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 .
Election/Restriction
Applicant’s election without traverse of Invention I, in the reply filed on 11AUG2025 is acknowledged.
Claims 13-19, 24, 28, and 32 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention and/or species. Election was made without traverse in the reply filed on 11AUG2025.
Claim Status
Claims 3-5, 9-11, and 23 have been amended.
Claims 20-22, 25-27, and 29-31 are cancelled.
Claims 1-19, 23-24, 28, and 32 are pending in the instant application.
Claims 1-12 and 23 are examined on the merits.
Priority
The present application claims priority under 35 USC §119(e), which claims benefit of US Provisional Patent Application No. PCT/US2020/047035, filed 19AUG2020 and US Provisional Patent Application No. 62/888724, filed 19AUG2019. Applicant’s claim for the benefit of prior-filed applications is acknowledged.
Information Disclosure Statement
The information disclosure statement(s) (IDS) submitted on 02MAY2022, 23OCT2023, and 06DEC2024 is/are acknowledged and the references cited therein have been considered.
Specification
The disclosure is objected to because of the following informalities:
INCORPORATION-BY-REFERENCE OF MATERIAL SUBMITTED ON A READ-ONLY OPTICAL DISC, AS A TEXT FILE OR AN XML FILE VIA THE PATENT ELECTRONIC SYSTEM is missing.
Appropriate correction is required.
Claim Objections
Claim 1 and 11 are objected to because of the following informalities:
Claim 1 includes a typographical error: “EP142-D9” should be updated to include a “0” between the “D” and the “9” for the purpose of consistency.
Claim 11 includes a grammatical error: “from” should be inserted between “selected” and “the” in line 2 of the claim.
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.
Enablement
Claims 1-11 and 23 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Scope of the claim:
In the instance of claim 1, the nature of the invention is drawn to an isolated CD19 antibody that binds to the same epitope on CD19 or competes for binding to CD19 as the reference antibodies (i.e., EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10), is not fully enabled. The broadest claim and dependent claims 2-11 and 23 are not enabled because:
The breadth of structures;
The lack of support and working examples provided by the specification (i.e., the reference examples are the only anti-CD19 antibodies disclosed);
The lack of predictability in the prior art to determine binding based on epitope or competitive binding, which have
80% identity to the HCDRs1-3 and/or LCDRs 1-3 of EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10,
85% identity to the VH and/or VL of EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10, and
specific binding affinity properties (i.e., result); and
The undue experimentation required of one of ordinary skill in the art
To determine the epitope which EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10 binds,
To screen alternative CD19 antibodies that bind to said epitope, and
To screen competitive binding to CD19 as compared to EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10.
Direction provided by the inventor and existence of working examples:
The specification discloses anti-CD19 antibodies that bind to the same epitope as EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10. Epitope is defined as the site on a target antigen that is recognized and bound by an antibody, which can be linear or conformational, and determined by epitope mapping (p 12, lines 5-12). An antibody is considered to bind the same epitope if it binds to i) the exact same epitope as the reference antibody, or ii) a substantially overlapping epitope (exemplarily less than 3, 2, or 1 non-overlapping amino acid residues) as the reference antibody (p 12, lines 12-15). However, no specific epitope is disclosed. The reference and exemplary isolated CD19 antibodies are the same, wherein the amino acid sequences of the VH/VL pairs and HCDR1-3/LCDR1-3 pairs of the reference and exemplary antibodies are set forth in Table 2. However, there is no full amino acid sequence set forth in the specification which encompasses the entirety of the HC/LC pair (i.e., inclusive of the constant regions) for any of the anti-CD19 antibody clones.
Working examples of the specification disclose, generation of fully human anti-CD19 antibodies, screening of CD19 binding, epitope binning of specific scFv anti-CD19 clones (i.e., EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10) compared to FMC63, and general binding properties of scFv anti-CD19 clones to endogenously or recombinantly expressed CD19 on the surface of cells. Although, this example supports generation/screening of antibodies that bind CD19 and competitive binding of the isolated and generated scFv anti-CD19 clones as compared to FMC63, there is no disclosure of the specific epitope on CD19 to which EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10 bind, that the clones bind to the same epitope on CD19 (i.e., only suggests that the scFv anti-CD19 clones do not bind to the same epitope as the FMC63 clone), and that EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10 competitively bind to CD19 as compared to each other.
In this instance, there is no disclosure provided regarding making an anti-CD19 antibody having the epitope or competitive binding properties of EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10.
State of prior art and level of predictability in the art:
Furthermore, the literature teaches that antibody structures are defined by six nondegenerate CDRs and the ability to predict the structure from the epitope is not possible. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway, et al., Immunobiology: The Immune System in Health and Disease, 5th edition, 2001). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff, et al., PNAS, 1982, 79, 1979-1983 see entire document, particularly the abstract and the middle of the left column of p 1982). Further, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well (Edwards, et al., J Mol Biol, 2003, 334, 103-118, see entire document).
Quantity of experimentation needed to make or use the invention based on the disclosure:
Thus, one skilled in the art would be unable to make and/or use an isolated CD19 antibody that binds to the same epitope on CD19 or competes for binding to CD19 as the reference antibody clones (i.e., EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10). Therefore, the implementation of the invention in view of the unclear nature (i.e., the epitope), breadth of variables (i.e., structures, inclusive of the constant domain for the full-length antibody), level of predictability in the art, and the lack of direction and support provided in the specification and working examples, would require undue experimentation for one of ordinary skill in the art to make and/or use the isolated anti-CD19 antibodies of the instantly claimed invention.
Written Description
Claims 1-11 and 23 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted: “A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin [e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate."). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.”
The court has further stated that “Adequate written description 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.” Id. at 1566, 43 USPQ2d at 1404 (quoting Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606). Also see Enzo-Biochem v. Gen-Probe 01-1230 (CAFC 2002). Recent court cases have emphasized the need for correlation between a well-defined structure and recited functional limitations. For example, the courts have indicated that recitation of an antibody which has specific functional properties in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See for example AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014) as well as Amgen v. Sanofi, (Fed Cir, 2017-1480. 10/5/2017). Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e., the antigen, as knowledge of the chemical structure of an antigen does not give the required kind of structure-identifying information about the corresponding antibodies, with the antibody-antigen relationship be analogized as a search for a key on a ring with a million keys on it. As such, knowledge of where an antibody binds provides no information as to what such an antibody necessarily looks like (i.e., its primary amino acid structure). Applicant is reminded that the courts have long ruled that “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. As such, disclosure of a screening assay to test for functional properties of a reagent (such as the epitope to which the reagent binds or the fact that it does or does not inhibit some process) does not provide evidence of possession of the reagent itself.
In Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017), relying upon Ariad Pharms., Inc. v. Eli Lily & Co., 94 USPQ2d 1161 (Fed Cir. 2010), the following is noted. To show invention, a patentee must convey in its disclosure that they “had possession of the claimed subject matter as of the filing date. Demonstrating possession “requires a precise definition” of the invention. To provide this precise definition” for a claim to a genus, a patentee must disclose “a representative number of species within the scope of the genus of structural features common to the members of the genus so that one of skill in the art can visualize or recognize the member of the genus” (see Amgen at page 1358). Further, an adequate written description must contain enough information about the actual makeup of the claimed products – “a precise definition, such as structure, formula, chemic name, physical properties of other properties, of species falling with the genus sufficient to distinguish the gene from other materials”, which may be present in “functional terminology when the art has established a correlation between structure and function” (Amgen page 1361). Indeed, the courts have long ruled that “When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.” See Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005). Also, “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.” See AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69. It should also be noted that the USPTO has released a Memo on the Clarification of Written Description Guidance For Claims Drawn to Antibodies and Status of 2008 Training Materials, 02/22/2018. See https://www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf. This Memo clarifies the applicability of USPTO guidance regarding the written description requirement of 35 U.S.C. § 112(a) concerning the written description requirement for claims drawn to antibodies and states: “In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional”. Further, the courts have indicated that the enablement and written description requirements of 35 USC 112 are separable as can be seen in for example Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111.
The teachings of the specification and the claimed invention:
Applicant has broadly claimed an isolated CD19 antibody that binds to the same epitope on CD19 or competes for binding to CD19 as the reference antibodies (i.e., EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10). The broadest claims do not require the isolated CD19 antibody to have any function apart from binding a specific epitope on CD19 or competitively bind CD19 as compared to the reference antibodies, with dependent limitations adding additional functional limitations, such as, binding affinity (i.e., claims 5-6). Additionally, it is clear that the claims encompass antibodies with potential CDR mutations and/or substitutions relative to EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10 (i.e., claims 2-4), but neither the claims nor the specification define where the mutation can occur that will maintain the claimed specificity. Therefore, no claims recite any specific or particular structure of the CD19 antibody that gives rise to the specific binding functions, apart from claim 12, which is limited to specific amino acid sequences of the reference antibodies (i.e., EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10) as set forth in SEQ ID NOs: 11, 12, 13, or 14.
To support such broad claims, the specification teaches anti-CD19 antibodies that bind to the same epitope as EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10. The term “epitope” is defined as the site on a target antigen that is recognized and bound by an antibody, which can be linear or conformational, and determined by epitope mapping (p 12, lines 5-12). An antibody is considered to bind the same epitope if it binds to i) the exact same epitope as the reference antibody, or ii) a substantially overlapping epitope (exemplarily less than 3, 2, or 1 non-overlapping amino acid residues) as the reference antibody (p 12, lines 12-15). However, no specific epitope is disclosed. The reference and exemplary isolated CD19 antibodies are the same, wherein the amino acid sequences of the VH/VL pairs and HCDR1-3/LCDR1-3 pairs of the reference and exemplary antibodies are set forth in Table 2. Although the claims are drawn to any CD19 antibody having the same epitope as the reference antibody clones or compete for CD19 binding as compared to the reference antibody clones, the experimental data teach generation of fully human anti-CD19 antibodies, screening of CD19 binding, epitope binning of specific scFv anti-CD19 clones (i.e., EP142-D[0]9, EP187-A12, EP188-A01, and EP188-B10) compared to FMC63, and general binding properties of scFv anti-CD19 clones to endogenously or recombinantly expressed CD19 on the surface of cells..
The state of the prior art:
With regard to antibodies, it should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope and similarly for scFv binding structures (i.e., fusion protein) they consist of a VH, linking peptide, and VL (i.e., six nondegenerate CDRs). The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway, et al., Immunobiology: The Immune System in Health and Disease, 5th edition, 2001 and Ahmad, et al., Clin Dev Immunol, 2012, 980250, 1-15, see entire document, specifically Figure 1). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff, et al., PNAS, 1982, 79, p 1979-1983 see entire document, particularly the abstract and the middle of the left column of p 1982). Thus, based upon the prior art, skilled artisans would reasonably understand that it is the structure of the CDRs within an antibody which gives rise to the functional property of antigen binding, the epitope to which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves.
Additionally, artisans are well aware that knowledge of a given antigen (for instance a specific epitope of CD19 to which a reference antibody clone binds) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well (Edwards, et al., J Mol Biol, 2003, 334, 103-118, see entire document). Goel et al. disclose the synthesis of three monoclonal antibodies that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (Goel, et al., J Immunol, 2004, 173, 7358-7367, see entire document). Further, it should be noted that degenerate binding of the same structural motif by antibodies does not require the existence of sequence homology or identity at any of their CDRs or other chemical similarities at the antigen-binding sites; side chain mobility of epitope residues can confer steric and electrostatic complementarity to differently shaped combining sites, allowing functional mimicry to occur (Lescar et al., J Biol Chem, 1995, 270, 18067-18076, see entire document, in particular Abstract and Discussion). As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen as there does not appear to be any common or core structure present within all antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound in a population of antibodies that bind to a given antigen no number of species appears to reasonably representative of the breadth of the genus of antibodies that bind the given antigen.
Claim analysis:
In this instance, the prior art supports that an antibody product structure be defined by six nondegenerate CDRs. As presently written, the claims recite that anti-CD19 antibody clone structures are defined by functions of binding a specific epitope of CD19 or competitively bind CD19 as compared to a specific set of reference antibodies. However, the specification and the working examples fail to disclose any data indicating that the breadth of structures (i.e., all CD19 antibody clones) encompassed by the language of the instant claims will have the same function as the reference antibodies.
Additionally, claims 2-4 allow for mutations within the CDR regions of the antibody. The specification does not provide guidance as to how to identify antibodies that express variations of the CDRs and maintain the claimed functions. Claims 2-4 disclose the sequence of the reference antibody HCDRs1-3 and/or LCDRs1-3, as well as the variable regions and allow for 80-85% variation, but do not offer guidance on what regions of the variable regions the sequences may differ and still function as claimed. Because these claims allow for mutations within the CDR regions of the antibody, one of ordinary skill in the art would neither expect nor predict the appropriate functioning of the antibodies as broadly as is claimed.
Therefore, as presently written, the claimed broad genus of anti-CD19 antibodies lacks adequate written description and one of ordinary skill in the art would reasonably conclude that the applicant was not in possession of the full breadth of the claimed genus because there does not appear to be any correlation between the structure of the antibody and the ability to bind a specific epitope as related to reference antibodies, at the time the instant application was filed.
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 filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-9 and 11-12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-39 of co-pending Application No. 18/262496; herein referred to as the “reference application.” Although the claims at issue are not identical, they are not patentably distinct from each other because the antigen binding moiety that binds CD19 of the reference application anticipates the anti-CD19 antibody of the instant application. Specifically, both antigen binding moieties directed at CD19 are related to the anti-CD19 EP187-A12 clone (i.e., SEQ ID NO: 9 of the reference application is 100% query match to SEQ ID NO: 11 of the instant application, see OA.APPENDIX).
The co-pending claims of the reference application recite: A bispecific CAR to CD19 and CD22, comprising a first and second antigen binding domain, co-stimulatory signaling domain, and cytoplasmic signaling domain, wherein the first antigen binding domain comprises the same HCDRs and LCDRs as reference antibody EPC-001-1 which binds CD19 (i.e., EP187-A12 of the instant application) and wherein the second antigen binding moiety comprises… each of which binds to CD22 (i.e., claim 1). The bispecific CAR of claim 1, wherein the first antigen binding moiety comprises the same VH/VL as EPC-001-1 (i.e., claim 2); or wherein the first and second antigen binding moieties are scFvs (i.e., claim 4). The bispecific CAR of claim 4, wherein the first antigen binding moiety is a scFv comprising the amino acid sequences of SEQ ID NO: 9 (i.e., claim 5).
In this instance, because the CD19 binding region of the reference application comprises SEQ ID NO: 9 is a 100% query match to the CD19 binding region of the instant application consisting of SEQ ID NO: 11, the CD-19 binding region of the bispecific antibody of the reference application anticipates the more general anti-CD19 binding agent of the instant application. In response, it is suggested that applicant either file a terminal disclaimer or amend the claims such that a clear and unmistakable line of separation exists between the products claimed in the instant application and those of the reference application.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
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.
Claims 1 and 23 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by WO2018/161017 A1 (Obsidian Therapeutics, Inc., et. al, 07SEP2018, included in IDS), herein referred to as “’017.”
‘017 teaches the generation and selection of human anti-CD19 scFvs which bind to CD19 on the cell surface to epitopes distinct from the anti-CD19 FMC63 clone and pharmaceutical compositions thereof (see entire document, specifically see ¶0046 and 00362).
The office does not have the facilities and resources to provide the factual evidence needed in order to establish that there is a difference between the materials, (i.e., that the claims are directed to new materials and that such a difference would have been considered unexpected by one of ordinary skill in the art, that is, the claimed subject matter (e.g., an anti-CD19 antibody binding to an undefined epitope, but is not the same as the epitope of an anti-CD19 FMC63 clone)), if new, is unobvious. In the absence of evidence to the contrary, the burden is on the Applicant to prove that the claimed materials are different from those taught by the prior art and to establish patentable differences. See In re Best 562F.2d 1252, 195 USPQ 430 (CCPA 1977) and Ex parte Gray 10 USPQ 2d 1922 (PTO Bd. Pat. App. & Int. 1989). Therefore, in the absence of evidence to the contrary, the anti-CD19 scFv antibody clones taught by ‘017 would have the claimed properties recited in claim 1.
Therefore, the prior art anticipates the invention as presently claimed.
Allowable Subject Matter
It is noted that the scFv anti-CD19 antibodies comprising the amino acid sequences selected from the group consisting of SEQ ID NOs: 12, 13, and 14 are free of the prior art.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SAMANTHA L. HOPKINS whose telephone number is (703)756-4666. The examiner can normally be reached Mon-Thurs 6:00 AM to 4:00 PM EST.
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/SAMANTHA LAKE HOPKINS/Examiner, Art Unit 1641
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641