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 .
1. Claims 24-43 are pending and being examined.
Specification/ Claim Objections
2. The specification and claims 25, 26, 29, 30, 33, 34, 37, and 38 are objected to because of the following informalities: the specification and claims state SEQ ID NOs: 92, 93, and 94 that are all represented by a dummy sequence “000” in the sequence listing. Therefore, referring to the SEQ ID NO does not provide the sequence information. Applicants are required to spell out the sequence wherever SEQ ID NOs: 92, 93, and 94 are stated, wherein SEQ ID NO:92 is SAS, SEQ ID NO:93 is SAR, and SEQ ID NO:94 is SAX where X can be S or R. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
3. Claims 24, 27, 28, 31, 32, 35, 36, 39, and 40-43 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. This is a WRITTEN DESCRIPTION rejection.
The claims are drawn to:
an antigen-binding molecule comprising a heavy chain variable (VH) region and a light chain variable (VL) region, wherein the antigen-binding molecule specifically binds to HER3, and wherein binding to HER3 comprises contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:229; a nucleic acid encoding the antibody, a cell comprising the nucleic acid encoding the antibody; and
a method of treating a cancer in a subject, comprising administering to a subject a therapeutically effective amount of an antigen-binding molecule comprising a heavy chain variable (VH) region and a light chain variable (VL) region, wherein the antigen-binding molecule specifically binds to HER3, and wherein binding to HER3 comprises contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:229.
Thus, the claims identify the antigen-binding molecule by function only, where the function is to:
bind HER3 and come into contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:229; and
treat cancer in a subject.
No antigen-binding molecule or antibody structure is recited.
Dependent claims 27, 31, 35, and 39 recite that the antibody/antigen-binding molecule comprises a partial structure of a VH region comprising an amino acid sequence having at least 70% sequence identity to a defined SEQ ID NO; and a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of a defined SEQ ID NO. Thus, these claims identify the antibody by function with partial structure, wherein the partial structure comprises up to 30% sequence discrepancy anywhere in the claimed VH and VL sequences including the CDRs, encompassing a vast genus of antibody variants.
The instant specification discloses seventeen total 10D1 antibody and 10D1-derived clones comprising defined pairs of VH and VL sequences in the Table of Example 1:
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Thus, the instant specification describes seventeen antibodies that function as claimed, wherein each of the seventeen antibodies comprises a defined single set of VH and VL sequences. The specification fails to disclose the sequence of any variants comprising up to 30% sequence discrepancy from the claimed VH and VL sequences that possess the function of binding HER3 and coming into contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:229, and treating cancer in a subject.
To provide adequate written description and evidence of possession of the claimed antibody genus, the instant specification can structurally describe representative antibody variants having up to 30% discrepancy in the claimed VH and VL SEQ ID NOs and that function to bind HER3 and come into contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:229 and treat cancer, or describe structural features common to the members of the genus, which features constitute a substantial portion of the genus. Alternatively, the specification can show that the claimed invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics (see University of California v. Eli Lilly and Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) and Enzo Biochem, Inc. V. Gen-Probe Inc.). A disclosure that does not adequately describe a product itself logically cannot adequately describe a method of using that product.
Although Applicants may argue that it is possible to screen for antibodies that bind HER3 and function as claimed, the court found in (Rochester v. Searle, 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention. “As we held in Lilly, “[a]n adequate written description of a DNA … ‘requires a precise definition, such as by structure, formula, chemical name, or physical properties,’ not a mere wish or plan for obtaining the claimed chemical invention.” 119 F.3d at 1566 (quoting Fiers, 984 F.2d at 1171). For reasons stated above, that requirement applies just as well to non-DNA (or RNA) chemical inventions.” Knowledge of screening methods provides no information about the structure of any future antibodies yet to be discovered that may function as claimed. The HER3 antigen and epitope SEQ ID NO:229 provide no information about the structure of an antibody that binds to them.
In this case, the only factor present in the claims is a recitation of the antibody functions as listed above or recitation of functions with partial structure. The instant specification fails to describe structural features common to the members of the genus, which features constitute a substantial portion of the genus because the instant specification discloses only seventeen defined exemplary antibody VH and VL sequence pairs that function as claimed. A definition by function does not suffice to define the genus because it is only an indication of what the antibody does, rather than what it is. Applicants have not established any reasonable structure-function correlation with regards to the sequences in the variable domains or CDRs that can be altered up to 30% and still maintain the claimed functions of binding HER3 at epitope SEQ ID NO:229 and treating cancer. The instant specification also fails to describe a representative number of variant antibody sequences for the genus of variant antibodies that function as claimed. One could not readily envision members of the broadly claimed genus required to practice the invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus required to make and practice the claimed invention.
Given the lack of representative examples to support the full scope of the claimed antibodies and those used in the claimed method, and lack of reasonable structure-function correlation with regards to what sequences can be altered up to 30% and maintain the claimed functions, the present claims lack adequate written description. Thus, the specification does not provide an adequate written description of antibodies that bind HER3 at epitope SEQ ID NO:229 that is required to practice the claimed invention. Since the specification fails to adequately describe the product to which the claimed method uses, it also fails to adequately describe the method.
Examiner Suggestion: Amend independent claims to recite and require the antigen-binding molecule/ antibody comprise at least the six heavy and light chain CDR SEQ ID NOs of claims 25 or 26 required to function as claimed. Delete the phrases “at least 70% amino acid sequence identity to” in claims 27, 31, 35, and 39.
Claim Rejections - 35 USC § 102
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.
4. Claim(s) 24, 36, and 40 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Boyd-Kirkup et al (Proceedings of the American Association for Cancer Research Annual Meeting, 2017: 2017 April 1-5; Washington DC. Philadelphia (PA): AACR; Cancer Research, 2017; 77(13 Suppl); Abstract 24) (IDS).
Boyd-Kirkup et al teach anti-HER3 antibody HMBD001 (10D1) and method of treating gastric cancer in a subject comprising administering to the subject a therapeutically effective amount of the antibody.
As evidenced by the published instant specification, antibody 10D1 inherently binds to HER3 by contacting residues in the region of SEQ ID NO:229:
[1433] The site of HER3 to which 10D1 and 10D1-derived clones was determined to bind corresponds to positions 218 to 235 of the amino acid sequence of human HER3 (as shown e.g. in SEQ ID NO:1); the amino acid sequence for this region of HER3 is shown in SEQ ID NO:229.
5. Claim(s) 24 and 36 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Thakker et al (European Journal of Cancer, November 13, 2018; 103S1; e36-e37; Poster Session; abstract 87) (IDS).
Thakker et al teach HMBD001-10D1 anti-HER3 antibody that blocks the heterodimerization of HER3 and teach the antibody has already been administered to subjects having cancer, demonstrating potent tumor growth inhibition across multiple tumor models that express HER3. Thakker et al teach administering 10D1 antibody to humans for clinical treatment of cancer.
As evidenced by the published instant specification, antibody 10D1 inherently binds to HER3 by contacting residues in the region of SEQ ID NO:229:
[1433] The site of HER3 to which 10D1 and 10D1-derived clones was determined to bind corresponds to positions 218 to 235 of the amino acid sequence of human HER3 (as shown e.g. in SEQ ID NO:1); the amino acid sequence for this region of HER3 is shown in SEQ ID NO:229.
6. Claim(s) 24, 28, 32, 36, 40, 41, and 42 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by WO 2012/059224, Aurisicchio, published May 2012.
Aurisicchio teaches monoclonal antibodies comprising VH and VL domains that bind to HER3 extracellular epitopes, including epitopes CFGPNPNQ (SEQ ID NO: 38), FGPNPNQC (SEQ ID NO: 39) or GPNPNQCC (SEQ ID NO: 40), CFGPNPNQC (SEQ ID NO: 46) or FGPNPNQCC (SEQ ID NO: 47), and CFGPNPNQCC (SEQ ID NO: 53) (p. 22-23; Figure 10). All of these sequences have 100% identity within instant SEQ ID NO:229 (CFGPNPNQCCHDECAGGC), therefore, the antibodies taught by Aurisicchio necessarily bind to HER3 and contact one or more residues of the region of HER3 shown in in instant SEQ ID NO:229.
Aurisicchio teaches nucleic acids encoding the antibodies and transfecting cells to express and produce the antibodies (Examples 9, 11, and 12).
Aurisicchio teaches administering the antibodies to subjects to treat cancer including pancreatic cancer and breast cancer (Examples 6-8). Aurisicchio teaches administering the antibodies in combination with HERCEPTIN™ (trastuzumab) anti-HER2 antibody to enhance treatment of cancer (Example 8).
Claim Rejections - 35 USC § 103
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.
7. Claim(s) 28 and 32 are rejected under 35 U.S.C. 103 as being unpatentable over Thakker et al (European Journal of Cancer, November 13, 2018; 103S1; e36-e37; Poster Session; abstract 87).
Thakker et al teach HMBD001-10D1 anti-HER3 antibody that blocks the heterodimerization of HER3 and demonstrates potent tumor growth inhibition across multiple tumor models that express HER3. Thakker et al teach the antibody shows excellent manufacturing ability including expression titers, stability, and purity. Thakker et al teach the antibody demonstrates over 90% efficacy in pre-clinical models known to be refractory to existing EGFR family therapy. Thakker et al teach in-human clinical trials of the antibody to treat cancer are planned.
As evidenced by the published instant specification, antibody 10D1 inherently binds to HER3 by contacting residues in the region of SEQ ID NO:229:
[1433] The site of HER3 to which 10D1 and 10D1-derived clones was determined to bind corresponds to positions 218 to 235 of the amino acid sequence of human HER3 (as shown e.g. in SEQ ID NO:1); the amino acid sequence for this region of HER3 is shown in SEQ ID NO:229.
Although Thakker et al do not teach nucleic acids or cells encoding the 10D1 antibody, it would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to produce nucleic acids and cells expressing the antibody because Thakker et al teach the need to produce the antibody for therapeutic application and teach the antibody already successfully shows excellent manufacturing ability including expression titers, stability, and purity which requires nucleic acids and cells encoding/expressing the antibody.
8. Claim(s) 24, 28, 32, 36, 40-43 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2012/059224, Aurisicchio, published May 2012; in view of WO 2008/100624, Schoebert et al, published May 2008.
Aurisicchio teaches monoclonal antibodies comprising VH and VL domains that bind to HER3 extracellular epitopes, including epitopes CFGPNPNQ (SEQ ID NO: 38), FGPNPNQC (SEQ ID NO: 39) or GPNPNQCC (SEQ ID NO: 40), CFGPNPNQC (SEQ ID NO: 46) or FGPNPNQCC (SEQ ID NO: 47), and CFGPNPNQCC (SEQ ID NO: 53) (p. 22-23; Figure 10; claim 21). All of these sequences have 100% identity with instant SEQ ID NO:229 (CFGPNPNQCCHDECAGGC), therefore, the antibodies taught by Aurisicchio necessarily bind to HER3 and contact one or more residues of the region of HER3 shown in in instant SEQ ID NO:229.
Aurisicchio teaches the anti-HER3 antibodies have one or more of the following anti-cancer functions (claim 20, p. 33-34):
i. inhibition of heregulin, epiregulin, betacellulin, epigen or biregulin-mediated signalling through ErbB3;
ii. inhibition of proliferation of cells expressing ErbB3;
iii. the ability to decrease levels of ErbB3 on cell surfaces;
iv. inhibition of VEGF secretion of cells expressing ErbB3;
v. inhibition of the migration of cells expressing ErbB3;
vi. inhibition of spheroid growth of cells expressing ErbB3;
vii a binding specificity to ErbB3 of 20 nM or less, and/or
viii. inhibits homo- and/or hetero-dimerization of ErbB3.
Aurisicchio teaches nucleic acids encoding the antibodies, transfecting cells to express and produce the antibodies, and hybridoma cells producing the antibodies (Examples 2, 9, 11, and 12).
Aurisicchio teaches administering the antibodies to subjects to treat cancer including pancreatic cancer and breast cancer (Examples 6-8; Figure 6). Aurisicchio teaches administering the antibodies in combination with HERCEPTIN™ (trastuzumab) anti-HER2 antibody to enhance treatment of cancer (Example 8). Aurisicchio suggests treating cancer with chemotherapeutics (p. 3) and suggests combining their antibody with an anti-neoplastic agent (p. 34).
Aurisicchio exemplifies making monoclonal antibody “A3” comprising VH and VL domains that bind to epitope QCNGHCFGPNPNQCC (SEQ ID NO:68) (Examples 1, 2, and 10), wherein the epitope comprises the N-terminal CFGPNPNQCC sequence of instant SEQ ID NO:229 (CFGPNPNQCCHDECAGGC), therefore is expected to bind to amino acid residues found in instant SEQ ID NO:229, however, Aurisicchio does not explicitly teach where the antibody makes contact with this epitope or isolate antibodies binding exclusively to epitope SEQ ID NOs:38-40, 46, 47, and 53. Aurisicchio does not teach additionally administering docetaxel to treat cancer.
Schoebert also teaches producing monoclonal antibodies against the HER3 extracellular domain wherein the antibodies have any of the following anti-cancer functions (claim 2):
(i) inhibition of heregulin, epiregulin, betacellulin, epigen or biregulin- mediated signaling through ErbB3 ;
(ii) inhibition of proliferation of cells expressing ErbB3;
(iii) the ability to decrease levels of ErbB3 on cell surfaces;
(iv) inhibition of VEGF secretion of cells expressing ErbB3 ;
(v) inhibition of the migration of cells expressing ErbB3; and/or
(vi) inhibition of spheroid growth of cells expressing ErbB3.
Schoebert also teaches compositions comprising the antibodies, nucleic acids encoding the antibodies (p. 4, 20-22, 38), and routine methods of making the antibodies by immunization of mammals, isolation of hybridoma cells producing the antibodies, isolating antibody clones from phage display, sequencing the antibodies, and transfecting cells to express the antibodies (p. 29-33; Example 1).
Schoebert teaches methods of treating cancer in a subject by administering the anti-HER3 antibody in combination with known anti-cancer agents, including docetaxel trastuzumab, and cetuximab, and treating breast and pancreatic cancer (p. 5, 22-29, 44; Example 9; claims 44-53).
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to produce antibodies against SEQ ID NOs:38-40, 46, 47, and 53 of Aurisicchio, and produce nucleic acids and cells expressing the antibodies. One would have been motivated to and have a reasonable expectation of success to because: (1) Aurisicchio specifically suggests doing so; and (2) Aurisicchio and Schoebert teach and demonstrate methods of producing antibodies to HER3 epitopes, isolating their encoding nucleic acid, and expressing them in cells is routine and successfully practiced.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer docetaxel in the method of treating cancer taught by Aurisicchio. One would have been motivated to and have a reasonable expectation of success to because: (1) Aurisicchio suggests combining anti-cancer agents with their antibody for the treatment of cancer and demonstrates that adding an anti-cancer agent to their anti-HER3 antibody improved therapeutic efficacy; (2) Aurisicchio suggests administering chemotherapeutic to treat cancer; and (3) Schoebert teaches docetaxel is a known chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. The anti-HER3 antibody of Aurisicchio and chemotherapeutic docetaxel are established anti-cancer agents and are expected to predictably treat cancer together.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
9. Claims 24-43 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-25 of U.S. Patent No. 10,662,241 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al.
Although the claims at issue are not identical, they are not patentably distinct from each other because the US Patent is claiming and antigen-binding molecule comprising a VH and VL region comprising the same CDR sequences instantly claimed that bind to HER3 epitope SEQ ID NO:229, a nucleic acid encoding the antigen-binding molecule, a cell expressing the antigen-binding molecule, and method of treating cancer in a subject comprising administering the antigen-binding molecule, wherein the cancer comprises cells expressing an EGFR family member, a cancer comprising cells expressing HER3, a solid tumor, breast cancer, and more, rendering obvious instant claims 24-40. The US Patent claims:
1. An antigen-binding molecule that specifically binds to HER3, comprising:
(i) a heavy chain variable (VH) region having the following CDRs:
HC-CDR1 having the amino acid sequence of SEQ ID NO:41
HC-CDR2 having the amino acid sequence of SEQ ID NO:45
HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and
(ii) a light chain variable (VL) region having the following CDRs:
LC-CDR1 having the amino acid sequence of SEQ ID NO:88
LC-CDR2 having the amino acid sequence of SEQ ID NO:92
LC-CDR3 having the amino acid sequence of SEQ ID NO:95.
2. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises:
a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and
a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83.
3. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises:
a VH region having the following framework regions (FRs):
HC-FR1 having the amino acid sequence of SEQ ID NO:53
HC-FR2 having the amino acid sequence of SEQ ID NO:59
HC-FR3 having the amino acid sequence of SEQ ID NO:66
HC-FR4 having the amino acid sequence of SEQ ID NO:71.
4. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises:
a VL region having the following framework regions (FRs):
LC-FR1 having the amino acid sequence of SEQ ID NO:104
LC-FR2 having the amino acid sequence of SEQ ID NO:110
LC-FR3 having the amino acid sequence of SEQ ID NO:120
LC-FR4 having the amino acid sequence of SEQ ID NO:125.
5. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171.
6. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177.
7. A nucleic acid, or a plurality of nucleic acids, encoding an antigen-binding molecule that specifically binds to HER3, wherein the antigen-binding molecule comprises:
(i) a heavy chain variable (VH) region having the following CDRs:
HC-CDR1 having the amino acid sequence of SEQ ID NO:41
HC-CDR2 having the amino acid sequence of SEQ ID NO:45
HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and
(ii) a light chain variable (VL) region having the following CDRs:
LC-CDR1 having the amino acid sequence of SEQ ID NO:88
LC-CDR2 having the amino acid sequence of SEQ ID NO:92
LC-CDR3 having the amino acid sequence of SEQ ID NO:95.
8. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises:
a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and
a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83.
9. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises:
a VH region having the following framework regions (FRs):
HC-FR1 having the amino acid sequence of SEQ ID NO:53
HC-FR2 having the amino acid sequence of SEQ ID NO:59
HC-FR3 having the amino acid sequence of SEQ ID NO:66
HC-FR4 having the amino acid sequence of SEQ ID NO:71.
10. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises:
a VL region having the following framework regions (FRs):
LC-FR1 having the amino acid sequence of SEQ ID NO:104
LC-FR2 having the amino acid sequence of SEQ ID NO:110
LC-FR3 having the amino acid sequence of SEQ ID NO:120
LC-FR4 having the amino acid sequence of SEQ ID NO:125.
11. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171.
12. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177.
13. A cell comprising a nucleic acid, or a plurality of nucleic acids, encoding an antigen-binding molecule that specifically binds to HER3, wherein the antigen-binding molecule comprises:
(i) a heavy chain variable (VH) region having the following CDRs:
HC-CDR1 having the amino acid sequence of SEQ ID NO:41
HC-CDR2 having the amino acid sequence of SEQ ID NO:45
HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and
(ii) a light chain variable (VL) region having the following CDRs:
LC-CDR1 having the amino acid sequence of SEQ ID NO:88
LC-CDR2 having the amino acid sequence of SEQ ID NO:92
LC-CDR3 having the amino acid sequence of SEQ ID NO:95.
14. The cell according to claim 13, wherein the antigen-binding molecule comprises:
a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and
a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83.
15. The cell according to claim 13, wherein the antigen-binding molecule comprises:
a VH region having the following framework regions (FRs):
HC-FR1 having the amino acid sequence of SEQ ID NO:53
HC-FR2 having the amino acid sequence of SEQ ID NO:59
HC-FR3 having the amino acid sequence of SEQ ID NO:66
HC-FR4 having the amino acid sequence of SEQ ID NO:71.
16. The cell according to claim 13, wherein the antigen-binding molecule comprises:
a VL region having the following framework regions (FRs):
LC-FR1 having the amino acid sequence of SEQ ID NO:104
LC-FR2 having the amino acid sequence of SEQ ID NO:110
LC-FR3 having the amino acid sequence of SEQ ID NO:120
LC-FR4 having the amino acid sequence of SEQ ID NO:125.
17. The cell according to claim 13, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171.
18. The cell according to claim 13, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177.
19. A method of treating a cancer in a subject, comprising administering to a subject a therapeutically effective amount of an antigen-binding molecule that specifically binds to HER3, wherein the antigen-binding molecule comprises:
(i) a heavy chain variable (VH) region having the following CDRs:
HC-CDR1 having the amino acid sequence of SEQ ID NO:41
HC-CDR2 having the amino acid sequence of SEQ ID NO:45
HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and
(ii) a light chain variable (VL) region having the following CDRs:
LC-CDR1 having the amino acid sequence of SEQ ID NO:88
LC-CDR2 having the amino acid sequence of SEQ ID NO:92
LC-CDR3 having the amino acid sequence of SEQ ID NO:95.
20. The method according to claim 19, wherein the antigen-binding molecule comprises:
a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and
a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83.
21. The method according to claim 19, wherein the antigen-binding molecule comprises:
a VH region having the following framework regions (FRs):
HC-FR1 having the amino acid sequence of SEQ ID NO:53
HC-FR2 having the amino acid sequence of SEQ ID NO:59
HC-FR3 having the amino acid sequence of SEQ ID NO:66
HC-FR4 having the amino acid sequence of SEQ ID NO:71.
22. The method according to claim 19, wherein the antigen-binding molecule comprises:
a VL region having the following framework regions (FRs):
LC-FR1 having the amino acid sequence of SEQ ID NO:104
LC-FR2 having the amino acid sequence of SEQ ID NO:110
LC-FR3 having the amino acid sequence of SEQ ID NO:120
LC-FR4 having the amino acid sequence of SEQ ID NO:125.
23. The method according to claim 19, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171.
24. The method according to claim 19, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177.
25. The method according to claim 19, wherein the cancer is selected from: a cancer comprising cells expressing an EGFR family member, a cancer comprising cells expressing HER3, a solid tumor, breast cancer, breast carcinoma, ductal carcinoma, gastric cancer, gastric carcinoma, gastric adenocarcinoma, colorectal cancer, colorectal carcinoma, colorectal adenocarcinoma, head and neck cancer, squamous cell carcinoma of the head and neck (SCCHN), lung cancer, lung adenocarcinoma, squamous cell lung carcinoma, ovarian cancer, ovarian carcinoma, ovarian serous adenocarcinoma, kidney cancer, renal cell carcinoma, renal clear cell carcinoma, renal cell adenocarcinoma, renal papillary cell carcinoma, pancreatic cancer, pancreatic adenocarcinoma, pancreatic ductal adenocarcinoma, cervical cancer, cervical squamous cell carcinoma, skin cancer, melanoma, esophageal cancer, esophageal adenocarcinoma, liver cancer, hepatocellular carcinoma, cholangiocarcinoma, uterine cancer, uterine corpus endometrial carcinoma, thyroid cancer, thyroid carcinoma, pheochromocytoma, paraganglioma, bladder cancer, bladder urothelial carcinoma, prostate cancer, prostate adenocarcinoma, sarcoma and thymoma.
With regards to claims 41-43, the US Patent does not claim additionally administering trastuzumab or docetaxel to treat cancer.
Aurisicchio and Schoebert teach as set forth above.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the US Patent. One would have been motivated to and have a reasonable expectation of success to because: (1) the US Patent claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy.
10. Claims 24-43 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 11,208,498, in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al. Although the claims at issue are not identical, they are not patentably distinct from each other because the US Patent is claiming a method of treating the same cancer instantly claimed comprising administering an antigen-binding molecule comprising VH and VL domains that comprise the same CDR sequences instantly claimed, thereby rendering obvious HER3 antigen-binding molecule of instant claims 24-27 and methods of treating cancer of instant claims 36-40.
1. A method of treating a cancer in a subject, wherein the cancer comprises cells having a mutation resulting in increased expression of a ligand for HER3, wherein the method comprises administering a therapeutically or prophylactically effective amount of an antigen-binding molecule which is capable of binding to HER3 to the subject, and wherein the antigen-binding molecule comprises:
(i) a heavy chain variable (VH) region incorporating the following CDRs:
HC-CDR1 having the amino acid sequence of SEQ ID NO:43
HC-CDR2 having the amino acid sequence of SEQ ID NO:46
HC-CDR3 having the amino acid sequence of SEQ ID NO:51; and
(ii) a light chain variable (VL) region incorporating the following CDRs:
LC-CDR1 having the amino acid sequence of SEQ ID NO:91
LC-CDR2 having the amino acid sequence of SEQ ID NO:94
LC-CDR3 having the amino acid sequence of SEQ ID NO:99.
2. The method according to claim 1, wherein the ligand for HER3 comprises an amino acid sequence having at least 60% sequence identity to the EGF-like domain of an NRG.
3. The method according to claim 1, wherein the mutation results in increased expression of the EGF-like domain of an NRG at the cell surface.
4. The method according to claim 1, wherein the cancer comprises cells having an NRG gene fusion.
5. The method according to claim 4, wherein the NRG gene fusion is selected from CLU-NRG1, CD74-NRG1, DOC4-NRG1, SLC3A2-NRG1, RBPMS-NRG1, WRN-NRG1, SDC4-NRG1, RAB2IL1-NRG1, VAMP2-NRG1, KIF13B-NRG1, THAP7-NRG1, SMAD4-NRG1, MDK-NRG1, TNC-NRG1, DIP2B-NRG1, MRPL13-NRG1, PARP8-NRG1, ROCK1-NRG1, DPYSL2-NRG1, ATP1B1-NRG1, CDH6-NRG1, APP-NRG1, AKAP13-NRG1, THBS1-NRG1, FOXA1-NRG1, PDE7A-NRG1, RAB3IL1-NRG1, CDK1-NRG1, BMPRIB-NRG1, TNFRSF10B-NRG1, MCPH1-NRG1 and SLC12A2-NRG2.
6. The method according to claim 4, wherein the NRG gene fusion is selected from CLU-NRG1, CD74-NRG1, SLC3A2-NRG1 or VAMP2-NRG1.
7. The method according to claim 1, wherein the cancer comprises cells expressing HER3.
8. The method according to claim 1, wherein the cancer derives from the lung, breast, head, neck, kidney, ovary, pancreas, prostate, uterus, gallbladder, colon, rectum, bladder, soft tissue or nasopharynx.
9. The method according to claim 1, wherein the cancer is selected from lung cancer, non-small cell lung cancer, lung adenocarcinoma, invasive mucinous lung adenocarcinoma, lung squamous cell carcinoma, breast cancer, breast carcinoma, breast invasive carcinoma, head and neck cancer, head and neck squamous cell carcinoma, renal cancer, renal clear cell carcinoma, ovarian cancer, ovarian serous cystadenocarcinoma, pancreatic cancer, pancreatic adenocarcinoma, pancreatic ductal adenocarcinoma, prostate cancer, prostate adenocarcinoma, endometrial cancer, uterine carcinosarcoma, gallbladder cancer, cholangiocarcinoma, colorectal cancer, bladder cancer, urothelial bladder cancer, sarcoma, soft tissue sarcoma, neuroendocrine tumor and neuroendocrine tumor of the nasopharynx.
10. The method according to claim 1, wherein the cancer is selected from lung cancer, non-small cell lung cancer, lung adenocarcinoma, invasive mucinous lung adenocarcinoma and lung squamous cell carcinoma.
11. The method according to claim 1, wherein the antigen-binding molecule comprises:
(i) a VH region incorporating the following CDRs:
HC-CDR1 having the amino acid sequence of SEQ ID NO:41
HC-CDR2 having the amino acid sequence of SEQ ID NO:45
HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and
(ii) a VL region incorporating the following CDRs:
LC-CDR1 having the amino acid sequence of SEQ ID NO:88
LC-CDR2 having the amino acid sequence of SEQ ID NO:92
LC-CDR3 having the amino acid sequence of SEQ ID NO:95.
12. The method according to claim 1, wherein the antigen-binding molecule comprises:
a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and
a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83.
13. The method according to claim 1, wherein the antigen-binding molecule comprises:
a VH region incorporating the following framework regions (FRs):
HC-FR1 having the amino acid sequence of SEQ ID NO:53
HC-FR2 having the amino acid sequence of SEQ ID NO:59
HC-FR3 having the amino acid sequence of SEQ ID NO:66
HC-FR4 having the amino acid sequence of SEQ ID NO:71.
14. The method according to claim 1, wherein the antigen-binding molecule comprises:
a VL region incorporating the following framework regions (FRs):
LC-FR1 having the amino acid sequence of SEQ ID NO:104
LC-FR2 having the amino acid sequence of SEQ ID NO:110
LC-FR3 having the amino acid sequence of SEQ ID NO:120
LC-FR4 having the amino acid sequence of SEQ ID NO:125.
15. The method according to claim 1, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171.
16. The method according to claim 1, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177.
The US Patent does not claim nucleic acids encoding the antibody, cells expressing the antibody, and additionally administering trastuzumab or docetaxel to treat cancer.
Aurisicchio and Schoebert teach as set forth above.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the US Patent. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the US Patent. One would have been motivated to and have a reasonable expectation of success to because: (1) the US Patent claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy.
11. Claims 24-43 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 11,780,933 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al.
Although the claims at issue are not identical, they are not patentably distinct from each other because the US Patent is claiming an antigen-binding molecule comprising a VH and VL region comprising all of the same CDR sequences instantly claimed that bind to HER3 epitope SEQ ID NO:229, nucleic acid encoding the antigen-binding molecule, a cell expressing the antigen-binding molecule, and method of treating cancer in a subject comprising administering the antigen-binding molecule, wherein the cancer includes cancer comprising cells expressing an EGFR family member, a cancer comprising cells expressing HER3, a solid tumor, breast cancer, and more, rendering obvious instant claims 24-40.
With regards to claims 41-43, the US Patent does not claim additionally administering trastuzumab or docetaxel to treat cancer.
Aurisicchio and Schoebert teach as set forth above.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the US Patent. One would have been motivated to and have a reasonable expectation of success to because: (1) the US Patent claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy.
12. Claims 24-43 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3, 4, 7, 8, 11-13, 15, 19, 21, 23-30 of copending Application No. 18/683,155 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al.
The copending application claims a method of treating HER3-associated cancer in a subject comprising administering to the subject an antigen-binding molecule which binds to HER3; wherein the cancer is a solid tumor, breast cancer, gastric cancer, pancreatic cancer, and more; wherein the HER3 antibody is 10D1F or comprises a VH and VL as follows:
(a) (i) a heavy chain variable (VH) region incorporating the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:40 HC-CDR2 having the amino acid sequence of SEQ ID NO:43 HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and (ii) a light chain variable (VL) region incorporating the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:66 LC-CDR2 having the amino acid sequence of SEQ ID NO:69 LC-CDR3 having the amino acid sequence of SEQ ID NO:74; or
(b) (i) a heavy chain variable (VH) region incorporating the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:38 HC-CDR2 having the amino acid sequence of SEQ ID NO:42 HC-CDR3 having the amino acid sequence of SEQ ID NO:45; and (ii) a light chain variable (VL) region incorporating the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:63 LC-CDR2 having the amino acid sequence of SEQ ID NO:67 LC-CDR3 having the amino acid sequence of SEQ ID NO:70; wherein SEQ ID NOs:38, 42, 45, 63, 67, and 70 are 100% identical to instant CDR SEQ ID NOs:41, 45, 48, 88, 92, and 95, respectively;
wherein the VH comprises SEQ ID NO:33 and VL comprises SEQ ID NO:58 that are 100% identical to instant SEQ ID NOs:36 and 83, respectively.
The copending application claims treating the same cancer population instantly claimed by administering the same HER3 antibody comprising the same CDR and VH and VL sequences. The method of the copending application renders obvious the instant HER3 antibody itself. Therefore, the copending claims overlap in scope with, and render obvious instant claims 24-27 and 36-40.
The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering trastuzumab or docetaxel.
Aurisicchio and Schoebert teach as set forth above.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy.
This is a provisional nonstatutory double patenting rejection.
13. Claims 24-43 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 4, 7, 9, 17, 18, 22, 24, 26, 30-32, 34-37, 39, 42, 46 and 47 of copending Application No. 18/688,576 in view of WO 2008/100624, Schoebert et al.
The copending application claims a HER3 antigen-binding molecule comprising VH and VL CDR SEQ ID NOs:43, 46, 51, 91, 94, and 99 that are identical to the same instant SEQ ID NOs; or comprising CDR SEQ ID NOs:41, 45, 48, 88, 92, and 95 that are identical to the same instant SEQ ID NOs; a method of treating cancer in a subject comprising administering to the subject an antigen-binding molecule which binds to HER3; wherein the cancer is breast, gastric, pancreatic cancer and more; and wherein the composition is administered in combination with cetixumab or trastuzumab.
The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering docetaxel.
Schoebert teaches as set forth above.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Schoebert teaches and demonstrates that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer in combination with other anticancer agents; (2) Schoebert suggests combining anti-cancer agents with HER3 antibody for the treatment of cancer, and (3) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy.
This is a provisional nonstatutory double patenting rejection.
14. Claims 24-43 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of copending Application No. 18/403,476 in view of in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al.
The copending application claims an antibody binding to HER3 that comprises CDR SEQ ID NOs:38, 42, 45, 63, 67, 70, that are 100% identical to instant SEQ ID NOs:41, 45, 48, 63, 67, and 70; and comprises VH and VL SEQ ID NOs:33 and 58, that are 100% identical to instant VH and VL SEQ ID NOs:36 and 83; methods of treating cancer comprising administering the antibody, wherein the cancer is cancer cells comprising cells expressing EGFR family member, breast cancer, gastric cancer, pancreatic cancer, and more cancers. Therefore, the copending claims overlap in scope with, and render obvious, the instantly claimed antibody and method of treating cancer.
The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering trastuzumab or docetaxel.
Aurisicchio and Schoebert teach as set forth above.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy.
This is a provisional nonstatutory double patenting rejection.
15. Claims 24-43 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3-16 of copending Application No. 19/301,118 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al.
The copending application claims a method of treating cancer in a subject comprising administering to the subject an antigen-binding molecule which binds to HER3; wherein the cancer is a lung cancer, breast cancer, pancreatic cancer, and more; wherein the HER3 antibody is comprises a VH and VL comprising CDR SEQ ID NOs: 43, 46, 51, 91, 94, and 99 that are 100% identical to the instantly claimed CDR sequences; or comprising CDR SEQ ID NOs:41, 45, 48, 88, 92, and 95 that are 100% identical to the instantly claimed CDR sequences; wherein the VH comprises SEQ ID NO:36 and VL comprises SEQ ID NO:83 that are 100% identical to instant SEQ ID NOs:36 and 83.
The copending application claims treating the same cancer population instantly claimed by administering the same HER3 antibody comprising the same CDR and VH and VL sequences. The method of the copending application renders obvious the instant HER3 antibody itself. Therefore, the copending claims overlap in scope with, and render obvious instant claims 24-27 and 36-40.
The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering trastuzumab or docetaxel.
Aurisicchio and Schoebert teach as set forth above.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy.
This is a provisional nonstatutory double patenting rejection.
16. Conclusion: No claim is allowed. It is noted that Boyd-Kirkup et al (Proceedings of the American Association for Cancer Research Annual Meeting, 2017: 2017 April 1-5; Washington DC. Philadelphia (PA): AACR; Cancer Research, 2017; 77(13 Suppl); Abstract 24) and Thakker et al (European Journal of Cancer, November 13, 2018; 103S1; e36-e37; Poster Session; abstract 87) teach HMBD001-10D1 antibody, but do not teach the antibody sequences or disclose that the antibody is publicly available.
17. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LAURA B GODDARD whose telephone number is (571)272-8788. The examiner can normally be reached Mon-Fri, 7am-3:30pm.
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/Laura B Goddard/Primary Examiner, Art Unit 1642