell type. In order to determine the meaning of the claims to polypeptide SEQ ID NO: 1 and 2, the specification was consulted (MPEP §804.B.1). The specification discloses that the polypeptide may be made by expression in a host-expression vector system, and that the host may be for example a microorganism or a mammalian cell selected from a list (Col. 65 lines 15-43; Col. 68 lines 40-60).
It would have been obvious for a person of ordinary skill in the art, before the effective filing date, to make the polypeptide complex using a mammalian host-expression vector system to benefit from a method of making the claimed polypeptide. As set forth in MPEP §2145 (II) “[m]ere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention”. Products of identical composition cannot have mutually exclusive properties. See MPEP § 2112. As evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 ““the advanced mammalian folding, secretion and post-translational apparatus is capable of producing antibodies indistinguishable from those in the human body with least concerns for immunogenic modifications” (p. 5 right column, “Mammalian Cells” section ¶1, emphasis is the Examiner’s). Thus, a polypeptide complex of SEQ ID NO: 1 and SEQ ID NO: 2 with the characteristics a)-g) as claimed is made obvious by the claims of ‘078 because the polypeptide complex comprising SEQ ID NO: 1 and SEQ ID NO: 2 of ‘078 would inherently possess all of the recited characteristics when made in a mammalian host-expression vector system.
Regarding dependent claims 4, 8, 19, 20, 21, 24, 28, 38-42, 44, 46,and 50-51, as described for claim 1, each of these characteristics would be an inherent property of the polypeptide complex consisting of 100% identity to SEQ ID NO: 1 and SEQ ID NO: 2 provided the polypeptide complex was produced in mammalian cells in order to produce the same folding and post-translational modifications. Thus, the claims directed at the particular disulfide bonds and positions of disulfide bonds (claims 19, 20, 21, 24, 28, 39-41) or lack thereof as free sulfhydryl (claim 38), the secondary and tertiary structures and resultant far UV and near UV circular dichroism peaks (claim 42, 46, 50-51), and melting temperatures would be characteristics inherently possessed by a polypeptide complex that has the same folding and post-translational modifications as the instantly claimed polypeptide complex.
Regarding claim 53, the claims of ‘078 do not explicitly recite a method of treating cancer comprising administering to a subject in need thereof the isolated recombinant polypeptide complex of claim 1.
MPEP 804.B.1 teaches “In particular, when ascertaining the scope of the reference’s claim(s) to a compound, the examiner should consider the reference’s specification, including all of the compound’s uses that are disclosed. See Sun Pharm. Indus., 611 F.3d at 1386-88, 95 USPQ2d at 1801-02”. Thus, the disclosed uses in the specification of ‘078 were consulted. The specification teaches use of the polypeptide complex: “In some embodiments, are methods of treating cancer in a subject need in need thereof comprising administering to the subject an isolated polypeptide or polypeptide complex as described herein”. Therefore, claim 53 is also directed to an obvious variant (a disclosed use) of the polypeptide complex of SEQ ID NO: 1 and SEQ ID NO: 2.
Claims 1, 4, 8, 19-21, 24, 28, 38-42, 44, 46, 50-51, and 53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 31 and 61 of copending Application No. 18055932 (reference application) as evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 published 28 July 2013 (PTO-892 dated 1/20/2026). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of '932 make obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Regarding claims 1, 10, and 15, claims 31 and 61 of the ‘932 application teach a method of treating prostate cancer in a subject comprising administering a polypeptide complex according to Formula I: A2-A1-L1-P1-H1 wherein A1 comprises a first antigen recognizing molecule that binds to an effector cell antigen, wherein A1 comprises an anti-CD3 binding molecule comprising complementary determining regions (CDRs) heavy and light chain SEQ ID NOs: 1-6; P1 comprises a peptide that binds to A1 of a particular formula as recited; wherein L1 comprises a linking moiety that connects A1 to P1 and is a substrate for a tumor specific protease; H1 comprises a half-life extending molecule; and A2 comprises a second antigen recognizing molecule that binds to PSMA (claim 31), wherein the polypeptide complex comprises the amino acid sequences according to SEQ ID NO: 72 and SEQ ID NO: 73 which are identical to instant SEQ ID NO: 1 and 2 (claim 61) as shown below:
Query Match 100.0%; Score 3414; Length 645;
Best Local Similarity 100.0%;
Matches 645; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSY 60
Qy 61 ADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLV 120
Qy 121 TVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQ 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 TVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQ 180
Qy 181 LVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 LVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYA 240
Qy 241 DSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 DSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTV 300
Qy 301 SSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPG 360
Qy 361 QAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGG 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 QAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGG 420
Qy 421 TKLTVLGGGGSDIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWYQQKTGKVPKFLIY 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 TKLTVLGGGGSDIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWYQQKTGKVPKFLIY 480
Qy 481 EASTLQSGVPSRFSGGGSGTDFTLTISSLQPEDVATYYCQNYNSAPFTFGPGTKVDIKRT 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 EASTLQSGVPSRFSGGGSGTDFTLTISSLQPEDVATYYCQNYNSAPFTFGPGTKVDIKRT 540
Qy 541 VAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSK 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 VAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSK 600
Qy 601 DSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 645
|||||||||||||||||||||||||||||||||||||||||||||
Db 601 DSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 645
Query Match 100.0%; Score 1199; Length 226;
Best Local Similarity 100.0%;
Matches 226; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVQLVESGGGVVQPGRSLRLSCAASGFAFSRYGMHWVRQAPGKGLEWVAVIWYDGSNKYY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVESGGGVVQPGRSLRLSCAASGFAFSRYGMHWVRQAPGKGLEWVAVIWYDGSNKYY 60
Qy 61 ADSVKGRFTISRDNSKNTQYLQMNSLRAEDTAVYYCARGGDFLYYYYYGMDVWGQGTTVT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTQYLQMNSLRAEDTAVYYCARGGDFLYYYYYGMDVWGQGTTVT 120
Qy 121 VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL 180
Qy 181 QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC 226
||||||||||||||||||||||||||||||||||||||||||||||
Db 181 QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC 226
The claims of ‘932 do not explicitly teach the characteristics:(a) at least one disulfide bond formed by a pair of cysteine residues in the first chain or the second chain or by a pair of cysteine residues in the first chain and the second chain; (b) a secondary structure composition comprising a P-sheet or a random coil; (c) at least one pyroglutamine in the second chain; (d) a melting temperature (Tm) between of about 65 °C to about 85 °C when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0 mg/mL in a buffer comprising 10 mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3 (e) a far UV circular dichroism peak at a wavelength between 190 nm and 205 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.1mg/mL in 10mM potassium phosphate buffer pH 7.0; (f) a far UV circular dichroism dip at a wavelength between 210 nm and 220 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.1mg/mL in 10mM potassium phosphate buffer pH 7.0; or (g) a near UV circular dichroism peak at a wavelength between 250 nm and 300 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0mg/mL in a buffer comprising 10mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3, the claims of the ‘932 patent are silent. However, each of the properties a)-g) are inherent properties of the polypeptide complex consisting of SEQ ID NO: 1 and 2, because a protein with the same primary structure would be expected to have the same secondary structure, tertiary structure, and post-translational modifications provided it is made in a mammalian cell type. In order to determine the meaning of the claims to polypeptide SEQ ID NO: 1 and 2, the specification was consulted (MPEP §804.B.1). The specification discloses that the polypeptide may be made by expression in a host-expression vector system, and that the host may be for example a microorganism or a mammalian cell selected from a list ([199], [217-218]).
It would have been obvious for a person of ordinary skill in the art, before the effective filing date, to make the polypeptide complex using a mammalian host-expression vector system to benefit from a method of making the claimed polypeptide. As set forth in MPEP §2145 (II) “[m]ere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention”. Products of identical composition cannot have mutually exclusive properties. See MPEP § 2112. As evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 ““the advanced mammalian folding, secretion and post-translational apparatus is capable of producing antibodies indistinguishable from those in the human body with least concerns for immunogenic modifications” (p. 5 right column, “Mammalian Cells” section ¶1, emphasis is the Examiner’s). Thus, a polypeptide complex of SEQ ID NO: 1 and SEQ ID NO: 2 with the characteristics a)-g) as claimed is made obvious by the claims of ‘932 because the polypeptide complex comprising SEQ ID NO: 1 and SEQ ID NO: 2 of ‘932 would inherently possess all of the recited characteristics when made in a mammalian host-expression vector system.
Regarding dependent claims 4, 8, 19, 20, 21, 24, 28, 38-42, 44, 46,and 50-51, as described for claim 1, each of these characteristics would be an inherent property of the polypeptide complex consisting of 100% identity to SEQ ID NO: 1 and SEQ ID NO: 2 provided the polypeptide complex was produced in mammalian cells in order to produce the same folding and post-translational modifications. Thus, the claims directed at the particular disulfide bonds and positions of disulfide bonds (claims 19, 20, 21, 24, 28, 39-41) or lack thereof as free sulfhydryl (claim 38), the secondary and tertiary structures and resultant far UV and near UV circular dichroism peaks (claim 42, 46, 50-51), and melting temperatures would be characteristics inherently possessed by a polypeptide complex that has the same folding and post-translational modifications as the instantly claimed polypeptide complex.
Claims 1, 4, 8, 19-21, 24, 28, 38-42, 44, 46, 50-51, and 53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 19320207 (reference application) as evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 published 28 July 2013 (PTO-892 dated 1/20/2026). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of '207 make obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Regarding claims 1, 10, and 15, claims 1-20 of the ‘207 application teach a method of extending half-life and improving toxicity of a T-cell engager comprising tethering an inhibitory peptide mask to the T-cell engager via a cleavable linker to generate modified T-cell engager according to Formula I: A2-A1-L1-P1-H1 wherein A1 comprises a first antigen recognizing molecule that binds to an effector cell antigen; P1 comprises a peptide that binds to A1 of a particular formula as recited; wherein L1 comprises a linking moiety that connects A1 to P1 and is a substrate for a tumor specific protease; H1 comprises a half-life extending molecule; and A2 comprises a second antigen recognizing molecule(claim 1). Claim 2 recites wherein A1 comprises an antibody selected from a group of formats including single chain variable format; claim 3 recites wherein the A1 is anti-CD3. Claim 4 recites wherein P1 is bound to A1 through a list of types of interactions. Claim 5 recites wherein P1 has less than 70% sequence homology to the effector cell antigen. Claims 6 and 7 recites wherein P1 comprises an amino acid of no more than 40 amin acids, and at least 10 amino acids and no more than 20 amino acids in length. Claims 8-10 recites wherein the tumor specific protease is selected from a group including particular MMPs and serine proteases. Claims 12 and 13 recite the sequence formula for the linker. Claim 17 recites where H1 is a single domain antibody. Claim 19 recites the A2 is selected from a group of antibody formats including a Fab. Claim 20 recites the second antigen recognizing molecule binds to PSMA. In order to understand the scope of the claims, the specification was consulted for embodiments of the particular protein complexes as claimed. The specification recites the polypeptide complexes with pairs of sequences from SEQ ID NOs: 72 and 73, SEQ ID NOs: 62 and 63, SEQ ID NOs: 64 and 65, SEQ ID NOs: 66 and 67, SEQ ID NOs: 68 and 69, SEQ ID NOs: 70 and 71, and SEQ ID NOs: 74 and 75 ([003], see bottom of p. 5- top p. 6) wherein the polypeptide complex comprises the amino acid sequences according to SEQ ID NO: 72 and SEQ ID NO: 73 which are identical to instant SEQ ID NO: 1 and 2 (claim 61) as shown below:
Query Match 100.0%; Score 3414; Length 645;
Best Local Similarity 100.0%;
Matches 645; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSY 60
Qy 61 ADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLV 120
Qy 121 TVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQ 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 TVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQ 180
Qy 181 LVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 LVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYA 240
Qy 241 DSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 DSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTV 300
Qy 301 SSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPG 360
Qy 361 QAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGG 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 QAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGG 420
Qy 421 TKLTVLGGGGSDIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWYQQKTGKVPKFLIY 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 TKLTVLGGGGSDIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWYQQKTGKVPKFLIY 480
Qy 481 EASTLQSGVPSRFSGGGSGTDFTLTISSLQPEDVATYYCQNYNSAPFTFGPGTKVDIKRT 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 EASTLQSGVPSRFSGGGSGTDFTLTISSLQPEDVATYYCQNYNSAPFTFGPGTKVDIKRT 540
Qy 541 VAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSK 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 VAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSK 600
Qy 601 DSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 645
|||||||||||||||||||||||||||||||||||||||||||||
Db 601 DSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 645
Query Match 100.0%; Score 1199; Length 226;
Best Local Similarity 100.0%;
Matches 226; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVQLVESGGGVVQPGRSLRLSCAASGFAFSRYGMHWVRQAPGKGLEWVAVIWYDGSNKYY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVESGGGVVQPGRSLRLSCAASGFAFSRYGMHWVRQAPGKGLEWVAVIWYDGSNKYY 60
Qy 61 ADSVKGRFTISRDNSKNTQYLQMNSLRAEDTAVYYCARGGDFLYYYYYGMDVWGQGTTVT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ADSVKGRFTISRDNSKNTQYLQMNSLRAEDTAVYYCARGGDFLYYYYYGMDVWGQGTTVT 120
Qy 121 VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL 180
Qy 181 QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC 226
||||||||||||||||||||||||||||||||||||||||||||||
Db 181 QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC 226
Thus, the claims of ‘207 are directed towards a genus of which SEQ ID NO: 72 and 73 are obvious species.
The claims of ‘207 do not explicitly teach the characteristics:(a) at least one disulfide bond formed by a pair of cysteine residues in the first chain or the second chain or by a pair of cysteine residues in the first chain and the second chain; (b) a secondary structure composition comprising a P-sheet or a random coil; (c) at least one pyroglutamine in the second chain; (d) a melting temperature (Tm) between of about 65 °C to about 85 °C when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0 mg/mL in a buffer comprising 10 mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3 (e) a far UV circular dichroism peak at a wavelength between 190 nm and 205 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.1mg/mL in 10mM potassium phosphate buffer pH 7.0; (f) a far UV circular dichroism dip at a wavelength between 210 nm and 220 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.1mg/mL in 10mM potassium phosphate buffer pH 7.0; or (g) a near UV circular dichroism peak at a wavelength between 250 nm and 300 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0mg/mL in a buffer comprising 10mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3, the claims of the ‘207 application are silent. However, each of the properties a)-g) are inherent properties of the polypeptide complex consisting of SEQ ID NO: 1 and 2, because a protein with the same primary structure would be expected to have the same secondary structure, tertiary structure, and post-translational modifications provided it is made in a mammalian cell type. In order to determine the meaning of the claims to polypeptide SEQ ID NO: 1 and 2, the specification was consulted (MPEP §804.B.1). The specification discloses that the polypeptide may be made by expression in a host-expression vector system, and that the host may be for example a microorganism or a mammalian cell selected from a list ([194], [217-218]).
It would have been obvious for a person of ordinary skill in the art, before the effective filing date, to make the polypeptide complex using a mammalian host-expression vector system to benefit from a method of making the claimed polypeptide. As set forth in MPEP §2145 (II) “[m]ere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention”. Products of identical composition cannot have mutually exclusive properties. See MPEP § 2112. As evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 ““the advanced mammalian folding, secretion and post-translational apparatus is capable of producing antibodies indistinguishable from those in the human body with least concerns for immunogenic modifications” (p. 5 right column, “Mammalian Cells” section ¶1, emphasis is the Examiner’s). Thus, a polypeptide complex of SEQ ID NO: 1 and SEQ ID NO: 2 with the characteristics a)-g) as claimed is made obvious by the claims of ‘207 because the polypeptide complex comprising SEQ ID NO: 1 and SEQ ID NO: 2 of ‘207 would inherently possess all of the recited characteristics when made in a mammalian host-expression vector system.
Regarding dependent claims 4, 8, 19, 20, 21, 24, 28, 38-42, 44, 46,and 50-51, as described for claim 1, each of these characteristics would be an inherent property of the polypeptide complex consisting of 100% identity to SEQ ID NO: 1 and SEQ ID NO: 2 provided the polypeptide complex was produced in mammalian cells in order to produce the same folding and post-translational modifications. Thus, the claims directed at the particular disulfide bonds and positions of disulfide bonds (claims 19, 20, 21, 24, 28, 39-41) or lack thereof as free sulfhydryl (claim 38), the secondary and tertiary structures and resultant far UV and near UV circular dichroism peaks (claim 42, 46, 50-51), and melting temperatures would be characteristics inherently possessed by a polypeptide complex that has the same folding and post-translational modifications as the instantly claimed polypeptide complex.
Claims 1, 4, 8, 19-21, 24, 28, 38-42, 44, 46, 50-51, and 53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 11, 55, 136-145, and 150 of copending Application No. 19374607 (reference application) as evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 published 28 July 2013 (PTO-892 dated 1/20/2026). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of '607 make obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Regarding claims 1, 10, and 15, claims 11, 55, 136-145, and 150 of the ‘607 application teach an isolated polypeptide according to Formula I: A1-L1-P1 wherein A1 comprises a first antigen recognizing molecule that binds to CD3 comprising particular CDR sequences; P1 comprises a peptide that binds to A1 of SEQ ID NOs: 150-165; wherein L1 comprises a linking moiety that connects A1 to P1 and is a substrate for a tumor specific protease (claim 11). Claim 55 recites wherein the recombinant antibody or antigen binding fragment thereof further comprises an antigen binding domain. Claim 136 recites the antigen binding domain is a PSMA binding domain. Claims 137-145 recite wherein the isolated polypeptide sequence at least 90% identity to particular amino acid sequences that are at least 80% identical to instant SEQ ID NO: 1 and 2 (SEQ ID NOs: 230, 234, 232, 228; and SEQ ID NOs: 231, 235, 229, 233), for example claim 143 wherein the polypeptide complex comprises the amino acid sequences according to SEQ ID NO: 230 and SEQ ID NO: 231 which are 99.6 and 100% identical to instant SEQ ID NO: 1 and 2, respectively.
The claims of ‘607 do not explicitly teach the characteristics:(a) at least one disulfide bond formed by a pair of cysteine residues in the first chain or the second chain or by a pair of cysteine residues in the first chain and the second chain; (b) a secondary structure composition comprising a P-sheet or a random coil; (c) at least one pyroglutamine in the second chain; (d) a melting temperature (Tm) between of about 65 °C to about 85 °C when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0 mg/mL in a buffer comprising 10 mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3 (e) a far UV circular dichroism peak at a wavelength between 190 nm and 205 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.1mg/mL in 10mM potassium phosphate buffer pH 7.0; (f) a far UV circular dichroism dip at a wavelength between 210 nm and 220 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 0.1mg/mL in 10mM potassium phosphate buffer pH 7.0; or (g) a near UV circular dichroism peak at a wavelength between 250 nm and 300 nm when the isolated recombinant polypeptide complex is formulated at a concentration of 1.0mg/mL in a buffer comprising 10mM histidine buffer, 8% (w/v) Sucrose, 0.01% (w/v) polysorbate 20, pH 6.3, the claims of the ‘607 patent are silent. However, each of the properties a)-g) are inherent properties of the polypeptide complex consisting of SEQ ID NO: 1 and 2, because a protein with the same primary structure would be expected to have the same secondary structure, tertiary structure, and post-translational modifications provided it is made in a mammalian cell type. In order to determine the meaning of the claims to polypeptide SEQ ID NO: 1 and 2, the specification was consulted (MPEP §804.B.1). The specification discloses that the polypeptide may be made by expression in a host-expression vector system, and that the host may be for example a microorganism or a mammalian cell selected from a list ([194], [217-218]).
It would have been obvious for a person of ordinary skill in the art, before the effective filing date, to make the polypeptide complex using a mammalian host-expression vector system to benefit from a method of making the claimed polypeptide. As set forth in MPEP §2145 (II) “[m]ere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention”. Products of identical composition cannot have mutually exclusive properties. See MPEP § 2112. As evidenced by Frenzel, André, et. al. "Expression of recombinant antibodies." Frontiers in immunology 4 (2013): 217 ““the advanced mammalian folding, secretion and post-translational apparatus is capable of producing antibodies indistinguishable from those in the human body with least concerns for immunogenic modifications” (p. 5 right column, “Mammalian Cells” section ¶1, emphasis is the Examiner’s). Thus, a polypeptide complex of SEQ ID NO: 1 and SEQ ID NO: 2 with the characteristics a)-g) as claimed is made obvious by the claims of ‘607 because the polypeptide complex comprising SEQ ID NO: 1 and SEQ ID NO: 2 of ‘607 would inherently possess all of the recited characteristics when made in a mammalian host-expression vector system.
Regarding dependent claims 4, 8, 19, 20, 21, 24, 28, 38-42, 44, 46,and 50-51, as described for claim 1, each of these characteristics would be an inherent property of the polypeptide complex consisting of 100% identity to SEQ ID NO: 1 and SEQ ID NO: 2 provided the polypeptide complex was produced in mammalian cells in order to produce the same folding and post-translational modifications. Thus, the claims directed at the particular disulfide bonds and positions of disulfide bonds (claims 19, 20, 21, 24, 28, 39-41) or lack thereof as free sulfhydryl (claim 38), the secondary and tertiary structures and resultant far UV and near UV circular dichroism peaks (claim 42, 46, 50-51), and melting temperatures would be characteristics inherently possessed by a polypeptide complex that has the same folding and post-translational modifications as the instantly claimed polypeptide complex.
Response to Arguments
Applicant’s arguments filed 17 July 2026 have been fully considered but are not persuasive. Applicant argues that Frenzel (PTO-892 dated 1/20/2026) teaches that the same protein expressed in different expression systems can affect protein function (Remarks 7/17/2026 p. 9-10). Applicant additionally argues that other evidence e.g. Spencer et. al. (IDS dated 7/17/2026) teaches that a protein with the same primary structure does NOT necessarily have the same secondary structure, tertiary structure, and post-translational modifications when expressed in different expression systems (Remarks 7/17/2026 p. 10). This is not persuasive. MPEP §2112 teaches that “"[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer." Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977). In In re Crish, 393 F.3d 1253, 1258, 73 USPQ2d 1364, 1368 (Fed. Cir. 2004)”. The Examiner also notes that it is entirely routine to claim proteins by primary sequence and those proteins are considered to be both described and enabled for the entire genus of post-translational modifications that may result from the production of those proteins because making of proteins by expression in cell lines is considered to be routine in the art as described in Frenzel et. al. MPEP §2112 further states that "In relying upon the theory of inherency, the examiner must provide a basis in fact and/or technical reasoning to reasonably support the determination that the allegedly inherent characteristic necessarily flows from the teachings of the applied prior art." Ex parte Levy, 17 USPQ2d 1461, 1464 (Bd. Pat. App. & Inter. 1990) (emphasis in original). As described in the non-statutory double patenting rejections above, Frenzel et. al. teaches that “the advanced mammalian folding, secretion and post-translational apparatus is capable of producing antibodies indistinguishable from those in the human body with least concerns for immunogenic modifications” (p. 5 right column, “Mammalian Cells” section ¶1, emphasis is the Examiner’s). A person of ordinary skill in the art would understand the description by Frenzel of the antibodies that are “indistinguishable” from those in the human body to create a reasonable expectation that characteristics of instant SEQ ID NOs: 1 and 2 would be the same, so long as they are produced in mammalian cells as described in the instant specification. Thus, the Examiner has met the prima facie burden to show that the characteristics a)-g) for example the disulfide bonds, melting temperature, and far UV dichroism peak at a particular wavelength in a particular formulation are inherent characteristics and the burden is shifted to the Applicant to show that the prior art product do not necessarily or inherently possess the characteristics of the claimed product (MPEP §2112.V). Applicant is reminded that “"Products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present” (MPEP §2112.01.II). Applicant argues that Frenzel et. al. and Spencer et. al. show that production in different cell lines may result in different secondary or tertiary structure for the same primary sequence. However, the Examiner reminds the Applicant that the instant claims do not recite any structural components that would distinguish the instantly claimed protein from the prior art; rather, a person of ordinary skill in the art is left to speculate what structures other than the claimed primary sequence could result in the claimed properties. This suggests that if, en arguendo, Applicant was correct that the instantly claimed properties did not flow from the instantly claimed primary sequences, Applicant would not be enabled for the full scope of the instant claims because a person of ordinary skill in the art would not be able to determine without undue experimentation which methods of producing the instant protein would result in the claimed characteristics other than those made by the exact method of manufacturing in the instant specification. The Examiner notes that Applicant’s own specification describes a variety of mammalian cell systems “(e.g., COS, CHO, BH, HEK293, 293T, 3T3 cells)” [0247] without describing any subtypes of each beyond the particular CHO-K1 cells described in the working examples (See e.g. Example 2, [0285]). In addition, the scope of Frenzel and Spencer as cited is not sufficient to demonstrate that the instantly claimed primary sequence would not inherently possess the claimed characteristics because the examples are directed towards N-linked glycans and O-xylosylation, and there is no evidence of record that either of these types of post-translational modifications would alter the claimed characteristics a)-g). There is also no evidence of record of changes in disulfide bonds, beta sheets, random coils, and melting temperature by expression systems. The claims are not directed towards Applicants protein made by a particular method or expression system to restrict the claims to these characteristics if they were not inherent. The Examiner suggests amending the claims to include additional structural requirements of the recombinant polypeptide that would lead to the claimed characteristics and structurally distinguish the instantly claimed polypeptide from the patentably indistinct claims as described above or that the rejection may be overcome by filing terminal disclaimer(s) over the relevant patents and copending applications above.
Conclusion
No claims are allowed.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/KATHLEEN CUNNINGCHEN/ Examiner, Art Unit 1646
/GREGORY S EMCH/Supervisory Patent Examiner, Art Unit 1678
