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 .
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.
Status of Claims
Claims 1-11, 13-14, and 16-17 are pending. Claims 16-17 are new. Claims 1-9 and 14 are drawn to the nonelected invention. Claims 10, 11, 13 and 16-17 are under examination.
Withdrawn Rejection
In light of the amendments, the 35 U.S.C. 103 rejection over Theodore, as evidenced by Masatoshi, and Takakura is here by withdrawn.
In light of the approved terminal disclaimer dated 06/23/2026, the nonstatutory double patenting rejection over Application 18179759 is here by withdrawn.
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 10, 11, 13 and 16-17 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 10 recites “a multimer having the polypeptide as a monomer unit” is not structurally distinct from the recited polypeptide that is comprising (open-ended). Because the claim recites an alternative to a polypeptide is a multimer that only has the polypeptide as a monomer unit, it is unclear to what is the structural distinction between the polypeptide and multimer in the claim. Meanwhile, a “polypeptide comprising” (open-ended) may contain the other subunits to be a multimer. Although they are in the alternative form, these elements have the same structural limitations expressed by the claim. Also, the specification has not provided a definition for the structure of a multimer. Claims 11, 13 and 16-17 are rejected as being dependent from claim 10.
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.
Claims 10, 11, 13 and 16-17 are rejected under 35 U.S.C. 103 as being unpatentable over Wong et al. (US9353161B2 (Application No. 14343883), published 05/31/2016) in view of Theodore et al. (US2003/0129191A1, published 07/10/2003, see 892 dated 03/25/2026 ) and Cho et al. (“Site-directed Immobilization of Antibody onto Solid Surfaces for the Construction of Immunochip”, Biotechnology and Bioprocess Engineering, 2004, vol. 9, pgs. 112-117).
Wong teaches a new streptavidin muteins and the mutein binds to biotin or biotinylated molecules, does so in a reversible fashion and it is stable enough to allow reuse (see abstract). Wong teaches the streptavidin mutein comprising a substitution of the glycine at residue 48 corresponding to full-length wild-type streptavidin (SEQ ID NO: 1).
Sequence alignment of instant SEQ ID NO: 1 and Wong’s SEQ ID NO: 1:
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Wong teaches a method of binding a biotin to a solid matrix or support by a solid with the solid matrix or support comprising said streptavidin mutein (at col. 3, lines 55-63). Wong teaches the engineered streptavidin mutein is designated as SBPM18 (at col. 5, lines 25-27). Wong teaches that SBPM18 immobilizes to different platforms such as protein arrays, ELISA plates, magnetic beads, biosensor chips and bioreactors for different applications and antibodies (at col. 25, lines 17-25). Wong teaches ELISAs often makes use of biotinylated primary antibodies against the antigen of interest (at col. 8, lines 43-45). Wong teaches D-biotin was used (at col. 18, lines 10-12).
Because Wong teaches the claimed polypeptide (see above), Wong’s polypeptide would have a binding ability to L-biotin and has substantially no binding ability to D-biotin, wherein a specific change in a sensorgram due to binding to D-biotin is not detected by surface plasmon resonance (SPR). Note the recitation of SPR is in a wherein clause. Thus, these limitations are based on the ability and structures of the polypeptide rather being performed in an active step of SPR.
Although Wong teaches the streptavidin mutein (SBPM18) immobilizes to different platforms such as a solid matrix or support, the reference does not teach a detector that binds to the test substance and forming a complex of capture body, a detector and the test substance (i.e., sandwich assay). Additionally, Wong does not teach L-biotin.
Theodore teaches ELISA assay (at para. [0418] and Table 2). Theodore teaches sandwich assay for diagnostic (at paras. [0059] and [0061]). Theodore teaches the natural avidin and streptavidin are formed of L-amino acids to bind to D-biotin and the affinity of natural avidin and streptavidin for L-biotin is so low that L-biotin is non-competitive with D-biotin for such binding (at para. [0325]). Theodore further teaches that streptavidin or avidin formed with D-amino acids for interacting with L-biotin rather than D-biotin and the D-amino acid forms of streptavidin or avidin will show binding specificity for L-biotin rather than naturally occurring, endogenous D-biotin (at para. [0328]). Theodore also teaches that high affinity avidin or streptavidin-binding will be preserved in the mirror image format and biotin binding peptides may also be converted to mirror image configuration in this manner to bind L-biotin rather than D-biotin and preparation of mirror image biotin binding peptides may be conducted by solid phase peptide synthesis in accordance with known techniques therefor (at para. [0328]). Theodore teaches biotinylated monoclonal antibody (at para. [0415]). Theodore teaches biotinylated antibody species exhibited 98% specific binding to immobilized avidin-agarose (at bottom of para. [0421]). Theodore teaches streptavidin-agarose bead and biotinylated, radiolabeled protein was added to beads (at right col. of para. [0519]).
Cho teaches the biotinylated antibody was bound to a streptavidin-coated surface via the streptavidin-biotin reaction and this method can control the orientation of the antibody molecules present on a solid support and also can significantly reduce the possibility of steric hindrance in the antigen-antibody reactions (abstract). Fig. 4 shows the configurations of sandwich immune complexes formed in the respective immunoassay system with different capture antibodies (also at caption).
Therefore, it would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to have used the streptavidin mutein (SBPM18) as taught by Wong with L-biotin and sandwich assay as taught by Theodore because Wong teaches SBPM18 immobilizes to different platforms such as protein arrays and ELISA plates and Theodore recognizes that (1) streptavidin formed with D-amino acids interacts strongly with L-biotin rather than D-biotin and (2) high affinity streptavidin-binding will be preserved in the mirror image format and biotin binding peptides may also be converted to mirror image configuration to bind to L-biotin. Even though Wong recognizes that its streptavidin mutein (SBPM18) is for binding to D-biotin for reversibility in purification, the reference also recognizes that its streptavidin mutein (SBPM18) can be utilized in different platforms for detection. Based on the knowledge in the art, it would have been obvious to the person to have employed the sandwich assay as taught by Cho (Fig. 4) with the streptavidin mutein (SBPM18) of Wong with L-biotins because it has been recognized by Wong and Theodore the configurations of streptavidin and biotin for binding affinity and Cho teaches the ability to control orientation in sandwich assays with streptavidin-biotin reaction.
The person would have a reasonable expectation of success in using Wong’s streptavidin mutein (SBPM18) with L-biotin in a sandwich assay because it has been well understood in the art the configurations of streptavidin and biotin for sandwich assays.
With respect to claim 11, Although Wong teaches the streptavidin mutein (SBPM18) immobilizes to different platforms such as ELISA, the reference does not teach biotinylated antibody. Theodore teaches biotinylated monoclonal antibody (at para. [0415]). Cho teaches in Fig. 4 enzyme conjugate and biotinylated antibody (also at caption). It would have been obvious to have used streptavidin mutein (SBPM18) with biotinylated antibodies because Wong teaches that it’s streptavidin mutein (SBPM18) immobilizes to different platforms for immunoassay detection and Cho teaches the ability to control orientation in sandwich assays with streptavidin-biotin reaction.
With respect to claim 13, Wong teaches fluorescent dye or HRP can be applied to probing SBP tagged, biotinylated proteins, and ELISA but does not explicitly teach detector comprises a fluorescent substance or an enzyme. Cho teaches in Fig. 4 enzyme conjugate and biotinylated antibody (also at caption). It would have been obvious to have used enzyme such as HRP in a sandwich ELISA for detection.
With respect to claim 16, Wong teaches the claimed polypeptide (see above). Thus, Wong’s polypeptide would be able to have the claimed dissociation constant with D-biotin.
With respect to claim 17, Wong’s polypeptide of SEQ ID NO: 1 reads on the claimed sequence (SEQ ID NO:1).
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Response to Arguments
Applicant’s arguments filed 06/23/2026 have been considered but are moot because Applicant’s amendments necessitated a new ground of rejection. Because Theodore is used as a secondary reference, certain arguments will be addressed below.
Note that Applicant has added to the arguments documents that contain over 100 pages. However, Applicant has not disclosed what is the purpose of these documents with respect to the arguments. Therefore, these documents have not been considered as part of the arguments.
With respect to 35 U.S.C. 112(b), Applicant argues on page 9 that in biochemical arts, these distinct structural states, the monomer represents the individual block, whereas the multimer represents the functional complex of these monomers.
The argument is not found persuasive because the structure of the claimed “multimer having the polypeptide as a monomer unit” do not necessarily contain the other subunits. Meanwhile, a “polypeptide comprising” (open-ended) may also contain the subunits to be a multimer. Also, there is no definition in specification to the structure of a multimer. Thus, the phrase “multimer” does not provide any additional structural limitation to the claimed polypeptide.
With respect to 35 U.S.C. 103, Applicants argue on page 11 (last paragraph) that Theodore does not teach a polypeptide including a specific amino acid sequence as claimed, much less disclosed the specific SPR binding characteristics of the polypeptide (i.e., a specific change in a sensorgram due to binding to D-biotin is not detected by surface plasmon resonance (SPR)).
The arguments are not found persuasive for the following reasons. As stated above in the rejection, Wong teaches the claimed polypeptide. Because Wong teaches the claimed polypeptide (see above), Wong’s polypeptide would have a binding ability to L-biotin and has substantially no binding ability to D-biotin, wherein a specific change in a sensorgram due to binding to D-biotin is not detected by surface plasmon resonance (SPR). Note the recitation of SPR is in a wherein clause. Thus, these limitations are based only on the ability and structures of the polypeptide rather being performed in an active step of SPR.
For completeness, with respect to Masatoshi not being a prior art reference, the argument is not found persuasive because Masatoshi was used as an evidentiary art to establish the structure of streptavidin.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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