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 .
Applicant’s 3-5-26 election of the invention of Group I, without traverse, and applicant’s further election of species of “the following CDR sequences (IMGT numbering scheme) of the antibody clone MAB-19-0202: HCDR1: SEQ ID NO: 28; HCDR2: SEQ ID NO: 11; HCDR3: SEQ ID NO: 6; LCDR1: SEQ ID NO: 42; LCDR2: QAS; and LCDR3: SEQ ID NO: 33. The heavy chain variable region (VH) of antibody clone MAB-19-0202 is depicted in SEQ ID NO: 52, and the light chain variable region (VL) is depicted in SEQ ID NO: 57. A humanized antibody clones derived from MAB-19-0202 is MAB-19-0618 (VH: SEQ ID NO: 62; VL: SEQ ID NO: 68),” is acknowledged. With respect to applicant’s election of species response, because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Claims 20, 21, 24, 27, 30, 33, 36, 38, 40, 45, 47, 49-57, 64-68, 75, 77, 89, 91-95, 99-101 and 104-106 are pending.
Claims 20, 21, 36, 38, 40, 45, 47, 49, 51-57, 64-68, 75, 77 and 104-106 are under examination as they read on the elected species of invention: “the following CDR sequences (IMGT numbering scheme) of the antibody clone MAB-19-0202: HCDR1: SEQ ID NO: 28; HCDR2: SEQ ID NO: 11; HCDR3: SEQ ID NO: 6; LCDR1: SEQ ID NO: 42; LCDR2: QAS; and LCDR3: SEQ ID NO: 33. The heavy chain variable region (VH) of antibody clone MAB-19-0202 is depicted in SEQ ID NO: 52, and the light chain variable region (VL) is depicted in SEQ ID NO: 57. A humanized antibody clones derived from MAB-19-0202 is MAB-19-0618 (VH: SEQ ID NO: 62; VL: SEQ ID NO: 68).”
Claims 24, 27, 30, 33, 50, 89, 91-95 and 99-101 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Group or Species of invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 3-5-26.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 53, 57, 64 and 65 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 53 recites “The antibody or the antigen-binding fragment thereof of claim 20, wherein the antibody or the antigen-binding fragment thereof is a Fab fragment, F(ab')2 fragment, Fv fragment, or a single chain (scFv) antibody.” The skilled artisan would not be clear as to how exactly the “…is a Fab fragment, F(ab')2 fragment, Fv fragment, or a single chain (scFv) antibody” language modifies the “the antibody or the antigen-binding fragment thereof” language of this claim. Some may assert that the language of this claim is non-sensical because it lacks a noun modifier for “the antibody,” i.e., it recites “The antibody or the antigen-binding fragment thereof of claim 20, wherein the antibody….” and fails to state anything about “the antibody.” However, others may argue that the language of this claim implies that the various fragment species explicitly recited in this claim can themselves be considered either (i) “the antibody” or (ii) “the antigen-binding fragment thereof.” If so, what exactly is meant by “an antibody” which “…is a Fab fragment, F(ab')2 fragment, Fv fragment, or a single chain (scFv) antibody” but is somehow distinct from “a fragment thereof”? For example, is this language meant to somehow imply that the PD-1 antibody may be, e.g., “a Fab fragment, F(ab')2 fragment, Fv fragment, or a single chain (scFv) antibody” so long as it is joined to an Fc domain? Different skilled artisans would have different opinions about how this language does or does not modify the metes and bounds of base claim 20.
The ordinarily skilled artisan would not understand how claim 57 could depend on base claim 20 in its preamble, and thus have all the limitations of claim 20 including, e.g., a heavy chain variable region (VH) comprising certain CDRs identified by SEQ ID NOs: AND a light chain variable region (VL) comprising certain CDRs identified by SEQ ID NOs:, and at the same time be drawn to “a multispecific antibody or the antigen-binding fragment thereof comprising a first antigen-binding region binding to PD- 1… wherein the first antigen-binding region binding to PD-1 comprises the heavy chain variable region (VH) and/or the light chain variable region (VL) as set forth in claim 20.” Given this contradictory language the skilled artisan would be uncertain where the metes and bounds of claim 57 lie.
Claim 64 and dependent claims thereof recites “[a] multimer, comprising at least two antibodies or antigen binding fragments thereof having the ability of binding to PD-1, wherein the antibody or antigen binding fragment thereof comprises a heavy chain.…” It would be unclear to the ordinarily skilled artisan if the preamble of this claim means the multimer, in general, binds to PD-1, but not necessarily via each of the “at least two antibodies or antigen binding fragments thereof” that it contains. According to such an interpretation, the claimed multimer could also be bispecific. Such an interpretation would be consistent with the teachings at, e.g., page 21, 1st full paragraph – page 22, 1st full paragraph; page 23, 3rd full paragraph – 4th paragraph.
However, a different interpretation would consider the language of claim 64 to imply that the “at least two antibodies or antigen binding fragments thereof” must themselves each bind to PD-1. If so, would a conventional antibody comprising two Fab domains joined to an Fc domain be considered to also be encompassed in the breadth of claim 64? For prior art examination purposes, each of the above interpretations of claim 64 will be considered as possibilities.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 56 and 57 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. The species of antibody of claim 20 under examination includes the heavy and light chain CDRs of SEQ ID NOs: (28, 11, 6)(VH) and (42, QAS, 33)(VL). As described in Example 1, antibodies comprising said CDRs were generated by immunizing rabbits with recombinant human His-tagged PD-1 protein, and then said antibodies were isolated based on cellular human PD-1 binding assay and by human PD-1/PD-Ll blockade bioassay as described in Examples 3-4. For example, in example 3 the ability of said antibodies to bind to cell surface expressed hPD-1 was analyzed using HEK-293 cells ectopically expressing full-length human-PD1. At page 130, 1st full paragraph, the specification teaches: “Binding curves for the cellular binding of the chimeric anti-PD-1 antibodies MAB-19-0202…to human-PD- 1 were comparable to the reference antibodies anti-hPD-1-Ni-hlgG4 and anti-hPD1-Pem-hlgG4 as shown in Figure 2.” Thus, the teachings of the instant specification demonstrate that the antibodies of claim 20 inherently have the requisite structure for binding to the native epitope of PD-1 present on the surface of living cells. Therefore, claim 56 fails to further limit the subject matter of the claim upon which it depends.
Turning to claim 57, this claim recites “The antibody or the antigen-binding fragment thereof of claim 20 , wherein the antibody or the antigen-binding fragment thereof is a multispecific antibody or the antigen-binding fragment thereof comprising a first antigen-binding region binding to PD- 1… wherein the first antigen-binding region binding to PD-1 comprises the heavy chain variable region (VH) and/or the light chain variable region (VL) as set forth in claim 20.” As described above the meaning of this claim would be unclear to the ordinarily skilled artisan, that said, assuming arguendo that the preamble of claim 57 (“The antibody or the antigen-binding fragment thereof of claim 20 , wherein the antibody or the antigen-binding fragment thereof is a multispecific antibody or the antigen-binding fragment thereof comprising”) is not controlling, how could the antibody of claim 57 which has a first antigen-binding region binding to PD-1 which comprises the heavy chain variable region (VH) and/or the light chain variable region (VL) as set forth in claim 20 be said to be further limiting claim 20? Instead, the highlighted language above expands the breadth of claim 57 beyond that of base claim 20.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim(s) 66, 68, 75 and 77 are rejected under 35 U.S.C. 102(a)(1)/(a)(2) as being anticipated by Carven et al. (9834605, cited herewith).
Carven teaches a nucleic acid comprising a nucleic acid sequence encoding an antibody or antigen binding fragments thereof having the ability of binding to PD-1 (see Example 4), and further teaches host cells comprising said nucleic acid (see, e.g., claim 4 and col. 7, 2nd full paragraph from the bottom). Carven further teaches pharmaceutical compositions comprising an active agent, wherein the active agent is an antibody having the ability of binding to PD-1, and wherein the pharmaceutical compositions suitable for cardiovascular administration such as subcutaneous, intraperitoneal, parenteral, intraarterial or intravenous injection (see, e.g., at col. 20, 2nd full paragraph). Thus, the teachings of Carven anticipate the instant claims.
Note that claims 66, 75 and dependent claims thereof read on “[a] nucleic acid comprising a nucleic acid sequence encoding (i) an antibody or antigen binding fragments thereof having the ability of binding to PD-1 or….,” and “[a] pharmaceutical composition comprising an active agent and a pharmaceutically acceptable carrier, wherein the active agent is an antibody or antigen binding fragment thereof having the ability of binding to PD-1, or….,” respectively, which is the embodiment anticipate by the teachings of Craven.
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.
Claim(s) 66, 67, 68, 75, 77 and 106 are rejected under 35 U.S.C. 103 as being unpatentable over Carven et al. (9834605) as applied to claims 66, 68, 75 and 77 above, and further in view of Rybakova et al. (Mol Ther. 2019 Aug 7;27(8):1415-1423, cited herewith).
The teachings of Craven as applied to claims 66, 68, 75 and 77 are set forth above.
However, Craven does not explicitly teach either “[a] nucleic acid comprising a nucleic acid sequence encoding (i) an antibody or antigen binding fragments thereof having the ability of binding to PD-1…, wherein the nucleic acid is RNA (claim 67), or “a pharmaceutical composition comprising an active agent and a pharmaceutically acceptable carrier, wherein the active agent is an antibody or antigen binding fragment thereof having the ability of binding to PD-1…, wherein the active agent is nucleic acids and the antibody heavy chain and the antibody light chain of the encoded antibody or the antigen binding fragment thereof are encoded by separate nucleic acids” (claim 106).
Rybakova teaches the use of lipid-based nanoparticles (LNPs) for in vivo delivery of in-vitro-transcribed mRNA (IVT-mRNA) encoding a biologic therapeutic such as an antibody-based drug like the anti-Her2 antibody trastuzumab (see Abstract and Introduction), which offers several advantages over conventional manufacturing and delivery of antibodies (see 1st paragraph Discussion). As shown in Fig. 1A of Rybakova, the mRNAs encoding antibody heavy and light chains occur as separate nucleic acids, consistent with claim 106.
Given the reference teachings it would have been obvious to one of ordinary skill in the art that LNPs comprising IVT-mRNAs encoding the heavy and light chains of the anti-PD-1 antibodies of Craven provide an alternative means to delivery anti-PD-1 antibodies to a patients that offers several advantages over conventional manufacturing and delivery of antibodies. Thus, it would have been obvious to one of ordinary skill in the art to make RNA-based nucleic acids encoding the heavy and light chains of the anti-PD-1 antibodies of Craven to enable in vivo delivery as described by Rybakova.
In view of the reference teachings it was apparent that one of ordinary skill in the art would have had a reasonable expectation of success in arriving at the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made.
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 20, 21, 45, 47, 49, 51-56, 64, 66, 75 and 77 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 6-8, 18-20, 24 and 27 of U.S. Patent No. 11932693 (cited on an IDS). Although the claims at issue are not identical, they are not patentably distinct from each other because the reference claims anticipate the instant claims.
Reference claims 6 and 7 are drawn to the antibody or the antigen-binding fragment thereof of claim 1 having the heavy and light chain variable domains of SEQ ID NOs: 20 and 21; likewise,
reference claims 18 and 19 are drawn to the nucleic acid of claim 12, wherein the encoded heavy chain variable region (VH) comprises…the amino acid sequence of the VH sequence as set forth in SEQ ID NO: 20, and the encoded light chain variable region (VL) comprises…the amino acid sequence of the VH sequence as set forth in SEQ ID NO: 21.
The reference SEQ ID NOs: 20 and 21 are identical to SEQ ID NOs: 62 and 68 of the instant claims.
Furthermore, reference claim 8 is drawn to the antibody or the antigen-binding fragment thereof of claim 1, wherein the heavy chain comprises the sequence as set forth in SEQ ID NO: 56, and the light chain comprises the sequence as set forth in SEQ ID NO: 57.
Moreover, reference claim 18 is drawn to “The nucleic acid of claim 12, wherein the encoded heavy chain variable region (VH) comprises…the amino acid sequence of the VH sequence as set forth in SEQ ID NO: 20, and the encoded light chain variable region (VL) comprises a sequence…as set forth in SEQ ID NO: 21.”
Additionally, reference claim 20 is drawn to the nucleic acid of claim 12, wherein the encoded heavy chain comprises the sequence as set forth in SEQ ID NO: 56, and the encoded light chain comprises the sequence as set forth in SEQ ID NO: 57.0
As to reference claim 24 it recites “[t]he pharmaceutical composition of claim 21, wherein the heavy chain of the antibody comprises the sequence as set forth in SEQ ID NO: 56, and the light chain of the antibody comprises the sequence as set forth in SEQ ID NO: 57,” and further reference claim 27 recites “[t]he pharmaceutical composition of claim 25, wherein the encoded heavy chain comprises the sequence as set forth in SEQ ID NO: 56, and the encoded light chain comprises the sequence as set forth in SEQ ID NO: 57.”
The reference SEQ ID NOs: 56 and 57 comprise SEQ ID NOs: 62 and 68 of the instant claims.
Thus, reference claims 6-8, 18-20, 24 and 27 anticipate instant claims 20, 21, 45, 47, 49, 51-56, 64, 66, 75 and 77.
Claim 57 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 6-8, 18-20, 24 and 27 of U.S. Patent No. 11932693 in view of Fayadat-Dilman et al. (20190233518, cited herewith) and NCT03708328 (NLM, “A Dose Escalation and Expansion Study of Lomvastomig, a PD-1/TIM-3 Bispecific Antibody, in Participants With Advanced and/or Metastatic Solid Tumors,” pages 1-29, October 12, 2018, cited herewith).
Fayadat-Dilman describes the production of a bispecific PD1xLAG-3 antibody and its use for the treatment of various cancers (see, e.g., at para 16; at Sections 5.5, 5.12 and 6.3). NCT teaches a clinical trial of another bispecific PD1xLAG-3 antibody in various cancer patients (see pages 9, 11-12).
Given the reference teachings it would have been obvious to one of ordinary skill in the art to make the antibodies of the reference claims multispecific for the purpose of targeting not only PD-1 but also targeting another other T-cell inhibitory surface proteins such as LAG-3 which was known to be “…expressed on tolerized TILs suggesting that they contribute to tumor-mediated immune suppression. Inhibition of LAG3 may lead to enhanced activation of antigen-specific T cells from which a therapeutic benefit may be gained,” as described by Fayadat-Dilman at para 8. One of ordinary skill in the art would have had a reasonable expectation of success in doing so based not only on the teachings of Fayadat-Dilman but also on the clinical trial described by NCT wherein a PD-1/TIM-3 bispecific antibody was administered to participants with advanced and/or metastatic solid tumors.
In view of the reference teachings it was apparent that one of ordinary skill in the art would have had a reasonable expectation of success in arriving at the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made.
Claim 64, 65, 104 and 105 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 6-8, 18-20, 24 and 27 of U.S. Patent No. 11932693 in view of Liu et al. (Biochem. J. (2007) 406, 237–246, cited herewith) and Rashidian et al. (Proc Natl Acad Sci U S A. 2019 Aug 20;116(34):16971-16980, cited herewith).
The teachings of reference claims 6-8, 18-20, 24 and 27 are given above.
However, the reference claims do not anticipate the multimer of claim 65 having 4-9 antibodies or antigen binding fragments thereof, nor do they teach coupling the anti-PD-1 antibodies to a radioisotope.
Liu teaches a protein multimer comprising at least four copies of anti-TNFα scFv joined to a p53 multimerization domain wherein the anti-TNFα scFv p53 multimerization domains form tetramers which are soluble in an aqueous medium (see page 239, left col., at lines 21-24; page 240, right col., last paragraph - page 241, left col., 2nd full paragraph and Figs. 1A and 1B). Liu teaches tetramerization of the TNFα binding domain “…resulted in an enormous gain in avidity, which endowed TNF-TeAb with a stronger ability to inhibit both receptor binding and cytolytic activity of TNF-α,” (see abstract) and further that “[t]he targeting efficacy of antibody fragments can be improved by the use of multimeric formats of antibody fragments with higher avidity and a molecular mass slightly above the renal-filtration threshold [4–6].” (see page 237 col. bridging paragraph). These advantages are further discussed in the first two paragraph of the Discussion section.
Rashidian teaches coupling a PD-1 binding antibody to a 89Zr radioisotope allows for noninvasive immuno-positron emission tomography (PET) imaging of PD-1 antibody in the body including when PD-1 expressing immune cells infiltrate the tumor microenvironment (see, e.g., Abstract and Introduction). Rashidian concludes: “As shown here, noninvasive imaging by immuno-PET can help monitor intratumoral CD8+ T cells, even without knowing their specificity, and gauge the progression of the antitumor response to anti–PD-1 treatment. Such observations might inform better decisions on treatment options for patients. Our findings provide an impetus for similar studies in a clinical setting to determine whether comparable results could assist in the early identification of responders and nonresponders.” (see last paragraph of Discussion).
Given the reference teachings it would have been obvious to one of ordinary skill in the art, and one of ordinary skill in the art would have been motivated to substitute, e.g., scFvs domains comprising the PD-1-binding heavy and light chain variable domains of the reference claims for the “Peprotech” anti-TNFα scFv of Liu. A motivation to make such a tetravalent PD-1 binding molecule was to increase the avidity and neutralizing potential of the PD-1 antibodies of the reference claims. Moreover, it further would have been obvious to one of ordinary skill in the art to couple said PD-1-binding tetramers to a radioisotope used for imaging purposes, e.g., Zr89, so as to be able to non-invasively track the movement of PD-1 expressing cells into the tumor tissue or elsewhere.
In view of the reference teachings it was apparent that one of ordinary skill in the art would have had a reasonable expectation of success in arriving at the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made.
No claims are allowed. However, claims 36, 38, 40 are objected to for being dependent on a rejected claim insofar as they read on the elected species of antibody comprising “the following CDR sequences (IMGT numbering scheme) of the antibody clone MAB-19-0202: HCDR1: SEQ ID NO: 28; HCDR2: SEQ ID NO: 11; HCDR3: SEQ ID NO: 6; LCDR1: SEQ ID NO: 42; LCDR2: QAS; and LCDR3: SEQ ID NO: 33. The heavy chain variable region (VH) of antibody clone MAB-19-0202 is depicted in SEQ ID NO: 52, and the light chain variable region (VL) is depicted in SEQ ID NO: 57. A humanized antibody clones derived from MAB-19-0202 is MAB-19-0618 (VH: SEQ ID NO: 62; VL: SEQ ID NO: 68)” as set forth by applicant in their remarks filed 3-5-26 at page 19-20 bridging paragraph – 1st full paragraph on page 20. Claims 36, 38 and 40 would be allowable if rewritten in independent form limited to the elected species of antibody. Additional species encompassed by claim 20 may be allowable as well but have not yet been examined on the merits.
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/ZACHARY S SKELDING/Primary Examiner, Art Unit 1644
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