DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2 Applicant's amendment, filed on 07/17/2025, is acknowledged.
3. Claims 1-18 are pending.
4. Applicant’s election with traverse of Group I, claims 1-8 directed to anti-fibronectin (FN) antibodies, filed on 12/23/2025, is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.03(a)).
5. Claims 9-18 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions.
6. Claims 1-8 are under examination as they read on anti-fibronectin (FN) antibodies.
7. Applicant’s IDS, filed 07/17/2025, is acknowledged.
8. 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.
9. Claims 1-8 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 and 27-30 of copending Application No. 18573975 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the `975 application claims an H5-IgG1 anti-FN antibody comprising the VH-CDRs of SEQ ID NO: 24-25-27 (see SEQ ID NOs: 8-10-12 of the `975) and the VL-CDRs of SEQ ID NO: 28-29-30 (see SEQ ID NO: 20-22-24 of the `975).
Alignment of claimed VH-CDRs of SEQ ID NO: 24-25-27 with referenced SEQ ID NOs: 2/4
Qy 1 SYAM--------------SDIYDGGGTNYADSVKG------------------------- 21
|||| |||||||||||||||||
Db 31 SYAMSWVRQAPGKGLEWVSDIYDGGGTNYADSVKGRFTTSRDNSKNTLYLQMNSLRAEDT 90
Qy 22 -------TADNFD 27
||||||
Db 91 AVYYCTKTADNFD 103
Alignment of claimed VL-CDRs of SEQ ID NO: 28-29-30 with referenced SEQ ID NOs:14/ 16.
Qy 1 RASQSISSYLN---------------AASTLQS--------------------------- 18
||||||||||| |||||||
Db 24 RASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDFTLTISSLQPEDF 83
Qy 19 -----QQANSAPTT 27
|||||||||
Db 84 ATYYCQQANSAPTT 97
Alignment of claimed aa 1-113 of SEQ ID NO: 2 with referenced SEQ ID NO: 4 (VH)
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYA 60
Qy 61 DSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTV 113
|||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 DSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTV 113
Alignment of claimed aa 132-237 of SEQ ID NO: 2 with referenced SEQ ID NO: 16 (VL)
Qy 132 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPS 191
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPS 60
Qy 192 RFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEIKR 239
||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEIKR 108
The claims of the `975 anticipate the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
10. Claims 1-8 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 of U.S. Patent No. 12410245 B1. Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of the `245 patent claims antibody comprising an amino acid sequence selected from the group consisting of SEQ ID NOs: 6 and 9-12, or an antigen-binding fragment thereof, wherein the antigen-binding fragment thereof selectively binds to a conformational state of fibronectin (FN) comprising FnIII9-4G-10 (4G). The `245 patent claim an anti-FN antibody comprising VH-CDRs of SEQ ID NO: 24-25-27 (see SEQ ID NOs: 6, 9, 11-12 of the `245 pat) and the VL-CDRs of SEQ ID NO: 28-29-30 (see SEQ ID NO:6, 9-12 of the `245 pat).
Alignment of VH-CDRs of SEQ ID NO: 24-25-27 with patented SEQ ID NOs: 6, 9, 11-12.
Qy 1 SYAM--------------SDIYDGGGTNYADSVKG------------------------- 21
|||| |||||||||||||||||
Db 31 SYAMSWVRQAPGKGLEWVSDIYDGGGTNYADSVKGRFTTSRDNSKNTLYLQMNSLRAEDT 90
Qy 22 -------TADNFD 27
||||||
Db 91 AVYYCTKTADNFD 103
Alignment of VL-CDRs of SEQ ID NO: 28-29-30 with patented SEQ ID NO:6, 9-12.
Qy 1 RASQSISSYLN---------------AASTLQS--------------------------- 18
||||||||||| |||||||
Db 155 RASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDFTLTISSLQPEDF 214
Qy 19 -----QQANSAPTT 27
|||||||||
Db 215 ATYYCQQANSAPTT 228
Alignment of claimed 132-237 of SEQ ID NO: 2 with referenced SEQ ID NO: 6, 9-12
Qy 1 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 132 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPS 191
Qy 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEI 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 192 RFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEI 237
Alignment of claimed 1-113 of SEQ ID NO: 2 with referenced SEQ ID NO: 12
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYA 60
Qy 61 DSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTV 113
|||||||||||||||||:|||||||||||||||||||||||||||||||||||
Db 61 DSVKGRFTTSRDNSKNTMYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTV 113
The claims of `245 patent anticipate claim 1 and 3-9 and render claim 2 obvious.
11. 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.
12. Claims 1-2 and 4-8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Cao et al (ACS Nano. 2017 July 25; 11(7): 7110–7117. doi:10.1021/acsnano.7b02755, IDS #95) as is evidenced by the specification at page 12, lines 24-25.
Cao et al teach the anti-FN antibody, clone H5 displayed high selectivity toward the extended (FnIII9-4G-10), but not the native, stabilized (FnIII9*10) conformation (Supporting Information Figure S2) (see page 3, 1st ¶ and 2nd ¶, Figure 2A,B). Clone 5 is a conformation-sensitive single-chain antibody to the integrin-binding FnIII9-10 domain of FN and demonstrated its mechano-sensitive binding to FN in multiple model systems in vitro and ex vivo (page 6, last ¶). Further, Cao et al teach the use of H5 scFv as probel pathologic ECMs, specifically tumor stroma and fibrotic ECMs which contain highly contractile myofibroblasts (see page 5, last ¶). Claims 7-8 are included because Cao et al teach that primary antibodies diluted in Pblec buffer (composition with excipient) (see Supplement on page 9, under On postnatal mouse retina) Also, Cao et al, Suppl teaches that the H5 antibody in 100ng/ml composition (page 7, 2nd ¶).
H5 scFv is the claimed SEQ ID NO: 2 as is evidence by the instant specification at pae 12, lines 24-25 that SEQ ID NO: 2 is the amino acid sequences of the H5 scFv.
Claim 4 is included because Cao et al teaches the use of the single fold scFv library I (Tomlinoson I) to obtain H5 scFv (see Fig. 2 and 4 in the Suppl). Tomlinson I is human single fold scFv library.
Although the reference does not teach the sequences for the CDRs from the clone H5, these are intrinsic properties of the Clone H5. Also, it is an inherent property of the H5 immunoglobulin light and heavy chains to bind to the same antigen as the original antibody. Therefore, the light and heavy chain CDRs instantly claimed are unpatentable over the prior art as the sequences are intrinsic properties of the antibody.
The Courts have held that there is no requirement that those of ordinary skill in the art know of the inherent property. See MPEP 2131.01(d) and MPEP 2112 - 2113.
The issues presented herein are akin to the holding in In re Crish, 73 USPQ2d 1364 (CAFC 2004) where the Federal Circuit held that the claimed promoter sequence obtained by sequencing a prior art plasmid that was not previously sequenced was anticipated by the prior art plasmid which necessarily possessed the same DNA sequence as the claimed oligonucleotides. The court stated that “just as the discovery of properties of a known material does not make it novel, the identification and characterization of a prior art material also does not make it novel.”
Like the references in Crish, the prior art of Cao et al reference discloses a material containing the same sequence recited in the claims. It is undisputed that Cao discloses an antibody that contains the amino acids recited in Applicant’s claims. That disclosure is anticipatory, even if it was not until the present application that Applicants characterized Clone H5 by its amino acid sequences.
The reference teachings anticipate the instant claims.
12. Claims 1-2, 4-8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Lizhi Cao (Dissertation May 2014), as is evidenced by the specification on page 12, lines 24-25.
Cao teaches the use of H5 scFv antibody in fibronectin targeting in diagnosis and monitoring of disease progression in mouse model of pulmonary fibrosis (page xviii) and in vivo imaging (page 12). Cao found that the H5 antibody clone, which preferentially targeted to FnIII9-4G-10, was found to be particular effective in blocking Fn-integrin αVβ3 interactions (see page 47, 1st ¶ under Discussion and Conclusions). Cao teaches that H5 scFv was obtained using human single fold (scFv) antibody (page 38, 2nd ¶) (Tomlinson I) (see Table 2 and page 39 tope ¶).
H5 scFv is the claimed SEQ ID NO: 2 as is evidence by the instant specification at page 12, lines 24-25 that SEQ ID NO: 2 is the amino acid sequences of the H5 scFv.
Claim 4 is included because Cao teaches the use of the single fold scFv library I (Tomlinson I) to obtain H5 scFv (see Fig. 2& 4 in the Suppl). Tomlinson I is human single fold scFv library.
Claims 7-8 are included because the Cao teaches dilutions of scFv antibodies were prepared in binding buffer (10mM HEPES, 150mM NaCl, 0.0001% Triton-X 100, pH 7.4) in concentrations ranging from 0.5μg/mL to 120μg/mL, and injected over the chip surface using kinetic injections at 30μL/min, with a 10min dissociation time (see page 36, 2nd ¶).
Although the reference does not teach the sequences for H5 scFv and its CDRs, these are intrinsic properties of the H5 scFv. The Courts have held that there is no requirement that those of ordinary skill in the art know of the inherent property. See MPEP 2131.01(d) and MPEP 2112 - 2113.
The issues presented herein are akin to the holding in In re Crish, 73 USPQ2d 1364 (CAFC 2004) where the Federal Circuit held that the claimed promoter sequence obtained by sequencing a prior art plasmid that was not previously sequenced was anticipated by the prior art plasmid which necessarily possessed the same DNA sequence as the claimed oligonucleotides. The court stated that “just as the discovery of properties of a known material does not make it novel, the identification and characterization of a prior art material also does not make it novel.”
Like the references in Crish, the prior art of Cao dissertation discloses a material containing the same sequence recited in the claims. It is undisputed that Cao discloses a H5 scFv that contains the amino acids recited in Applicant’s claims. That disclosure is anticipatory, even if it was not until the present application that Applicants characterized H5 scFv by its amino acid sequences.
The reference teachings anticipate the claimed invention.
13. Claims 1-2 and 4-8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Leandro Moretti (Thesis, December 2016), as is evidenced by the specification on page 12, lines 24-25.
Moretti teaches an antibody fragment (scFv), termed H5, capable of selectively binding to the integrin binding domain of fibronectin (Fn) under a strained configuration, typically due to forces exerted on the extracellular matrix (ECM) by cells (page x, 1st ¶). Moretti teaches that pIT2 vector sequence provide the complete DNA sequence of H5 was recovered (page x, 3rd ¶). Moretti teaches that the H5 DNA was recombined with error prone PCR, to generate a library of random mutants, which was transformed into a stable, E. coli strain. This library will be panned on the targets again through phage display in order to find an improved version of H5, defined by more selective binding to the extended conformation of the integrin binding domain of Fn (page x, 3rd ¶). Moretti teaches that the H5 scFv antibody through phage display from the (human) Tomlinson I + J libraries (page 18, 1st ¶).
Importantly, Moretti teaches that the newly designed primers allowed amplification of the insert DNA of both H5 and the anti-ubiquitin scFv, provided with the libraries as a positive control during the phage display process. The PCR products of both scFv were sequenced, thus enabling the reconstruction of H5 (page 18, 1st ¶). Additionally, two new stocks of H5 bacteria were identified, one prepared on May 2012 and another on July 2012 (page 21, top ¶).
Moretti teaches methods employed to generate potentially beneficial mutations in the H5 antibody fragments are described in this section (page 31, 1st ¶). The library is now ready to be screened through phage display in order to identify an improved version of the H5 probe (see page 39). Given that our past H5 antibody version demonstrated such effectiveness in vitro, the new H5 would be ready for in vivo studies, bar functionalization to improve circulation time and organ targeting (page 42, 1st ¶). The new H5 shows even greater potential for not only imaging and diagnostic application in fibrosis, but also for targeting therapeutic moieties on Fn, thus becoming a prime candidate for future theragnostic assays in animal models (page 42, 2nd ¶).
Appendix A show nucleic acid sequences of H5 recovered. The amino acid of the recovered H5 sequences is
MKYLLPTAAAGLLLLAAQPAMAEVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYADSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTVSSGGGGSGGGGSGGGGSTDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEIKRAAAHHHHHHGAAEQKLISEEDLNGAA
Alignment of claimed SEQ ID NO: 2 with recovered H5 from Moretti.
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 23 EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYA 82
Qy 61 DSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTVSSGGGGS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 83 DSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTVSSGGGGS 142
Qy 121 GGGGSGGGGSTDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIY 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 143 GGGGSGGGGSTDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIY 202
Qy 181 AASTLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEIKRA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 203 AASTLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEIKRA 262
Qy 241 AA 242
||
Db 263 AA 264
Appendix A show nucleic acid sequences of Codon optimized portion. The amino acid of the recovered H5 sequences is
MKYLLPTAAAGLLLLAAQPAMAEVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYADSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTVSSGGGGSGGGGSGGGGSTDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEIKRX
gBlock used for ePCR
MKYLLPTAAAGLLLLAAQPAMAEVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSDIYDGGGTNYADSVKGRFTTSRDNSKNTLYLQMNSLRAEDTAVYYCAKTADNFDYWGQGTLVTVSSGGGGSGGGGSGGGGSTDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSAPTTFGQGTKVEIKRAAAHHHHHHX
Moretti teaches that Fig. 4 show diabody (bispecific), triabody (trivalent) and tetrabody (tetravalent).
Claims 7-8 are included because Moretti teaches that several dilutions of the scFv fragments will be prepared in binding buffer (page 41, 1st ¶).
The reference teachings anticipate the claimed invention.
14. 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.
15. Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Cao et al (ACS Nano. 2017 July 25; 11(7): 7110–7117, IDS #95) or Lizhi Cao (Dissertation May 2014) or Moretti (Thesis, December 2016), as is evidenced by the specification on page 12, lines 24-25, as applied to claims 1-2 and 4-8, above, and further in view of Bujak et al (Methods Mol Biol. 2014:1131:315-34. doi: 10.1007/978-1-62703-992-5_20).
The teachings of Cao references and Moretti have been discussed, supra.
The reference teachings differ from the claimed invention only in the recitation of the anti-FN antibody or antigen binding fragment is an immunoglobulin comprising at least a portion of an immunoglobulin constant region (Fc).
Bujak et al teach the scFv-Fc format allows for rapid characterization of candidate scFvs isolated from phage display libraries before conversion into a full-length IgG. This format offers several advantages over the phage display-derived scFv, including bivalent binding, longer half-life, and Fc-mediated effector functions. Bujak provides a detailed method which describes the cloning, expression, and purification of an scFv-Fc fragment, starting from scFv fragments obtained from a phage display library. This method facilitates the rapid screening of candidate antibodies, prior to a more time-consuming conversion into a full IgG format. Alternatively, the scFv-Fc format may be used in the clinic for therapeutic applications (abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to format the referenced H5 scFv taught by Cao et al and Moretti references into scFv-Fc format taught by Bujak et al which offers several advantages over the phage display-derived scFv, including bivalent binding, longer half-life, and Fc-mediated effector functions.
From the combined teachings of the references, it is apparent that one of ordinary skill in the art would have had a reasonable expectation of success in producing the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the references, especially in the absence of evidence to the contrary.
16. The following is a quotation of 35 U.S.C. 112(a) (Pre-AIA 35 U.S.C. 112, first paragraph):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
17. Claims 1-8 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. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 1 reads on an antibody comprising CDRs identified as having “an amino acid sequence of” the indicated SEQ ID Nos. , the claim reads on antibodies that comprise less than the full sequences of the indicated CDRs. It is known in the art that variations to the CDR sequences often impact the ability of an antibody to bind to a particular antigen. In the present case, there is no disclosure of any antibodies comprising less than the full length CDRs of the indicated SEQ ID NOs, much which of such variant CDR sequences would retain the fibronectin specificity of the original antibody.
Claims 1 recites the use of open language “comprising” and “amino acid sequence of SEQ ID NO: X”. the phrase results in an fibronectin antibody comprising the claimed VH sequence, VH and VL sequences or any portion of the claimed “SEQ ID NO: X”. The claim terminology “an amino acid sequence of SEQ ID NO: X, does not place size limits on the VH and VL but rather reads on any portion of the claimed VH and VL of SEQ ID NO. The VH and VL are generic with respect to size, encompassing anything from dimers on up to the full size of the claimed SEQ ID NOs. It is suggested that the phrases “an amino acid sequence of SEQ ID NO: X” be changed to “the amino acid sequence of SEQ ID NO: X” to overcome this rejection.
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the written description inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116.). Consequently, Applicant was not in possession of the instant claimed invention. See University of California v. Eli Lilly and Co. 43 USPQ2d 1398.
Applicant is invited to point to clear support or specific examples of the claimed invention in the specification as-filed.
18. No claim is allowed.
19. Any inquiry concerning this communication or earlier communications from the examiner should be directed to MAHER M HADDAD whose telephone number is (571)272-0845. The examiner can normally be reached on Monday-Friday from7:00AM to 4:30PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Misook Yu, can be reached at telephone number 571-272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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January 26, 2026
/MAHER M HADDAD/ Primary Examiner, Art Unit 1644