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 1-15 are pending. Claims 1-9 and 14 are drawn to the nonelected invention. Claims 10-13 and 15 are under examination.
Election/Restrictions
Applicant’s election without traverse of Group II (claims 10-13 and 15) in the reply filed on 02/06/2026 is acknowledged. Applicant has further elected the sequence of 19th to 133rd sequence of the amino acid sequence set forth in SEQ ID NO: 1.
Claims 1-9 and 14 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse.
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 10-13 and 15 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 measurement method for a test substance using a solid phase on which the polypeptide is immobilized, but the claim is unclear to the process of obtaining the measurement. In particular, the claim is unclear to the relationship between the polypeptide and the capture body with L-biotin. Is the capture body attached to the polypeptide or L-biotin or neither? Although the claim does recite the capture body is added with L-biotin, is unclear whether the L-biotin is linked or conjugated to the capture body or maybe the test substance? Is there a second capture body in the assay that is conjugated to L-biotin because the recited capture body immobilized on the solid phase when the test substance is detected. Therefore, it is unclear to a method that does not provide a clear relationship between structural elements to produce the recited outcome of measurements in the presence of a test substance.
Because said measurement method only recites a single general step of using a solid phase and the other elements are “wherein” clauses, it is unclear to what are the steps that would bring said method to produce a measurement. A measurement process without meaningful steps would raise an issue of clarity in the process of obtaining measurement data in the presence of the test substance. MPEP 2173.05(q) states that “For example, a claim which read: "[a] process for using monoclonal antibodies of claim 4 to isolate and purify human fibroblast interferon" was held to be indefinite because it merely recites a use without any active, positive steps delimiting how this use is actually practiced. Ex parte Erlich, 3 USPQ2d 1011 (Bd. Pat. App. & Inter. 1986)” (Emphasis added).
Additionally, the claim recites the polypeptide “comprises a D-amino acid residue in 90% or more of amino acid residues among amino acid residues other than glycine” is unclear to (1) how a single D-amino acid residue can be a part of the 90% or more residues and (2) is the D-amino acid residues within the 90% or more residues or 90% or more amino acids are D-amino acid residues?
Lastly, the recitation of “a multimer having the polypeptide as a monomer unit” is not structurally distinct from the recited polypeptide. Because the claim recites an alternative to a polypeptide is a multimer and a multimer only requires a polypeptide (as recited), it is unclear to what is the distinction between the polypeptide and the multimer in this claim. Claims 11-13 are rejected as being dependent from claim 10.
With respect to claim 15, as stated above, because said measurement method only recites a single general step of employing the kit and the other elements in the independent claim are “wherein” clauses, it is unclear to what are the steps that would bring said method to produce a measurement. A measurement process without meaningful steps would raise an issue of clarity in the process of obtaining measurement data because it merely recites a use without any additional active, positive steps delimiting how this kit is actually practiced to produce measurements.
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 10-13 and 15 are rejected under 35 U.S.C. 103 as being unpatentable over Theodore et al. (US2003/0129191A1, published 07/10/2003), as evidenced by Masatoshi et al. (“Mirror-image streptavidin with specific binding to L-biotin, the unnatural enantiomer” Scientific Reports, 2022, vol. 12, 9568, pgs. 1-9) and Takakura et al. (“Tamavidins - novel avidin-like biotin-binding proteins from the Tamogitake mushroom”, FEBS Journal, vol. 276, pgs. 1383-1397, published 2009).
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 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 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 prelocalization of biotinylated monoclonal antibody; administration of avidin for formation of a sandwich at the target site (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]). Theodore teaches the antibody is used as a targeting moiety and tumor is used a target (at para. [0042]). Theodore teaches enzymes are chiral molecules having strict selectivity for substrates with the correct stereochemical configuration (at para. [0326]). Theodore teaches any inefficiencies in in vivo operation of pretreating protocols caused by endogenous biotin can be obviated or substantially reduced by forming streptavidin or avidin of D-amino acids (at para. [0328]). Theodore teaches a schematic of sandwich assay (at para. [0059]).
Even though Theodore teaches the ability to bind to L-biotin by forming avidin or streptavidin with D-amino acids, the reference does not explicitly teach binding L-biotin to the polypeptide or the multimer comprising a D-amino acid residue in the polypeptide or multimer other than glycine.
However, it would have been obvious before the effective filing date of the claimed invention to have produced an avidin or streptavidin with D-amino acid residues as taught by Theodore for the binding of L-biotin because Theodore recognizes that L-biotin is produced and utilized in situations where endogenous biotins (D-biotins) are not effective. Therefore, it would have been obvious to have used an effective avidin or streptavidin against L-biotin in an immunoassay reaction for effective binding relationship of streptavidin and biotin. Because Theodore recognizes that avidin or streptavidin with D-amino acid residues has a strong correlation to L-biotin, for the exception of achiral amino acid residues, it would have been obvious to have modified all the non-achiral residues of avidin or streptavidin for the ability to strongly interact with L-biotin.
Meanwhile, the evidentiary teachings of Masatoshi indicate that the streptavidin peptide compose of D-amino acids and achiral glycine (at pg. 2, para. 1 of Results and discussion). Therefore, it would have been obvious to have modified all non-achiral residues to D-amino acid residues of avidin or streptavidin for the exception of achiral amino acids because achiral molecules are chemical structures that are superimposable on their mirror images, which already possess symmetry.
With respect to the elected species, the evidentiary teachings of Takakura indicate that streptavidin has the claimed amino acid sequence of SEQ ID NO: 1 (see Fig. 2 under Streptavidin_mat).
The person would have a reasonable expectation of success in modifying the amino acids of streptavidin or avidin to the D-amino acid stereoisomer because Theodore recognizes producing L-biotin and D-amino acid residues strongly bind to L-biotin.
With respect to claim 11, Theodore teaches biotinylated antibody species exhibited 98% specific binding to immobilized avidin-agarose (at bottom of para. [0421]).
With respect to claim 12,Theodore teaches a schematic at para. [0059], which would read on contacting the solid phase, the capture body, a detector that binds to the test substance, and the test substance with each other to form a complex containing the solid phase, the capture body, the detector, and the test substance; and measuring the test substance based on the detector contained in the complex. Theodore teaches streptavidin-agarose bead and biotinylated, radiolabeled protein was added to beads (at right col. of para. [0519]).
With respect to claim 13, Theodore teaches streptavidin-agarose bead and biotinylated, radiolabeled protein was added to beads (at right col. of para. [0519]).
With respect to claim 15, see stated discussion. However, Theodore does not specifically invoke the terminology “kit”. Meanwhile, the term kit is not found to further limit the scope of the claims beyond the reagents. This terminology of a “kit” does not clearly invoke any additional ingredients or provide antecedent basis for terms appearing in the body of the claim (such as specific packaging or container elements, for example). See also MPEP 2111.02.
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 10-13 and 15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 6-16 of copending Application No. 18/179,759 (‘759) in view of Theodore et al. (US2003/0129191A1, published 07/10/2003), as evidenced by Masatoshi et al. (“Mirror-image streptavidin with specific binding to L-biotin, the unnatural enantiomer” Scientific Reports, 2022, vol. 12, 9568, pgs. 1-9).
Application ‘759 recites in claim 6 a method for measuring a sample comprising L-biotin, comprising: preparing a measurement sample by mixing a sample comprising L-biotin with the reagent for measuring L-biotin according to claim 1; and measuring absorbance of the measurement sample, the measured value of absorbance being an index of concentration of L-biotin in the sample. Claim 8 recites a method for determining a number of labels of an L-biotin-labeled substance, comprising: preparing a measurement sample by mixing a sample comprising an L-biotin-labeled substance with the reagent for measuring L-biotin according to claim 1; measuring absorbance of the measurement sample; determining a concentration of L-biotin in the sample based on the measured value of absorbance; and determining a number of L-biotin groups per molecule of the L-biotin-labeled substance based on the concentration of L-biotin in the sample and a concentration of the substance. Claim 13 recites a method for producing a solid phase on which an optically isomeric biotin-binding site is immobilized, comprising: preparing a measurement sample by mixing a sample separated from a liquid comprising an L-biotin-labeled polypeptide with the reagent for measuring L-biotin according to claim 1; measuring absorbance of the measurement sample; determining a concentration of L-biotin in the measurement sample based on the measured value of absorbance; determining a number of L-biotin groups per molecule of the L-biotin-labeled polypeptide in the sample based on the concentration of L-biotin and a concentration of the polypeptide; when the number of L-biotin groups is within a predetermined range, contacting the liquid with a solid phase capable of binding to the polypeptide to immobilize the L-biotin-labeled polypeptide on the solid phase; and contacting the solid phase on which the L-biotin-labeled polypeptide is immobilized with an optically isomeric biotin-binding site to immobilize the optically isomeric biotin-binding site on the solid phase. Claim 9 recites comprising determining the concentration of the substance in the sample.
Copending Application ‘759 does not recite the polypeptide belongs to the avidin-streptavidin family comprises a D-amino acid residue in 90% or more of amino acid residues among amino acid residues other than glycine. Theodore and Masatoshi have been discussed above.
Therefore, it would have been obvious at the time of filing to have used the L-biotin conjugated to antibody as recited by the copending Application with an avidin or streptavidin with D-amino acid residues as taught by Theodore for strong affinity binding because Theodore recognizes using an effective avidin or streptavidin against L-biotin in an immunoassay reaction for effective binding relationship of streptavidin and biotin. Because Theodore recognizes that avidin or streptavidin with D-amino acid residues has a strong correlation to L-biotin, for the exception of achiral amino acid residues, it would have been obvious to have used avidin or streptavidin comprising D-amino acid residues for the ability to strongly interact with L-biotin.
Meanwhile, the evidentiary teachings of Masatoshi indicate that the streptavidin peptide compose of D-amino acids and achiral glycine (at pg. 2, para. 1 of Results and discussion). Therefore, it would have been obvious to have modified all non-achiral residues to D-amino acid residues of avidin or streptavidin for the exception of achiral amino acids because achiral molecules are chemical structures that are superimposable on their mirror images, which already possess symmetry.
This is a provisional nonstatutory double patenting rejection.
Conclusion
No claim is allowed.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678