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.
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 04/20/2026 has been entered.
Status of Claims
Claims 1, 3, 8-11 and 17-21 are pending. Claims 17-21 are drawn to the nonelected invention. Claims 1, 3 and 8-11 are under examination.
Withdrawn Rejections
In light of the amendments, the 35 U.S.C. 102 rejection over Jegaskanda is hereby withdrawn.
In light of the amendments, the 35 U.S.C. 103 rejection over Dowell in view of Wessels is hereby withdrawn.
In light of the amendments and arguments, the 35 U.S.C. 112, new matter, rejection is hereby withdrawn.
New Rejections
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 1, 3 and 8-11 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.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 1 recites the broad recitation “wherein the target-binding entity comprises an Fc portion”, and the claim also recites “a target-binding entity that is an antibody or antibody fragment thereof that recognizes and binds the target” which is the narrower statement of the range/limitation. (Emphasis added). The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Even if the claim is amended to recite “antibody or antibody fragment thereof comprising an Fc portion”, the claim would be unclear to the metes and bounds of the structure of the antibody or antibody fragment binding to the target antigen only containing an Fc portion. The claim should reflect an Fc portion of the antibody or antibody fragment thereof. Also, claims 3 and 8-11 are rejected as being dependent from claim 1.
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, 3 and 8-10 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Shang et al. (“Multiplexed In-cell Immunoassay for Same-sample Protein Expression Profiling”, Scientific Reports, vol. 5:13651, pgs. 1-12, published 09/02/2015), as evidenced by Langone et al. (“Complexes prepared from protein A and human serum, IgG, or Fc gamma fragments: characterization by immunochemical analysis of ultracentrifugation fractions and studies on their interconversion”, Mol. Cell Biochem., 1985, Jan;65(2): pgs. 159-70, abstract only).
With respect to claims 1 and 8, Shang teaches in Fig. 1 shows an antibody binding to a cell antigen with Protein A-ssDNA (Ab/PrA-ssDNA) (see caption of Fig. 1). Shang further teaches protein A is PrA-ssDNA (see pg. 2, middle of para. 2) and ssDNA probes are within 20-100 nucleotides (see pg. 8, Materials under Sequences of DNA probes), which would read on a complex comprising a target conjugate pair, wherein the target conjugate pair comprises a target (i.e., cell antigen) and a conjugate associated with the target; and (b) a stabilizing component, wherein the conjugate associated with the target comprises a target-binding entity that is an antibody or antibody fragment thereof that recognizes and binds the target, wherein the target-binding entity comprises an Fc portion and is linked to an oligonucleotide (i.e., indirectly linked to Fc portion of the antibody, which is consistent with instant specification, see Figs. 3-4), wherein the oligonucleotide comprises a nucleic acid sequence of 20 to 100 nucleotides, wherein the target is an antigen that is not an antibody, wherein the stabilizing component binds to the target conjugate pair by binding to the Fc portion of the target-binding entity. The evidentiary teachings of Langone indicate that Protein A is an Fc receptor for IgG (see abstract). Based on claim 8, the conjugate may be Protein A.
Shang teaches the claimed complex, which has all the structural limitations as discussed above for the association constant (Ka) of the complex is greater than the Ka of the complex without the stabilizing component.
With respect to claim 3, Shang teaches ssDNA linked to protein A is PrA-ssDNA (see pg. 2, middle of para. 2) and ssDNA probes are within 20-100 nucleotides (see pg. 8, Materials under Sequences of DNA probes).
With respect to claim 8, Shang teaches in Fig. 1 shows an antibody binding to a cell antigen with Protein A-ssDNA (Ab/PrA-ssDNA) (see caption of Fig. 1), which reads on the binding pair is immunoglobulin/Protein A.
With respect to claim 9, Shang further teaches 5’ biotin tag for self-assembly with streptavidin-alkaline phosphatase (SAv-AP).
With respect to claim 10, Shang teaches IgG (see pg. 4, para. 3).
Claims 1, 3, 8 and 10 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Tran et al. (“A Universal DNA-Based Protein Detection System”, J. Am. Chem. Soc. 2013, vol. 135, pgs. 14008-14011, with Supporting Information pgs. S1-S10), as evidenced by Langone et al. (“Complexes prepared from protein A and human serum, IgG, or Fc gamma fragments: characterization by immunochemical analysis of ultracentrifugation fractions and studies on their interconversion”, Mol. Cell Biochem., 1985, Jan;65(2): pgs. 159-70, abstract only).
With respect to claim 1, Tran teaches in Figs. 1 and 2 a complex, comprising: (a) a target conjugate pair, wherein the target conjugate pair comprises a target and a conjugate associated with the target; and (b) a stabilizing component (i.e., protein binding moiety), wherein the conjugate associated with the target comprises a target-binding entity that is an antibody or antibody fragment thereof that recognizes and binds the target, wherein the target-binding entity comprises an Fc portion and is linked to an oligonucleotide (i.e., indirectly linked to Fc portion of the antibody, which is consistent with instant specification, see Figs. 3-4; also see Supporting Information, Supplementary Figure 2, pg. S3), wherein the oligonucleotide comprises a nucleic acid sequence of 20 to 100 nucleotides (see in the Supporting Information section of document, pg. S8, Table 1). Tran teaches EZZ protein in the universal adapter is an engineered variant of protein A (see pg. 14008, right col., last para.), which binds to the Fc region of IgG. In particular, Fig. 2 shows the attachment of the universal adapter attached at Fc region of IgG and binding to protein targets on PVDF membrane wherein the target is an antigen that is not an antibody, wherein the stabilizing component binds to the target conjugate pair by binding to the Fc portion of the target-binding entity, wherein the stabilizing component is an Fc receptor (FcR) (i.e., universal adapter is an engineered variant of protein A). The evidentiary teachings of Langone indicate that Protein A is an Fc receptor for IgG (see abstract).
Fig. 1 is reproduced below:
PNG
media_image1.png
378
398
media_image1.png
Greyscale
Tran teaches the claimed complex, which has all the structural limitations as discussed above for the association constant (Ka) of the complex is greater than the Ka of the complex without the stabilizing component.
With respect to claim 3, the universal adapter (see Fig. 1 above) shows a ssDNA oligonucleotide.
With respect to claim 8, Fig. 2 shows an antibody on the bead is bound to the protein target.
With respect to claim 10, Fig. 1 shows IgG antibody.
Claims 1, 3 and 8-11 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Lack et al. (WO2006/048781A2, published 05/11/2006).
With respect to claims 1 and 11, Lack teaches an IgE-Retargeting Function-Altering Molecules (ERFAM) construct of the formula A’-B’, wherein A’ represents a moiety that binds an IgE and B’ represents a moiety that binds an inhibitory receptor or a construct of the formula A’-X-B’ wherein A’ represents a moiety that binds an IgE, X represents a linker moiety, B’ represents a moiety that binds an inhibitory receptor (see abstract). Lack teaches in Example 2 that the IgE-binding oligonucleotide has a ssDNA oligonucleotide of 20 to 100 nucleotides and ERFAM is coupling an IgE-binding oligonucleotide with an anti-FcγR antibody (see pg. 36, lines 10-20 and Fig. 1). In particular, Lack teaches sulfhydryl-containing IgE-binding oligonucleotides and maleimide-activated anti-CD3-B (i.e., anti-FcγR antibody) (see pg. 37, lines 3-5 and lines 25-26) which would read on a complex, comprising: (a) a target conjugate pair, wherein the target conjugate pair comprises a target (i.e., allergen) and a conjugate associated with the target; and (b) a stabilizing component (i.e., anti-FcγR antibody), wherein the conjugate associated with the target comprises a target-binding entity that is an antibody or antibody fragment thereof that recognizes and binds the target, wherein the target-binding entity comprises an Fc portion and is linked to an oligonucleotide (see Fig. 1), wherein the oligonucleotide comprises a nucleic acid sequence of 20 to 100 nucleotides, wherein the target is an antigen that is not an antibody (i.e., allergen), wherein the stabilizing component binds to the target conjugate pair by binding to the Fc portion of the target-binding entity, wherein the stabilizing component is an Fc gamma receptor (FcR) (i.e., anti-FcγR antibody).
Lack teaches the claimed complex, which has all the structural limitations as discussed above for the association constant (Ka) of the complex is greater than the Ka of the complex without the stabilizing component.
With respect to claim 3, Lack teaches in Example 2 that the IgE-binding oligonucleotide has a ssDNA oligonucleotide of 20 to 100 nucleotides and ERFAM is coupling an IgE-binding oligonucleotide with an anti-FcγR antibody (see pg. 36, lines 10-20 and Fig. 1).
With respect to claim 8, Fig. 1 shows additional binding pair of ligand and receptor.
With respect to claim 9, Lack teaches using biotin and streptavidin (see pg. 9, line 2).
With respect to claim 10, Fig. 1 shows IgE antibody for allergen.
Response to Arguments
Applicant’s arguments filed 03/26/2026 have been considered but are moot because Applicant’s amendments necessitated a new ground of rejection.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NAM P NGUYEN whose telephone number is (571)270-0287. The examiner can normally be reached Monday-Friday (8-4).
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Gregory Emch can be reached at (571)272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
Prosecution Insights