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 .
Claim Rejections - 35 USC § 112
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 19 and 20 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.
Claims 19 and 20 depend from claim 18, which has been canceled. Therefore claims 19 and 20 are vague and indefinite. For examination purposes, claims 19 and 20 will be interpreted as dependent from claim 16. However, clarification is required.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 16, 17 and 22-25 are rejected under 35 U.S.C. 103 as being unpatentable over Pescovitz et al. (WO 2009/120651 A1, IDS, 10/28/2021), in view of van de Donk et al. (Blood. 2016, IDS, 10/28/2021).
Regarding claim 16, Pescovitz discloses a kit for removing one or more therapeutic monoclonal antibodies from a biological sample, said kit comprising a solid support and one or more antigens, wherein the one or more antigens are specific for the one or more therapeutic antibodies (para [0012] "there is provided a kit for treating a sample ..., wherein the patient has been administered a monoclonal antibody treatment, the kit comprising a peptide, wherein the peptide selectively binds the monoclonal antibody and a solid support, wherein the peptide is conjugated to the solid support. The solid support may be a magnetic bead, a non-magnetic bead, a microtiter plate or a tube").
Regarding claim 16, Pescovitz fails to teach the monoclonal antibody is either daratumumab and elotuzumab, the antigen is CD38 (required by claim 16).
However, van de Donk teaches that CD38 is an antigen targeted by therapeutic monoclonal antibodies (abstract “Immunotherapeutic strategies are emerging as promising therapeutic approaches in multiple myeloma (MM), with several monoclonal antibodies in advanced stages of clinical development. Of these agents, CD38-targeting antibodies have marked single agent activity”, pg 682, col 1, para 3 "Daratumumab… isatuximab... and MOR202… are CD38-targeting antibodies"). Van de Donk teaches there are interference problems with these monoclonal antibodies in laboratory tests which need a solution (abstract "Therapeutic antibodies interfere with several laboratory tests. First, interference of therapeutic antibodies with immunofixation and serum protein electrophoresis assays may lead to underestimation of complete response”, pg 689, col 1 para 2 “mitigation strategies are needed to remove interference of the therapeutic antibody").
It would have been prima facie obvious for one of ordinary skill in the art at the time of filing to modify the kit of Pescovitz by substituting the CD38 peptide for the CD20 peptide, thereby resulting in a CD38 conjugated bead, in order to remove interfering therapeutic monoclonal anti-CD38 antibodies from biological samples as described and suggested by the teachings of van de Donk.
Moreover, regarding claim 16, Pescovitz et al. does not disclose that the antigen is SLAMF7 (required by claim 16).
However, van de Donk teaches that SLAMF7 is an antigen targeted by therapeutic monoclonal antibodies (abstract “Immunotherapeutic strategies are emerging as promising therapeutic approaches in multiple myeloma (MM), with several monoclonal antibodies in advanced stages of clinical development… elotuzumab (anti-SLAMF7)”, pg 682, col 1, para 2 “Elotuzumab… is an antibody targeting signaling lymphocytic activation molecule F7 (SLAMF7, also called CS1)”. Van de Donk teaches there are interference problems with these monoclonal antibodies in laboratory tests which need a solution (abstract "Therapeutic antibodies interfere with several laboratory tests. First, interference of therapeutic antibodies with immunofixation and serum protein electrophoresis assays may lead to underestimation of complete response”, pg 689, col 1 para 2 “mitigation strategies are needed to remove interference of the therapeutic antibody").
It would have been prima facie obvious for one of ordinary skill in the art at the time of filing to modify the kit of Pescovitz by substituting the SLAMF7 peptide for the CD20 peptide, thereby resulting in a SLAMF7 conjugated bead, in order to remove interfering therapeutic monoclonal anti-SLAMF7 antibodies, including elotuzumab, from biological samples as described and suggested by the teachings of van de Donk.
Claim 16 also recites “the one or more antigens is each at an approximate total concentration of between 1x10-6M and 5x10-5M on an aggregate of more than one of the solid support.”
Neither Pescovitz nor van de Donk disclose this concentration for the biomarkers.
Examiner notes that, under the broadest reasonable interpretation, “an aggregate of more than one of the solid support” encompasses all of the solid supports (beads) used, or any subset of the solid supports (beads) used.
Moreover, the recited concentration of beads falls within a workable or optimum range.
Where the general conditions of the claim are disclosed, discovery of a workable or optimum range requires ordinary skills in the art, rendering the discovery obvious. One skilled in the art would have been motivated to discover a workable range, or to optimize to achieve the best result. Such discovery merely requires modifying a parameter of a known limitation, in this case, the concentration of the antigens on an aggregate of the beads. The knowledge and skills to achieve this modification would have been possessed by one skilled in the assay art, rendering the modification obvious.
Regarding claim 17, Pescovitz discloses a kit for removing one or more therapeutic monoclonal antibodies from a biological sample using peptides linked to a solid support, as discussed for claim 16. Pescovitz further discloses the kit of claim 16, wherein the solid support is a bead or particle (para [0025] “After the desired peptide or peptides have been selected they may be immobilized by conjugation onto a solid support such as, but not limited to, beads").
Regarding claims 22-25, Pescovitz discloses a kit for removing one or more therapeutic monoclonal antibodies from a biological sample using peptides linked to a solid support, as discussed for claim 16. The “wherein” clauses of these claims recite limitations that further define the preamble of claim 16 “a kit for removing one or more therapeutic monoclonal antibodies from a biological sample”:
However, the “biological sample” in claim 16 is only part of the intended use of the kit. If the body of a claim fully and intrinsically sets forth all of the limitations of the claimed invention, and the preamble merely states, for example, the purpose or intended use of the invention, rather than any distinct definition of any of the claimed invention's limitations, then the preamble is not considered a limitation and is of no significance to claim construction. In other words, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. See MPEP 2111.02 (II). The prior art kit would be capable of performing the claimed uses for a “biological sample”. Regardless, Pescovitz teaches that the biological sample is serum (para [0021] “the biological sample, may be, but is not limited to, a serum or plasma sample”, abstract), derived from a subject having a plasma cell disorder (para [0002], “Rituximab was initially developed for the treatment of B cell lymphoma, using its ability to bind to CD20 on B cells”, para [0011] a method of treating a biological sample from a patient …wherein the patient has been administered rituximab”), and from a human patient (para [0021] “depleting a biological sample from a patient … of at least one monoclonal antibody”, [0014-0017], “human serum”).
Claim 19 is rejected under 35 U.S.C. 103 as being unpatentable over Pescovitz et al. (WO 2009/120651 A1, IDS, 10/28/2021), in view of van de Donk et al. (Blood. 2016, IDS, 10/28/2021), as applied to claim 16 above, and further view of Doshi (2015 US 2015/0246123 A1, IDS, 10/28/2021).
Pescovitz and van de Donk have been discussed above. Van de Donk fails to teach the CD38 antigen sequence.
However, Doshi teaches SEQ ID NO: 2, a 14 amino acid CD38 peptide that binds to a therapeutic monoclonal antibody, the peptide having 100% identity to SEQ ID NO: 8 of this application (para [0079] “a method of treating a subject having a CD38-positive hematological malignancy, comprising administering to a patient in need thereof an anti-CD38 antibody that binds to the region SKRNIQFSCKNIYR (SEQ ID NO: 2)… of human CD38", para [0045] "the CD-38 positive hematological malignancy is multiple myeloma").
It would have been prima facie obvious for one of ordinary skill in the art at the time of filing to modify the kit of Pescovitz by substituting the CD38 peptide for the CD20 peptide, thereby resulting in a CD38 conjugated bead, in order to remove interfering therapeutic monoclonal anti-CD38 antibodies from biological samples as described by van de Donk, as mentioned further above.
Further, it would have been prima facie obvious to use the specific CD38 peptide sequence taught by Doshi with the beads in the kit taught by Pescovitz to remove therapeutic monoclonal anti-CD38 antibodies from biological samples, because it was known that anti-CD38 antibodies bind to this sequence, as taught by Doshi. It is obvious to use a known antigen for its art recognized purpose. In this case, the anti-CD38 antibodies that would have been removed would necessarily include daratumumab as required by independent claim 16. One would have had a reasonable expectation of success in combining the CD38 peptide of Doshi with the kit of Pescovitz because conjugation of peptides to beads was well known in the art at the time of filing as described by Pescovitz (para [0025] “the peptide may be conjugated to the solid support by methods known in the art”), and as such, the artisan would have expected success in conjugating CD38 peptide in the same way the CD20 peptide was conjugated to beads as taught by Pescovitz.
Claim 20 is rejected under 35 U.S.C. 103 as being unpatentable over Pescovitz et al. (WO 2009/120651 A1, IDS, 10/28/2021), in view of van de Donk et al. (Blood. 2016, IDS, 10/28/2021), as applied to claim 16 above, and in further view of Andre et al. (US 2016/0257750 A1, PTO-892, 04/22/2025).
Regarding claim 20, Pescovitz and van de Donk do not disclose that the SLAMF7 sequence, specifically the amino acid sequence of SEQ ID NO: 11 (required by claim 20).
However, Andre teaches SEQ ID NO: 29, a 334 amino acid SLAMF7 polypeptide comprising an amino acid sequence with 100% sequence identity to SEQ ID NO: 11 of this application (para [0003] “CS1 (also known as SLAMF7…) is a cell surface glycoprotein that is highly expressed on multiple myeloma (MM) cells”, [0102] “The complete CS1 sequence can be found under GenBank Accession No.: NM_021181.3 and is as follows: (SEQ ID NO:29)”) and is a target of therapeutic antibodies (para [0008] “An exemplary anti-CS1 antibody is elotuzumab”).
It would have been prima facie obvious for one of ordinary skill in the art at the time of filing to modify the kit of Pescovitz by substituting the SLAMF7 peptide for the CD20 peptide, thereby resulting in a SLAMF7 conjugated bead, in order to remove interfering therapeutic monoclonal anti-SLAMF7 antibodies, including elotuzumab, from biological samples as described by van de Donk, as discussed further above. Further, it would have been prima facie obvious to use the specific SLAMF7 (CS1) peptide sequence taught by Andre with the beads in the kit taught by Pescovitz to remove therapeutic monoclonal anti-SLAMF7 (anti-CS1) antibodies from biological samples, because it is was known that anti-SLAMF7 (anti-CS1) antibodies (e.g. elotuzumab) bind to this sequence, as taught by Andre. It is obvious to use a known antigen for its art recognized purpose. The artisan would have had a reasonable expectation of success in combining the SLAMF7 (CS1) peptide of Andre with the kit of Pescovitz because conjugation of peptides to beads was well known in the art at the time of filing as described by Pescovitz (para [0025] “the peptide may be conjugated to the solid support by methods known in the art”). As such, the artisan would have expected success in conjugating the SLAMF7 (CS1) peptide as was done for the CD20 peptide taught by Pescovitz.
Response to Arguments
Applicant's arguments and affidavit filed 4/9/26 have been considered but are not persuasive.
Applicant asserts that Pescovitz does not teach or suggest a solid support loading concentration, but rather teaches the final in-solution concentration of antigen, or the concentration of the antigen in the sample solution. Applicant asserts that Pescovitz has no teaching about what the antigen concentration is prior to mixing the antigen (whether solid support bound or not) with the sample solution. Applicant states that, as noted in the declaration, the in-solution and solid-support concentrations are not the same number, and that one of ordinary skill in the art would need to work backwards from the in-solution concentration to determine the solid-support concentration taking into account many different parameters. Applicant also asserts that Pescovitz only teaches the in-solution concentration of CD20, and does not teach or suggest the solid support concentration of an entirely different antigen, CD38. Similarly, Applicant asserts that the cited references do not teach the solid support concentration for SLAMF7
Examiner acknowledge that neither Pescovitz, van de Donk et al., nor Doshi disclose the concentration of the biomarkers on the solid support, nor specifically this concentration being specifically between 1x10-6M and 5x10-5M. Examiner also acknowledges that the in-solution and solid-support concentrations are not necessarily the same number. However, such knowledge would have been possessed by the skilled artisan in the assay art. Moreover, it would have been within the skills of the ordinary artisan to discover the solid-support concentration that would be workable or optimal for the purposes disclosed by the prior art.
As mentioned in the grounds for rejection, where the general conditions of the claim are
disclosed, discovery of a workable or optimum range requires ordinary skills in the art, rendering the discovery obvious. One skilled in the art would have been motivated to discover a workable range, or to optimize to achieve the best result. Such discovery merely requires modifying a parameter of a known limitation, in this case, the concentration of the antigens on an aggregate of the beads. The knowledge and skills to achieve such modification would have been possessed by one skilled in the art, rendering the modification obvious.
Conclusion
No claim is allowed.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Ann Montgomery whose telephone number is (571)272-0894. The examiner can normally be reached Mon-Fri, 9-5:30 PM PST.
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/Ann Montgomery/ Primary Examiner, Art Unit 1678
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