DETAILED ACTION
This Office action details a first action on the merits for the above referenced application No. Claims 1-16 are pending in this application.
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 .
Priority
This application is a 35 USC 371 National Stage filing of international application No. PCT/JP2022/032709 filed on 31 Aug. 2022 and claims benefit under 35 USC 119(a)-(d) to foreign application No. JP 2021-141625 filed on 31 Aug. 2021.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 29 May 2024 has been considered by the examiner.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency - This application fails to comply with the requirements of 37 CFR 1.821 - 1.825. This application contains a “Sequence Listing” as a PDF file (37 CFR 1.821(c)(2)) or as physical sheets of paper (37 CFR 1.821(c)(3)). A copy of the "Sequence Listing" in computer readable form (CRF) has been submitted; however, the content of the CRF does not comply with one or more of the requirements of 37 CFR 1.822 through 1.824, as indicated in the "Error Report" that indicates the "Sequence Listing" could not be accepted. Refer to attachment or document "Computer Readable Form (CRF) for Sequence Listing – Defective" dated 27 Jun. 2024.
Required response – Applicant must provide:
A replacement "Sequence Listing" part of the disclosure, as described above in item 1); together with
An amendment specifically directing its entry into the application in accordance with 37 CFR 1.825(b)(2);
A statement that the "Sequence Listing" includes no new matter as required by 37 CFR 1.825(b)(5); and
A statement that indicates support for the amendment in the application, as filed, as required by 37 CFR 1.825(b)(4).
If the replacement "Sequence Listing" part of the disclosure is submitted according to item 1) a) or b) above, Applicant must also provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required incorporation-by-reference paragraph, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter and
An amendment to the specification to remove the “Sequence Listing previously submitted as a PDF file (37 CFR 1.821(c)(2)) or as physical sheets of paper (37 CFR 1.821(c)(3))
If the replacement "Sequence Listing" part of the disclosure is submitted according to item 1) c) or d) above, Applicant must also provide:
A CRF in accordance with 1.821(e)(1) or 1.821(e)(2) as required by 37 CFR 1.825(b)(6)(ii); and
Statement according to item 2) a) or b) above.
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 2, 4, and 12-13 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.
In claim 2, the ellipsis at “…(i)” is indefinite and not understood at least since an ellipsis can connote omitted text.
In claim 4, the recitation of “(wherein Xaa2 is a lysine residue)” is indefinite because it is not clear if the recitation is an example or required limitation.
In claims 12 and 13, the recitations of “which is used in” is indefinite because it indicates a method step in a composition claim. MPEP 2173.05(p).
Claim Rejections - 35 USC § 102
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.
Claim(s) 1, 6-7, 9-11, and 13-15 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Vivier et al. (J. Nucl. Med.; published 7 Feb. 2019; see IDS filed 29 May 2024).
Regarding claims 1, 6-7, and 14-15, Vivier et al. disclose 89Zr-DFO-sstrastuzumab-EndoS
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(Fig. 5).. This was site specifically modified in the Fc region of the antibody by click reaction of azide bearing sugars with DBCO-DFO and a degree of labeling of 1.3 DFO/monoclonal antibody (pg. 1177). Regarding claim 9, sstrastuzumabEndoS is an IgG antibody (pg. 1176). Regarding claim 10, sstrastuzumabEndoS is deglycosylated by cleaving a GlcNAc (Figs 1 and 2). Regarding claims 11 and 13, 89Zr-DFO-sstrastuzumab-EndoS was injected in NSG bearing subcutaneous BT474 xenografts (Pharmaceutical composition used in cancer diagnosis; Fig. 6).
Claim Rejections - 35 USC § 103
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 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.
Claim(s) 1-16 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vivier et al. (J. Nucl. Med.; published 7 Feb. 2019; see IDS filed on 29 May 2024), in view of Izawa et al. (CA 3158344 A1; published 21 Apr. 2021; see IDS filed 29 May 2024).
Vivier et al. teach as discussed above. Vivier et al. disclose 89Zr-DFO-nsstrastuzumab-PNGaseF
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. This was achieved by via random or non-site specific reaction of an isothiocyanate bearing variant of DFO with lysines of the antibody (see. 1176).
Vivier et al. teach the impact of FcγRI binding of immune PET. Vivier et al. synthesized a series of deferrioxamine-bearing immunoconjugates with differing glycosylation states and interrogated their FcyRI binding. A strong correlation was observed between the impaired in vitro FcγRI binding of deglycosylated immunoconjugates and significant decrease in the in vivo off-target uptake of corresponding 89Zr-labeled radioimmunoconjugates. Deglycosylation of antibodies represents a facile strategy for improving the quality of immune-PET in animals as well as certain patient populations (see abstract). 89Zr-DFO-nsstrastuzumab-PNGaseF produced high tumor-to-background activity concentration ratios and excellent immune-PET imaging despite the presence of fully reconstituted human immune system and the endogenous IgGs in huNSG mice (pg. 1180).
Vivier et al. do not teach a linker comprising an antibody modification composed of not less than 13 and not more that 17 amino acid residues represented by formula (i) (Xa)-Xaa1-(Xb)-Xaa2-(Xc)-Xaa3-(Xd)…(i) optionally wherein Xaa2 is a lysine residue and optionally wherein the antibody modification peptide comprises an antibody modification peptide consisting of the amino acid sequence shown in SEQ ID NO 2. Vivier et al. do not further teach a chelating agent derived from a compound represented by formula (A). Vivier et al. do not teach a conjugate of a chelating agent chelated with a radionuclide and a deglycosylated antibody wherein the radionuclide is 225Ac. Vivier et al. do not disclose a pharmaceutical composition which is used in an RI internal therapy for cancer. Vivier et al. do not disclose a method of production wherein the conjugation step is performed by click reaction of an antibody with a radioactive metal complex of DOTAGA-DBCO.
Izawa et al. teach a method for producing radioactive metal labeled antibody (see title). Izawa et al. teach a method for producing a radioactive metal labeled antibody comprising a step of conduction a click reaction of a radioactive metal complex and an antibody site specifically modified with a peptide to produce a radioactive metal labeled antibody wherein the click reaction is performed (see pg. 2). A specific site of the antibody is specifically modified by the peptide, preferably the Fc region of the antibody is specifically modified and preferably the lysine residue in the Fc region of the antibody is modified site-specifically (pg. 33). Preferably the amino acid sequence consisting of 13 to 17 amino acid residues represented by formula (i): (Xa)-Xaa1-(Xb)-Xaa2-(Xc)-Xaa3-(Xd)… (pgs. 33-34). Izawa et al. teach the amino acid sequence GPDCAYH(Xaa2)GELVWCTFH wherein Xaa2 is a lysine (pg. 36). A crosslinking reaction can be caused between the amino acids residue of Xaa2 in the peptide and an antibody. When human IgG (e.g. trastuzumab) is used as the antibody, site specific binding occurs via a crosslinked structure between the amino acid residue of Xaa2 and at least one of the Lys246 residue and the Lys246 residue according the to the Eu numbering in trastuzumab (pg. 38). When the radioactive metal labeled antibody is used for the treatment of a disease and 225Ac is used as a radioactive metal (pg. 41). Izawa et al. teach DOTAGA-DBCO
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(pg. 55). (DO3A-DBCO reads on a compound of formula (A) wherein R11=R13=R14=(CH2)pCOOH, p=1; R15=H; and R12=substituent group for conjugating an antibody.)
Izawa et al. teach a peptide containing 17 amino acid residues represented by formula (P3)
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(pg. 47). (P3 reads on instant SEQ ID NO: 2 and peptide of formula (i) wherein a=3, X=G-P-D; Xaa1=C; b=3, X=A-Y-H; Xaa2=Lys; c=5, X=G-E-L-V-W; Xaa3=C; d=3, X=T-F-H satisfying 3+3+5+3=14 and Xaa1 and Xaa3 are C and bonded via a disulfide.)
The peptide modified antibody has an Fc region of the antibody site specifically modified by the above mentioned peptide (pg. 48). Izawa et al. teach 225Ac labeling (pgs. 48-49). Izawa et al. teach DO3A-DBCO modified trastuzumab (example 3, table 1) It would have been obvious to a person of ordinary skill in the art before the effective filing date to modify the trastuzumab-PNGaseF in Vivier et al. by site specifically modifying a Lys in the Fc region of the antibody with a linker peptide comprising an azide such as the P3 taught by Izawa et al. and then optionally react that linker peptide antibody conjugate with a radioactive metal complex of DO3A-DBCO by click reaction as taught by Vivier et al. and Izawa et al. because it would have been expected to advantageously enable controlled and site specific attachment of a linker moiety having a reactive azide to a completely deglycosylated antibody and a one-step click reaction of a radioactive metal complex under mild conditions. It would have been obvious to a person of ordinary skill in the art before the effective filing date to further modify Vivier et al. so that the radionuclide is 225Ac such that radiopharmaceutical is capable of use in RI therapy for cancer as taught by Vivier et al. and Izawa et al. because the 225Ac and RI therapy would have been expected to advantageously enable alpha therapy of cancers including HER positive breast cancers.
Claim(s) 1-16 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vivier et al. (J. Nucl. Med.; published 7 Feb. 2019; see IDS filed on 29 May 2024), in view of Kishimoto et al. (Bioconjugate Chem.; published 2019; see attached 892) and Dudkin et al. (WO 2019/125982 A1; published 27 Jun. 2019; see attached 892).
Vivier et al. teach as discussed above.
Vivier et al. do not teach a linker comprising an antibody modification composed of not less than 13 and not more that 17 amino acid residues represented by formula (i) (Xa)-Xaa1-(Xb)-Xaa2-(Xc)-Xaa3-(Xd)…(i) optionally wherein Xaa2 is a lysine residue and optionally wherein the antibody modification peptide comprises an antibody modification peptide consisting of the amino acid sequence shown in SEQ ID NO 2. Vivier et al. do not further teach a chelating agent derived from a compound represented by formula (A). Vivier et al. do not disclose a method of production wherein the conjugation step is performed by click reaction of an antibody with a radioactive metal complex of DOTAGA-DBCO. Vivier et al. do not teach a conjugate of a chelating agent chelated with a radionuclide and a deglycosylated antibody wherein the radionuclide is 225Ac. Vivier et al. do not disclose a pharmaceutical composition which is used in an RI internal therapy for cancer.
Kishimoto et al. teach site-specific chemical conjugation of antibodies by using affinity peptide for the development of therapeutic antibody format (see title). The method enable a rapid modification of a specific residue (Lys248 on Fc) in a one step reaction under mild conditions to form a stable amide bond between the peptide and Fc. It is a suitable conjugate form that can be further conjugated into highly functional antibody therapeutics (see abstract). Kishimoto et al. teach identifying GPDCAYHRGELVWCTFH consisting of 17 amino acids which is intramolecularly crosslinked with a disulfide bond (pg. 699). Kishimoto et al. teach NHS-IgG-BP-biotin
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. (Fig. 2). Kishimoto et al. teach trastuzumab and NHS-IgG-DM1 (pg. 700). The CCAP reaction developed for the rapid synthesis of peptide/IgG conjugates proceeded rapidly under mild conditions and enable high yield of the product without the use of excess reagents (pg. 701).
Dudkin et al. teach radiolabeling polypetides using DOTAGA-DBCO (see title, abstract). Dudkin et al. teach the labeling scheme
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(see abstract, Fig. 1). Dudkin et al. teach that 225Ac radioimmunoconjugates are of particular interest (pg. 2). Dudkin et al. teach a method of labeling a polypeptide comprising contacting the modified polypeptide with a radiocomplex under a condition that allow for a first click reaction partner to react with a second reaction partner to thereby label the polypeptide (pg. 10_
It would have been obvious to a person of ordinary skill in the art before the effective filing date to modify the trastuzumab-PNGaseF in Vivier et al. by site specifically modifying a Lys in the Fc region of the antibody with a linker peptide comprising an azide such as the IgG-BP-NHS in Kishimoto et al. where an azide replaces the amine conjugated biotin and then optionally react that linker peptide antibody conjugate with a radioactive metal complex of DO3A-DBCO by click reaction as taught by Vivier et al., Kishimoto and Dudkin et al. because it would have been expected to advantageously enable controlled and site specific attachment of a linker moiety having a reactive azide to a completely deglycosylated antibody and a one-step click reaction of a radioactive metal complex under mild conditions.
It would have been obvious to a person of ordinary skill in the art before the effective filing date to further modify Vivier et al. so that the radionuclide is 225Ac such that radiopharmaceutical is capable of use in RI therapy for cancer as taught by Vivier et al. and Dudkin al. because the 225Ac and RI therapy would have been expected to advantageously enable alpha therapy of cancers including HER positive breast cancers.
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 1-16 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 11-12, and 16-28 of copending Application No. 17/769,657, in view of Vivier et al. (J. Nucl. Med.; published 7 Feb. 2019; see attached 892), and Dudkin et al. (WO 2019/125982 A1; published 27 Jun. 2019; see attached 892). This is a provisional nonstatutory double patenting rejection.
Claims 11-12, and 16-28 of copending Application No. 17/769,657 claim a radioactive metal conjugate metal labeled antibody site specifically modified at the Fc region via a peptide and a radioactive metal complex wherein the radioactive metal complex is directly or indirectly linked to the peptide wherein the peptide comprises an amino acid sequence of formula (I) optionally GPDCAYHXaaGELVWCTFH wherein Xaa is a lysine or P3 optionally wherein the radioactive metal complex is derived from DOTAGA such as DOTAGA-DBCO and optionally wherein the antibody is an IgG such as trastuzumab and optionally wherein a triazole skeleton is formed by click reaction between the alkyne of L1-4 and azide of P3.
Claims 11-12, and 16-28 of copending Application No. 17/769,657 do not claim a deglycosylated antibody or pharmaceutical composition thereof optionally wherein the dyglycosylation is performed by cleaving an N-type sugar chain or a radionuclide that is 225Ac or a radiopharmaceutical that is used in RI internal therapy for cancer or a method for producing the conjugate according to claim 1 comprising a conjugating step of producing a conjugate of a chelating agent chelated with a radionuclide and a deglycolylated antibody by click reaction and optionally by click reaction with a radioactive metal complex of DOTAGA-DBCO.
Vivier et al. teach as discussed above.
Dudkin et al. teach as discussed above.
It would have been obvious to a person of ordinary skill in the art before the effective filing date to modify claims 11-12, and 16-28 of copending Application No. 17/769,657 so the antibody is a deglycosulated human IgG antibody formed by cleaving and N-type sugar chain and optionally forms a pharmaceutical composition as taught by Vivier et al. because the deglycosylated antibody would have been expected to advantageously enable reductions in off-target uptake accompanied by a concomitant increase in tumoral activity concentrations ultimately yielding improved tumor to healthy organ contrast ratios and better PET images. It would have been obvious to a person of ordinary skill in the art before the effective filing date to further modify claims 11-12, and 16-28 of copending Application No. 17/769,657 so that the radionuclide is 225Ac such that radiopharmaceutical is capable of use in RI therapy for cancer as taught by Vivier et al. and Dudkin et al. because the 225Ac and RI therapy would have been expected to advantageously enable alpha therapy of cancers including HER positive breast cancers. It would have been obvious to a person of ordinary skill in the art before the effective filing date to further modify claims 11-12, and 16-28 of copending Application No. 17/769,657 to arrive at a method for producing a conjugate wherein the conjugation step is performed by a click reaction of the antibody with a radioactive metal complex of DOTAGA-DBCO as taught by claims 11-12, and 16-28 of copending Application No. 17/769,657, Vivier et al., and Dudkin et al. because it would have been expected to advantageously enable a conjugated radiometal complex formed in one step by click reaction.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SEAN R DONOHUE whose telephone number is (571)270-7441. The examiner can normally be reached on Monday - Friday, 8:00 - 5:00 EST.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Michael Hartley can be reached on (571)272-0616. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Michael G. Hartley/Supervisory Patent Examiner, Art Unit 1618
/SEAN R. DONOHUE/
Examiner, Art Unit 1618
Prosecution Insights