DETAILED ACTION
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 .
Response to Amendment
The Amendment filed 09/16/2025 in which claims 1, 9, 11, and 15 were amended has been entered. Claims 16 - 19 were previously withdrawn. Claims 2 – 4, 12 – 14, and 16 – 19 were cancelled.
Claims 1, 5, 9 - 11, and 15 are under examination on the merits.
Drawings
(Previous objection, withdrawn) Applicant’s substitute specification submitted on 09/16/2025 have overcome the objection previously set forth in the Non-Final Office Action mailed 04/21/2025.
Nucleotide and/or Amino Acid Sequence Disclosures
(Previous objection, withdrawn) Applicant’s substitute specification and sequence listing submitted on 09/16/2025 have overcome the objection previously set forth in the Non-Final Office Action mailed 04/21/2025.
Specification
(Previous objection, withdrawn) Applicant’s substitute specification and sequence listing submitted on 02/20/2026 have overcome the objection previously set forth in the Non-Final Office Action mailed 11/20/2025.
Claim Objections
(Previous objection, withdrawn) Applicant’s correction of claim 15 submitted on 02/20/2026 have overcome the objection previously set forth in the Non-Final Office Action mailed 11/20/2025.
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.
(New ground of rejection, necessitated by amendment as to claims 15). Claim 15 is drawn to a conjugating polypeptide comprising two binding motifs wherein the first binding motif comprises “(i) the amino acid sequence set forth in SEQ ID NO:10, (ii) the amino acid sequence set forth in SEQ ID NO:26, wherein X6 is leucine, methionine, or phenylalanine, or (iii) the amino acid sequence set forth in SEQ ID NO:27, wherein X13 is leucine, methionine, or phenylalanine.”
Kang discloses the sequence of SED ID NO: 10 (reproduced below). Kang discloses the methods to resolve a high-resolution structure of SpaA isopeptide-forming pilin-related protein from Streptococcus pyogenes (Figure 1). Kang also discloses the sequence of this protein (“Gram-positive pilus structure and assembly came with the structural analysis of the major pilin Spy0128 from Streptococcus pyogenes”). Kang discloses the exact sequence of SEQ ID NO: 10, including that X in SEQ ID NO: 10 can be D (reproduced below, Query is SEQ ID NO: 10; Sbjct is Kang). Kang also discloses the SpaA protein can conjugate with other SpaA proteins, which forms a conjugated polypeptide with multiple binding domains (Figure 1, “End-to-end stacking of successive molecules, in which the C-domain of one molecule, SpaAn, packs against the N-domain of the next, SpaAn + 1”).
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Thus, Kang anticipates the claimed invention.
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.
(New ground of rejection, necessitated by amendment to claims 1 and 5) Claims 1 and 5 are rejected under 35 U.S.C. 103 as being unpatentable over Tan in view of Schmidt, Boucas, Lee, and Arsic et al (Mol Ther, 2003, hereinafter, “Arsic”).
See claims 1 as submitted on 09/16/2025.
Claim 1 has been amended to further limit the original claim with the inclusion of
Insertion of SEQ ID NO: 1 at position 588 of VP1
in an AAV2
with a titer of the AAV2 of the composition is greater than 1014
Regarding claim 1, as previously indicated, Tan teaches that SEQ ID NO: 1 is the SdyTag (Catcher Construction/ Table S1). Tan also teaches that SdyTag has the same function as SpyTag but binds to a different Catcher protein (abstract).
Schmidt teaches engineering AAV capsids using SpyTag/ SpyCatcher (Figure 1B and Exemplary compositions and methods on page 30).
Boucas teaches that the most common site used for insertion into AAV2 capsids are amino acids 587 and 588 because they are located at the second highest capsid protrusion (Abstract).
Lee teaches that the AAV2 capsid has been successfully engineered to contain nonviral motifs (page 60- insertion of nonviral parts into AAV capsid) and that an AAV2-based product was the first FDA-approved gene therapy of a hereditary disease (page 59- AAV as a gene therapy vector).
These references do not teach the limitations of AAV with a titer of greater than 1014.
However, regarding claim 1, Arsic teaches the use of AAV2 to deliver VEGF and angiopeitin-1 (Abstract). These vectors are prepared in a manner that results in high titer (Abstract). Specifically, Arsic teaches AAV2 “preparations used in this work for animal transduction had titers between 1 × 1013 and 1 × 1014 viral genome particles per ml” (Section: Material and Methods: Production, purification and characterization of rAAV vectors).
Regarding claim 5, it is noted that no amendments were introduced to claim 5 in the amendment filed on 09/16/2025. As previously explained, Lee teaches design strategies for AAV capsid engineering (Abstract). Specifically, Lee teaches that the AAV2 capsid has been successfully engineered to contain nonviral motifs (page 60- insertion of nonviral parts into AAV capsid) and that an AAV2-based product was the first FDA-approved gene therapy of a hereditary disease (page 59- AAV as a gene therapy vector). Lee also teaches that small peptides flanked by protease cleavage sequences have been inserted into the AAV2 capsid and that the protease cleavage sites enable the peptide to be cleaved off of the capsid by extracellular proteases. For example, the peptide can prevent the AAV vector from transducing cells until the peptide is cleaved off by extracellular proteases, enabling fine tuning of transduction (page 60- insertion of nonviral parts into AAV capsid).
Tan, Schmidt, , Boucas, Lee, and Arsic are considered to be analogous to the claim invention because they all teach manipulating a cell’s proteomic landscape using exogenous genes. Tan teaches that SEQ ID NO: 1 is the SdyTag (Catcher Construction/ Table S1). Tan also teaches that SdyTag has the same function as SpyTag but binds to a different Catcher protein (abstract). Schmidt teaches engineering AAV capsids using SpyTag/ SpyCatcher (Figure 1B and Exemplary compositions and methods on page 30). Boucas teaches that the most common site used for insertion into AAV2 capsids are amino acids 587 and 588 because they are located at the second highest capsid protrusion (Abstract). Lee teaches that small peptides flanked by protease cleavage sequences have been inserted into the AAV2 capsid and that the protease cleavage sites enable the peptide to be cleaved off of the capsid by extracellular proteases. (page 60- insertion of nonviral parts into AAV capsid). Arsic teaches AAV2 “preparations used in this work for animal transduction had titers between 1 × 1013 and 1 × 1014 viral genome particles per ml” (Section: Material and Methods: Production, purification and characterization of rAAV vectors).
It would have been prima facie obvious to a person with ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of Schmidt, Tan, Boucas, Lee, and Arsic to insert SEQ ID NO: 1 into position 588 of VP1 of an AAV2. One would have been motivated to do so for the advantage of increased display of the inserted peptide due to high capsid protrusion and because of increased receptor binding and transduction efficiency. As taught by Boucas and Lee AAV2 are common serotypes used in biotechnological research. One would have been motivated to do so for the advantage of using a readily-engineered AAV2 subtype that has previously received FDA-approval and to enable further modification of the engineered capsid by cellular proteases. Furthermore, as taught by Arsic, one of ordinary skill in the art would be motivated to increase viral titers to 1014 because achieving high titers increases the number of cells infected. There would have been a reasonable expectation of success given the underlying materials and methods are widely known, successfully demonstrated, and commonly used as evidenced by the prior art.
Thus, the invention as a whole was prima facie obvious to one of ordinary skill in the art before the effective filing date of the invention, especially in the absence of evidence to the contrary.
(New ground of rejection, necessitated by amendment as to claims 9 - 11) Claim 9 – 11 are rejected under 35 U.S.C. 103 as being unpatentable over Tan and Schmidt in view of Kang et al (PNAS, 2009, hereinafter, “Kang”).
As discussed above and previously, SEQ ID NO: 1 is the SdyTag taught by Tan (Catcher Construction/ Table S1). Tan also teaches that SdyTag has the same function as SpyTag but binds to a different Catcher protein (abstract). Schmidt teaches engineering AAV capsids using SpyTag/ SpyCatcher (Figure 1B and Exemplary compositions and methods on page 30) and multiplexed gene delivery using multiple AAVs with engineered capsids (pages 30-31, exemplary compositions and methods).
These references fail to teach the newly added limitation of an a second AAV comprising the sequence set forth in SEQ ID NO: 10.
However, Kang teaches the methods to resolve a high-resolution structure of SpaA isopeptide-forming pilin-related protein from Streptococcus pyogenes (Figure 1). Kang also teaches the sequence of this protein (“Gram-positive pilus structure and assembly came with the structural analysis of the major pilin Spy0128 from Streptococcus pyogenes”). Regarding amended claim 9, Kang teaches the exact sequence of SEQ ID NO: 10, including that X in SEQ ID NO: 10 can be D (reproduced below, Query is SEQ ID NO: 10; Sbjct is Kang).
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Regarding claims 10 and 11, Tan teaches that SdyTag (i.e. SEQ ID NO: 1) binding to SdyCatcher creates a covalent ligation (Table 1). Schmidt teaches that covalent attachments to AAV capsids allow for complex mixtures of viral particles with different transgenes to target the same cell (page 4 lines 1-9).
Tan teaches that SdyTag (i.e. SEQ ID NO: 1) binding to SdyCatcher creates a covalent ligation (Table 1). Schmidt teaches that covalent attachments to AAV capsids allow for complex mixtures of viral particles with different transgenes to target the same cell (page 4 lines 1-9).
It would have been prima facie obvious to a person with ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of Tan, Schmidt, and Kang to generate a composition of two distinct AAVs with one comprising a capsid polypeptide comprising SEQ ID NO: 1 and the other SEQ ID NO:10. One would have been motivated to do so for the advantage of delivering multiple genes to the target cell, as taught by Schmidt, and for the advantage of tagging the viral capsid with a protein that is highly specific to a certain binding partner, as taught by Tan. There would have been a reasonable expectation of success given the underlying materials and methods are widely known, successfully demonstrated, and commonly used as evidenced by the prior art.
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.
(Previous rejection, maintained as necessitated by amendment as to claims 1, 5, and 9 - 11 modified in view of the amendments to claims 1, 5, and 9 - 11)).
Claims 1, 5, and 9 – 11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 and 22 of copending Application No. 18277933 as evidenced by Buning.
Claim 1 of the instant application and claims 1 and 3 of copending application ‘933 are drawn to a SdyTag inserted into the capsid polypeptide of AAV. However, claim 1 of copending application ‘933 specifies that the AAV comprises VP1, VP2, and VP3 polypeptides and that the heterologous amino acid sequence (i.e. SdyTag) is inserted into VP3. Buning evidences that VP1, VP2, and VP3 are the AAV capsid proteins (introduction paragraph 3). Buning also evidences that VP3 is a common region shared amongst all three AAV capsid proteins (introduction paragraph 4 and Figure 1). Thus, an AAV comprising VP1, VP2, and VP3 polypeptides (i.e. copending application ‘933 claim 1) is not distinct from an AAV comprising a capsid polypeptide (i.e. instant claim 1). Finally, claim 3 of copending application ‘933 is drawn to the heterologous amino acid sequence inserted into VP3 being SEQ ID NO: 1. SEQ ID NO: 1 of the instant application (as required by claim 1) is identical to SEQ ID NO: 1 of copending application ‘933 (see alignment below). Thus, claim 1 of the instant application is not patentably distinct from claims 1 and 3 of copending application ‘933.
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Amendments to claim 1 include the further limitation of SEQ ID NO: 1 being inserted at position 588, the AAV is an AAV2, and with a titer greater than 1014.
The amendments still do not address the overlap between the instant application and ‘933:
The AAV being AAV2 (claim 2 of instant application and claim 2 of copending application ‘933)
The heterologous amino acid sequence inserted into the AAV capsid comprising SEQ ID NO: 1 (claim 3 of instant application and claim 3 of copending application ‘933)
The SEQ ID NO: 1 polypeptide being inserted within 3 amino acid residues of position 588 of SEQ ID NO: 2 (claim 4 of instant application and claim 4 of copending application ‘933; 100% identity between SEQ ID NO: 2 of both applications- see alignment below)
At position 588 is still within three amino acid residues of position 588
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The AAV2 titer being greater than 1014 (claim 7 of ‘933 recites an AAV titer greater than 1011)
Regarding claim 5 the AAV capsid polypeptide comprising a protease cleavage site (claim 5 of instant application and claim 5 of copending application ‘933).
Regarding, claims 9 – 11 of the instant application and claim 22 of copending application ‘933 are drawn to a composition of two genetically distinct AAVs wherein the first AAV comprises SEQ ID NO: 1 inserted into the capsid polypeptide. However, claim 22 of copending application ‘933 specifies that the AAV comprises VP1, VP2, and VP3 polypeptides and that the heterologous amino acid sequence (i.e. SdyTag) is inserted into VP3. For the same reasons detailed above, Buning evidences that insertion into VP1, VP2, and VP3 is not patentably distinct from insertion into an AAV capsid polypeptide. Furthermore, SEQ ID NO: 10 of the instant application and SEQ ID NO: 60 of ‘933 are 100% identical (reproduced below, Sequence 1 is SEQ ID NO: 10 of the instant application, Sequence2 is SED IS NO:60 of ‘933). Regarding claims 10 and 11 ‘933 also includes a second AAV if covalently attached to the first [¶0014]
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Thus, claims 9 – 11 of the instant application is not patentably distinct from claim 22 of copending application ‘933.
Response to Arguments
Applicant's arguments filed 09/16/2025 have been fully considered but they are not persuasive.
Applicant argues on page 7 of Remarks: Applicant states that the amendments to claim 15 overcome the previous 102(a)(1) rejections. On page 9, applicant states that the amendments to claim 15 overcome the previous rejections. Applicant state “claim 15 was amended herein to recite that the first binding motif comprises (i) the amino acid sequence set forth in SEQ ID NO:10, (ii) the amino acid sequence set forth in SEQ ID NO:26, wherein X6 is leucine, methionine, or phenylalanine, or (iii) the amino acid sequence set forth in SEQ ID NO:27, wherein X13 is leucine, methionine, or phenylalanine. At no point do the combinations of cited references teach or suggest a conjugating polypeptide comprising such a first binding motif. In fact, none of the cited references discloses a polypeptide comprising (i) the amino acid sequence set forth in SEQ ID NO: 10, (ii) the amino acid sequence set forth in SEQ ID NO:26, wherein X6 is leucine, methionine, or phenylalanine, or (iii) the amino acid sequence set forth in SEQ ID NO:27, wherein X13 is leucine, methionine, or phenylalanine. Thus, presently presented claim 15 is patentable over the combinations of cited references.”
In response: This is not persuasive because as stated above and previously, regarding claim 15 of the amended set of claims, Kang teaches the exact sequence of SEQ ID NO: 10, including that X in SEQ ID NO: 10 can be D (reproduced below, Query is SEQ ID NO: 10; Sbjct is Kang). Kang also teaches that this sequence is naturally occurring and the proteins comprised of this sequence can stack together forming conjugated polypeptides with multiple binding sites.
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Applicant argues on page 8 of Remarks: That the amendments to claim 1 overcome the previous rejections. Applicant state “independent claim 1 was amended herein to recite a composition comprising an AAV, to recite that the capsid polypeptide comprises an amino acid segment comprising the amino acid sequence set forth in SEQ ID NO:1 at an amino acid position corresponding to position 588, and to recite that the AAV is an AAV2. Independent claim 1 also was amended herein to recite that the titer of the AAV2 of the composition is greater than 1014. At no point do the combinations of cited references teach or suggest such a composition. In fact, none of the cited references discloses such a high titer composition of AAV2 having an amino acid segment at position 588, let alone an amino acid sequence set forth in SEQ ID NO:1 at position 588. Thus, presently presented claims 1 and 5 are patentable over the combinations of cited references.” Furthermore, the applicant argues that AAV2 containing SEQ ID NO: 1 resulted in unexpected high titers (1014).
In response: This is not persuasive because as stated above and previously, regarding claim 1 – 4 of the previous set of claims, Tan, Schmidt, Boucas, and Lee teach the limitations of claim 1, as amended. Arsic teaches that AAV2 vectors are used in titers of 1 × 1013 and 1 × 1014 in practice (Section: Production, purification and characterization of rAAV vectors). The change in the AAV capsid that leads to a 1014 titer is not an unexpectedly high titer. Titers of 1014 are routine and seen as a bench mark for quality as taught by Arsic. Additionally, Arsic teaches that by varying methods of production and purification, AAV titers can be adjusted to be higher or lower depending on the need.
Therefore, it would have been obvious to one of ordinary skill in the art to not only place SEQ IN NO: 1 at position 588 of VP1 of AAV2 but to also prepare this vector at a titer of 1014 because doing so allows enough viral particles to be effective at increased cellular invasion and downstream activity.
Furthermore, Arsic teaches that a high titer can be achieved by production means and is not reliant on the capsid makeup of the AAV2. Therefore, claim 1 is rejected after consideration of the new amendments.
Applicant argues on page 9 of Remarks: That the amendments to claim 9 - 11 overcome the previous rejections. Applicant argues that “independent claim 1 was amended herein to recite a composition comprising an AAV, to recite that the capsid polypeptide comprises an amino acid segment comprising the amino acid sequence set forth in SEQ ID NO:1 at an amino acid position corresponding to position 588, and to recite that the AAV is an AAV2. Independent claim 1 also was amended herein to recite that the titer of the AAV2 of the composition is greater than 1014. At no point do the combinations of cited references teach or suggest such a composition. In fact, none of the cited references discloses such a high titer composition of AAV2 having an amino acid segment at position 588, let alone an amino acid sequence set forth in SEQ ID NO:1 at position 588. Thus, presently presented claims 1 and 5 are patentable over the combinations of cited references.” Furthermore, the applicant argues that AAV2 containing SEQ ID NO: 1 resulted in unexpected high titers (1014).
In response: This is not persuasive because as stated above and previously, regarding claim 9 - 11 of the previous set of claims, Tan and Schmidt teach the limitations of claims 9.
These references fail to teach the newly added limitation of an the second AAV comprising the sequence set forth in SEQ ID NO: 10.
However, Kang teaches the newly added limitation of the exact sequence of SEQ ID NO: 10, including that X in SEQ ID NO: 10 can be D (reproduced below, Query is SEQ ID NO: 10; Sbjct is Kang).
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It would have been prima facie obvious to a person with ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of Tan and Schmidt to generate a composition of two distinct AAVs with one comprising a capsid polypeptide comprising SEQ ID NO: 10. One would have been motivated to do so for the advantage of delivering multiple genes to the target cell, as taught by Schmidt , and for the advantage of tagging the viral capsid with a protein that is highly specific to a certain binding partner, as taught by Tan . There would have been a reasonable expectation of success given the underlying materials and methods are widely known, successfully demonstrated, and commonly used as evidenced by the prior art.
Applicant argues on page 9 of Remarks: Applicant has cancelled claims 2 – 4 and 12 – 14. Applicant also states the amendments made to claims 1, 9, 10, and 11, as discussed above, overcome the non-statutory obviousness-type double patenting and are patentably distinct from the claims of US Patent Application no 18277933.
In response: This is not persuasive because as stated above and previously, regarding claims 1, 5, and 9 - 11 of the amended set of claims all the limitations are taught in ‘933. The applicant amended claim 1 to include the titer of greater than 1014. However, claim 7 of ‘933 recites an AAV titer greater than 1011. Additionally, as discussed above, Arsic teaches the routine use of AAV2 at titers of 1 × 1013 and 1 × 1014. Additionally, Arsic teaches that by varying methods of production and purification, AAV titers can be adjusted to be higher or lower depending on the need. Therefore, the change in the AAV capsid that leads to a 1014 titer is not an unexpectedly high titer.
Conclusion
NO CLAIMS ARE ALLOWED
Prior art not discussed but pertinent to the application:
Wright et al (Molecular Therapy, 2013)
Clement et al (Mol Ther Methods Clin Dev, 2016)
Bordey et al (US12274756B2)
Gray et al (US10532110B2).
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Danyal H Alam whose telephone number is (571)272-1102. The examiner can normally be reached M - F 9am - 5pm.
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/DANYAL HASSAN ALAM/Examiner, Art Unit 1672
/THOMAS J. VISONE/Supervisory Patent Examiner, Art Unit 1672
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