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 .
Claims 25-74 are pending and being acted upon in this Office Action.
Priority
Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d). The certified copy has been filed in parent Application No. 16/472,749, filed on June 21, 2019. The translation of the foreign priority document is also in the parent application and was filed on December 22, 2021.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on September 24, 2024, April 17, 2024, November 28, 2023, July 17, 2023 and June 16, 2023 have been considered by the examiner and an initialed copy of the IDS is included with this Office Action.
Drawings
The drawings were received on July 17, 2023. These drawings are acceptable.
Specification
The substitute specification filed July 17, 2023 has been entered.
Applicants should amend the first line of the specification to update the relationship between the instant application and U.S. Application No. 16/472,749, filed June 21, 2019, now U.S. Patent No. 11,660,351.
The lengthy specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant's cooperation is requested in correcting any errors of which applicant may become aware in the specification.
Claim rejections under - 35 U.S.C. 112
The following is a quotation 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 35 U.S.C. 112 (pre-AIA ), first paragraph:
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.
Claims 25-74 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 MPEP § 2163 lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the Application. These include: (1) Actual reduction to practice, (2) Disclosure of drawings or structural chemical formulas, (3) Sufficient relevant identifying characteristics (such as: i. Complete structure, ii. Partial structure, iii. Physical and/or chemical properties, iv. Functional characteristics when coupled with a known or disclosed, and correlation between function and structure), (4) Method of making the claimed invention, (5) Level of skill and knowledge in the art, and (6) Predictability in the art. “Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient.”
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Reagents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). The recitation of a functional property alone, which must be shared by the members of the genus, is merely descriptive of what the members of the genus must be capable of doing, not of the substance and structure of the members. The Federal Circuit has cautioned that, for claims reciting a genus of antibodies with particular functional properties (e.g., binding to antigen, high affinity, neutralization activity, competing with a reference antibody for binding), “[c]laiming antibodies with specific properties, e.g., an antibody that binds to human TNF-α with A2 specificity, can result in a claim that does not meet written description even if the human TNF-α protein is disclosed because antibodies with those properties have not been adequately described." Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875, 1877-78 (Fed. Cir. 2011).
“[A] sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (“The ’128 and ’485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the genus.”). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species.
The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention. For antibodies, the Federal Circuit has found that possession of a mouse antibody heavy and light chain variable regions provides a structural "stepping stone" to the corresponding chimeric antibody, but not to human antibodies. Centocor, 97 USPQ2d at 1875 (“[T]he application only provides amino acid sequence information (a molecular description of the antibody) for a single mouse variable region, i.e., the variable region that the mouse A2 antibody and the chimeric antibody have in common. However, the mouse variable region sequence does not serve as a stepping stone to identifying a human variable region within the scope of the claims.”). A chimeric antibody shares the full heavy and light chain variable regions with the corresponding mouse antibody; that is, the structure shared between a mouse and chimeric antibody would generally be expected to conserve the antigen binding activity.
Even if a selection procedure is disclosed that was, at the time of the invention, sufficient to enable the skilled artisan to identify antibodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad, 94 USPQ2d at 1167; Centocor at 1876 (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”)
Additionally, “An adequate written description must contain enough information about the actual makeup of the claimed products—“a precise definition, such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other materials,” which may be present in “functional” terminology “when the art has established a correlation between structure and function.” Ariad, 598 F.3d at 1350. But both in this case and in our previous cases, it has been, at the least, hotly disputed that knowledge of the chemical structure of an antigen gives the required kind of structure-identifying information about the corresponding antibodies.” Amgen Inc v. Sanofi 124 USPQ2d 1354, 1361 (Fed. Cir. 2017). “Further, the “newly characterized antigen” test flouts basic legal principles of the written description requirement. Section 112 requires a “written description of the invention.” But this test allows patentees to claim antibodies by describing something that is not the invention, i.e., the antigen. The test thus contradicts the statutory “quid pro quo” of the patent system where “one describes an invention, and, if the law's other requirements are met, one obtains a patent.” Ariad, 598 F.3d at 1345.” Amgen at 1362.
Applicant claims antibody drug conjugates (ADC) comprising anti-CXCR5 antibodies attached to KSP inhibitors and methods of using said ADCs for the treatment of disease associated with CXCR5 expression, e.g., hyperproliferative disease, angiogenesis, cancers and tumors. This rejection pertains to the antibody portion of the ADC in that the antibody or antigen binding fragment thereof binds to CXCR5 (claims 25-35, 67).
The specification discloses just two antibodies TPP-9574 and TPP-9580 that bind to CXCR5. The TPP-9574 antibody comprises a heavy chain domain comprising the amino acid sequence of SEQ ID NO: 91 and a light chain domain comprising the amino acid sequence of SEQ ID NO: 95. The TPP-9580 antibody comprises a heavy chain domain comprising the amino acid sequence of SEQ ID NO: 101 and a light chain domain comprising the amino acid sequence of SEQ ID NO: 105.
However, the specification does not describe the structure-identifying information i. Complete structure, i.e., amino acid sequence of heavy and light chain variable domains, or ii. Partial structure, i.e., the six CDRs, iii. Physical and/or chemical properties and iv Functional characteristics, i.e., binding affinity or epitope specificity share by members of the genus of antibody or antigen binding fragment thereof that binds to any CXCR5, nor describe a representative number of species falling within the scope of the genus or structural feature common to the members of the genus so the one of skill in the art can visualize or recognize the member of the genus of the actual claimed antibody-drug conjugate themselves as a pharmaceutical composition.
It is known in the art that antibodies have a large repertoire of distinct structures and that a huge variety of antibodies can be made to bind to a single epitope.
For example, Lloyd et al. taught that hundreds of functional antibody fragments can be isolated from an antibody library that bind to the same antigen wherein these antibodies have distinct heavy and light chain sequences (Lloyd et al. Protein Engineering, Design & Selection 22:159-168, 2009; PTO 892; see, e.g., Discussion).
Similarly, Edwards et al., J Mol Biol. 334(1): 103-118, 2003; PTO 892, found that over 1000 antibodies, all different in amino acid sequence, were generated to a single protein; 568 different amino acid sequences identified for the V(H) CDR3 domains of these antibodies (Abstract).
Poosarla et al (Biotechn. Bioeng., 2017, 114(6): 1331-1342, 2017; PTO 892) teach substantial diversity in designed mAbs (sharing less than 75% sequence similarity to all existing natural antibody sequences) that bind to the same 12-mer peptide, binding to different epitopes on the same peptide. Said reference further teaches “most B-cell epitopes... in nature consist of residues from different regions of the sequence and are discontinuous...de novo antibody designs against discontinuous epitopes present additional challenges...". (See entire reference.)
Given that hundreds of unique antibody structures may bind a single antigen, the structure of an antibody cannot be predicted from the structure of the antigen (as held in Amgen), and a single species, or small group of species, cannot define a structure-function relationship so as to be representative of all the antibodies that bind to that antigen (as held in Abbvie).
Regarding the number of drug to antibody wherein n is 1 to 50 (claims 25-74), the specification discloses the drug to antibody ratio is about 3 to about 6, see p. 129, 129, and 137.
However, the specification does not teach double digit number of drugs per antibody, such as 50 drugs per antibody.
Nejadmoghaddam (Avicenna Journal of Medical Biotechnology 2(1): 3-23, 2019; PTO 892) discusses major obstacles of antibody-drug conjugates include off-target toxicity, tumor marker selection, antibody specificity, adequately affinity and receptor-mediated internalization are major aspects of choice, cytotoxic payload (e.g., up to 7 drugs per antibody), cytotoxic payload linkage strategy, aqueous solubility, non-immunogenic and stability in storage and bloodstream, see entire document, abstract, p. 15, in particular.
Regarding pharmaceutical acceptable salt thereof (claims 25-74), the specification has not provided a written description of the reagents or conditions for the formation of a single salt for the anti-CXCR5 conjugates encompassed by the claims. For example, It would not be expected that the reagents or conditions disclosed for the formation of crystalized unconjugated cetuximab or Mab h425 would be the same reagents or conditions for the formation of salts, hydrates or solvates for the instant genus of anti-Her3 conjugates claimed because Matheus et al teach that the crystallization of cetuximab and Mab h425 was an unexpected result.
Matheus et al (US 7,960,516) teach that antibodies exhibit a tendency towards aggregation which causes difficulties in crystallization (column 2, lines 58-61) and a tendency towards denaturation during the crystallization process (column 2, lines 63-66).
Morissette et al (Advanced Drug Delivery Reviews, Vol. 56, pp. 275-300, 2004; PTO 892) teach high through put method to determine optimal crystallization techniques for the formation of salts and solvates (title). Morissette et al do not specifically address high through put methods to determine optimal crystallization techniques for the formation of salts and solvates of antibodies that circumvent aggregation and denaturation. Further, the ability to screen for the required salt of a particular antibody which is not the inventive anti-CXCR5 antibodies does not provide an adequate written description of the salt comprising the antibody conjugate in a non-aggregated, non-denatured state because one of skill in the art cannot describe what is yet to be made. For these reasons, the skilled artisan would not recognize that applicants were in possession of the invention as broadly claimed at the time the application was filed.
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.).
Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
One cannot describe what one has not conceived. See Fiddles v. Baird, 30 USPQ2d 1481, 1483. In Fiddles v. Baird, claims directed to mammalian FGF’s were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence. Thus, the specification fails to describe these DNA sequences.
For genus claims, an adequate written description of a claimed genus requires more than a generic statement of an invention's boundaries. A patent must set forth either a representative number of species falling within the scope of the genus or structural features common to the members of the genus. Kubin, Exparte, 83 USPQ2d 1410 (Bd. Pat. App. & Int. 2007); Ariad Pharms., Inc. v. Eli Lilly& Co., 598 F.3d 1336, 1350 (Fed. Cir. 2010).
Therefore, only (1) an antibody-drug conjugate as set forth in claims 36-66 wherein n is 1 to 8 and (2) method for treatment of a disease associated with CXCR5 expression set forth in claims 68-74, but not the full breadth of the claims meets the written description provision of 35 U.S.C. § 112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. § 112 is severable from its enablement provision (see page 1115).
Claims 25-74 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for only (1) an antibody-drug conjugate as set forth in claims 36-66 wherein n is 1 to 8 and (2) method for treatment of a disease associated with CXCR5 expression set forth in claims 68-74, does not reasonably provide enablement for any antibody-drug conjugate as set forth in claims 25-66 and a method of treating any disease associated with CXCR5 expression using said antibody-drug conjugates. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make/use the invention commensurate in scope with these claims.
Enablement is considered in view of the Wands factors (MPEP 2164.01(a)). These factors include, but are not limited to: (A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. . In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988).
The claims recite a large and structurally varied genus of antibodies or antigen binding fragment thereof that bind to CXCR5 (claims 25-35).
The specification discloses just two antibodies TPP-9574 and TPP-9580 that bind to CXCR5. The TPP-9574 antibody comprises a heavy chain domain comprising the amino acid sequence of SEQ ID NO: 91 and a light chain domain comprising the amino acid sequence of SEQ ID NO: 95. The TPP-9580 antibody comprises a heavy chain domain comprising the amino acid sequence of SEQ ID NO: 101 and a light chain domain comprising the amino acid sequence of SEQ ID NO: 105.
However, the specification does not teach i. Complete structure, i.e., amino acid sequence of heavy and light chain variable domains, or ii. Partial structure, i.e., the six CDRs, iii. Physical and/or chemical properties and iv Functional characteristics, i.e., binding affinity or epitope specificity share by members of the genus of antibody or antigen binding fragment thereof that binds to any CXCR5 or common structure share by members of the genus of antibodies to enable one of skill in the art to make and use the claimed antibody-drug conjugates.
It is known in the art that antibodies have a large repertoire of distinct structures and that a huge variety of antibodies can be made to bind to a single epitope.
For example, Lloyd et al. taught that hundreds of functional antibody fragments can be isolated from an antibody library that bind to the same antigen wherein these antibodies have distinct heavy and light chain sequences (Lloyd et al. Protein Engineering, Design & Selection 22:159-168, 2009; PTO 892; see, e.g., Discussion).
Similarly, Edwards et al., J Mol Biol. 334(1): 103-118, 2003; PTO 892, found that over 1000 antibodies, all different in amino acid sequence, were generated to a single protein; 568 different amino acid sequences identified for the V(H) CDR3 domains of these antibodies (Abstract).
Poosarla et al (Biotechn. Bioeng., 2017, 114(6): 1331-1342, 2017; PTO 892) teach substantial diversity in designed mAbs (sharing less than 75% sequence similarity to all existing natural antibody sequences) that bind to the same 12-mer peptide, binding to different epitopes on the same peptide. Said reference further teaches “most B-cell epitopes... in nature consist of residues from different regions of the sequence and are discontinuous...de novo antibody designs against discontinuous epitopes present additional challenges...". (See entire reference.)
Given that hundreds of unique antibody structures may bind a single antigen, the structure of an antibody cannot be predicted from the structure of the antigen, and a single species, or small group of species, cannot define a structure-function relationship so as to be representative of all the antibodies that bind to that antigen..
Regarding the number of drug to antibody wherein n is 1 to 50 (claims 25-74), the specification discloses the drug to antibody ratio is about 3 to about 6, see p. 129, 129, and 137.
However, the specification does not teach double digit number of drugs per antibody, such as 50 drugs per antibody.
Nejadmoghaddam (Avicenna Journal of Medical Biotechnology 2(1): 3-23, 2019; PTO 892) discusses major obstacles of antibody-drug conjugates include off-target toxicity, tumor marker selection, antibody specificity, adequately affinity and receptor-mediated internalization are major aspects of choice, cytotoxic payload (e.g., up to 7 drugs per antibody), cytotoxic payload linkage strategy, aqueous solubility, non-immunogenic and stability in storage and bloodstream, see entire document, abstract, p. 15, in particular.
There are no in vivo working examples. It is unpredictable which antibody-drug conjugate having 50 drugs per antibody is effective for treating which disease associated with CXCR5 expression.
Regarding pharmaceutical acceptable salt thereof (claims 25-74), the specification fails to provide any teachings for how to make the solid forms of salts of the instant antibody conjugates.
Matheus et al (US 7,960,516) teach the unexpected result that stable pharmaceuticals can be prepared with solid forms of cetuximab and Mab h425 (column 4, lines 56-59) and that the antibodies are biologically active after re-dissolution (column 10, lines 51-59). Matheus et al teach that the crystallization of intact glycosylated antibodies is extremely difficult due to the size of the protein, the different glycosylation patterns of the individual molecules and associated micro-heterogeneities as well as the structural flexibility of the immunoglobulin make an ordered incorporation into a crystal lattice more difficult or even impossible (column 2, lines 50-56) and that there is a risk of denaturing antibodies during the crystallization process (column 2, lines 63-66). It is noted that the number of drugs attached to a single antibody varies between 1-50 (subscript “n”) in claims 25-74. The cumulative number of drug moieties plus linker required in the antibody-conjugate would vastly increase the size of the molecule, and alter flexibility and the micro-heterogeneity, especially since the number of attachments to a single antibody vary from 1-50. These factors are in opposition to the formation of an ordered crystal lattice necessary for solid phase salt formation. Antibodies have aqueous solubility of over 200 mg/ml in histidine buffer at pH 6 (Ke et al, International Journal of Pharmaceutics, Vol. 548, pp. 682-688, 2015, PTO 892, see page 684, first column, lines 6-7, page 683, lines 3-4 under section 2.2.2, lines 2-3 under section 2.2.3). The influence of a group that is much less hydrophilic than the antibody, such as the instant kinesin spindle inhibitor derivatives, on the ability of the antibody to go into a crystal lattice of a salt is unknown. Thus one of skill in the art would be subject to undue experimentation in order to make the salts of the anti-CXCR5 conjugates.
The scope of the claims must bear a reasonable correlation with the scope of enablement. See In re Fisher, 166 USPQ 19 24 (CCPA 1970).
In re wands, 858 F.2d at 737, 8 USPQ2d at 1404 (Fed. Cir. 1988), the decision of the court indicates that the more unpredictable the area is, the more specific enablement is necessary.
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 claims at issue 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); and 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 a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO internet Web site contains terminal disclaimer forms which may be used. Please visit http://www.uspto.gov/forms/. The filing date of the application will determine what form 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 http://www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 25-74 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-50 of U.S. Patent No. 11,660,351. Although the claims at issue are not identical, they are not patentably distinct from each other because while the ‘351 patent issued from the application which served as the parent for the present case, the examined application was filed as a CON, not a DIV, and therefore no shield against double patenting that might be provided by 35 U.S.C 121 would be applicable here.
The ’351 patent teaches the claimed antibody-drug conjugate of formula (I) comprising the same kinesin spindle protein (KSP) inhibitors conjugated to an anti-CXCR5 antibody selected from the group consisting of TPP-9574 and TPP-9580.
18182,093
11,660,351
SEQ ID NO: 92
TSGMH
TSGMH
SEQ ID NO: 93
YISSSSGFVYADAVKG
YISSSSGFVYADAVKG
SEQ ID NO: 94
SEAAF
SEAAF
SEQ ID NO: 96
RSQKSRLSRMGITPLN
RSQKSRLSRMGITPLN
SEQ ID NO: 97
RMSNLAS
RMSNLAS
SEQ ID NO: 98
AQFLEYPPT
AQFLEYPPT
PNG
media_image1.png
275
685
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A person of skill in the art, reading the claims of the ‘351 patent, would look to the patent and follow the ‘351 patent’s express instruction on how to make the product within the patent, e.g., Examples 1-11, thereby arriving at the antibody drug conjugate of the examined claims.
Claims 25-74 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 15-20 of US Patent 11,478,554. Although the claims at issue are not identical, they are not patentably distinct from each other because the only difference between the two sets of claims is the scope. Specifically, the scope of the claims in the instant application is narrower in that the KSP inhibitor of the ADC (antibody drug conjugate) is limited to a specific structure whereas in the reference application the KSP inhibitor is generic. The claims are also directed to use of conjugates for the treatment of disease associated with CXCR5 expression.
18182,093
11,478,554
SEQ ID NO: 92
TSGMH
TSGMH
SEQ ID NO: 93
YISSSSGFVYADAVKG
YISSSSGFVYADAVKG
SEQ ID NO: 94
SEAAF
SEAAF
SEQ ID NO: 96
RSQKSRLSRMGITPLN
RSQKSRLSRMGITPLN
SEQ ID NO: 97
RMSNLAS
RMSNLAS
SEQ ID NO: 98
AQFLEYPPT
AQFLEYPPT
Not Prior Art
WO 2016/207089 (published 12/29/2016, priority to 6/22/2015) (English equivalent is US 2018/0169256 is not prior art because the closest structure of the antibody-drug conjugate is shown below and differs from the claimed structure at location indicated in the arrow below.
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440
587
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and does not read on the claimed wherein R2 is methyl.
Lerchen et al WO 2015/096982 (English equivalent is US 2016/0346402 and the rejection will refer to passages in the US document) is not prior art because the reference KSP drug structures differ from than any of the structures of instant claims.
Free from art
Anti-CXCR5 antibodies TPP-9574 and TPP-9580 are free from the art of record.
Claims 36-66 and 68-74 are free of prior art.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to PHUONG HUYNH whose telephone number is (571)272-0846. The examiner can normally be reached on 9:00 a.m. to 6:30 p.m. The examiner can also be reached on alternate alternative Friday from 9:00 a.m. to 5:30 p.m.
If attempts to reach the examiner by telephone are unsuccessful, the examiner's supervisor, Misook Yu, can be reached at 571-270-3497. The fax phone number for the organization where this application or proceeding is assigned is 571-272-0839.
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/PHUONG HUYNH/ Primary Examiner, Art Unit 1641