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 .
Status of Application
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 09/01/2026 has been entered.
Claims 1-12 are pending.
Claim 1 is amended.
Claims 13-14 are new.
Claims 1-14 are pending and under examination on its merits in this application.
Priority
The instant application is a continuation application of a national stage entry of PCT/US2022/037601 filed on 07/19/2022, and has a provisional status from the application # 63/223,339 filed on 07/19/2021.
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.
Claims 8, 9 and 14 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 8 depends from claim 3 ("wherein the compound comprises an electrophile moiety"), not from claim 1 directly, and recites "wherein the vinyl sulfone is configured as an isostere of a mixed phosphoric carboxylic anhydride." Claim 3's "electrophile moiety" is broad enough to encompass both species of claim 1's alternative — a vinyl sulfone or a sulfonyl acrylamide are each an electrophile moiety. For the sulfonyl acrylamide embodiments captured by claims 1 and 3, "the vinyl sulfone" in claim 8 has no antecedent basis in the claim, rendering the claim indefinite as to those embodiments. Clarification is required — e.g., amending claim 8 to recite "wherein the electrophile moiety is a vinyl sulfone, wherein the vinyl sulfone is configured as..."
Claim 9 is rejected as indefinite on two independent grounds: 1) Claim 9 depends from claim 7 ("wherein the compound is a dipeptide"), not claim 1, and recites "wherein the compound is configured to match a binding pocket of the enzyme target." The phrase "configured to match a binding pocket" is a functional, result-oriented limitation with no corresponding structural or quantitative standard given anywhere in the claim to establish what degree or type of structural complementarity satisfies "match." It is unclear whether any measurable binding affinity suffices, or whether some more specific steric/electronic correspondence is required, and the claim gives no way to determine the boundary between compounds that are and are not "configured to match." See MPEP § 2173.05(g). 2) Independently, "the binding pocket of the enzyme target" lacks clear antecedent basis, since neither claim 1 nor claim 7 introduces or otherwise characterizes a "binding pocket" of the ASADH enzyme target.
Claim 14 introduces "a fungal ASADH" and "a bacterial ASADH ortholog," and it is unclear whether "a fungal ASADH" is intended to refer back to and further limit the ASADH of claim 1, or whether it introduces an additional, distinct enzyme not otherwise operated on by the method steps of claim 1. Clarification is required, e.g., "wherein the ASADH is a fungal ASADH."
Appropriate corrections to all of the above is required.
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.
Claims 1-14 are rejected under 35 U.S.C. 103 as being unpatentable over A Fragment Library Screening Approach to Identify Selective Inhibitors against an Essential Fungal Enzyme (hereinafter the reference is referred as Dahal) in view of
Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases (hereinafter the reference is referred as Powers), and A Diels-Alder approach to biaryls (DAB): synthesis of the western portion of TMC-95 (hereinafter the reference is referred as Ashburn) and further in view of Viola et al. (US 10,449,168 B2 hereinafter “Viola ‘168”).
Regarding claim 1 (amended): Dahal teaches a method comprising: (i) providing a compound having selective inactivation activity against aspartate β-semialdehyde dehydrogenase (ASADH), an essential microbial enzyme target (Dahal, abstract; pp. 521, 524–525); (ii) providing ASADH as the enzyme target (Dahal, pp. 521–522); and (iii) a basis for inactivating that enzyme target, in that Dahal explicitly acknowledges that ASADH’s active site contains a cysteine nucleophile that can be covalently modified to lead to an inactivated enzyme (Dahal, p. 524, right col. ¶ 2–3). Dahal does not teach that the compound is a vinyl sulfone or sulfonyl acrylamide, nor irreversible covalent inactivation.
Powers teaches that vinyl sulfones and related sulfonyl-containing Michael acceptors function as irreversible covalent warheads for enzymes bearing an active-site cysteine nucleophile (Powers, pp. 4639, 4645 right col. ¶ 2; pp. 4683, 4687, 4740). As to the sulfonyl acrylamide alternative, Powers's disclosure of acrylamide-class Michael acceptors together with its disclosure of sulfonyl-containing warheads (Powers, p. 4645, right col. ¶ 2; Table 2.1) renders a sulfonyl acrylamide — a straightforward structural hybrid of these two known warhead classes — an obvious design choice for covalently targeting a cysteine nucleophile.
It would have been obvious to apply the vinyl sulfone or sulfonyl acrylamide warhead chemistry of Powers to the ASADH target of Dahal, with a reasonable expectation of success, motivated by Dahal's own SAR discussion that exploiting the full active-site environment could yield more potent inhibitors (Dahal, p. 525, left col. ¶ 2–3), and by Dahal's disclosure of covalent cysteine modification as a mechanistic possibility. KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 416 (2007).
Regarding claims 2 (claim 2 original; claim 3 amended): Claim 2 recites the compound comprises a sulfonyl group. Powers teaches vinyl sulfones and sulfonylating compounds comprising sulfonyl group–containing warheads as irreversible enzyme inactivators (Powers, p. 4645, right col. ¶ 2; Table 2.1; p. 4683; p. 4736, right col. ¶ Other Sulfonylating Compounds).
Claim 3 recites the compound comprises an electrophile moiety. Powers teaches a broad class of electrophilic warheads including vinyl sulfones, vinyl sulfonamides, and other Michael acceptors as irreversible covalent inactivators of cysteine-nucleophile enzymes (Powers, p. 4645, right col. ¶ 2). The “electrophile moiety” limitation of claim 3, is fully encompassed by Powers’ teaching of electrophilic warheads.
Regarding claims 4 and 5: Dahal teaches compounds bearing nitro and carboxyl groups in various combinations and positions, screened against ASADH for inhibitory activity (Dahal, p. 525, right col. ¶ 1, last 3 lines; abstract). The antifungal and antibacterial properties recited in claim 5 are taught by Dahal, which discloses selective ASADH inhibitors active against pathogenic fungal and bacterial species (Dahal, p. 521, left col. ¶ 1; pp. 524–525).
Regarding claim 6: Claim 6 recites that the compound bonds with a cysteine residue nucleophile. Dahal explicitly teaches that the ASADH active site contains a cysteine nucleophile susceptible to covalent modification (Dahal, p. 524, right col. ¶ 2–3). Powers teaches covalent bond formation between vinyl sulfone warheads and active-site cysteine nucleophiles (Powers, pp. 4639, 4645, 4683).
Claim 7 recites that the compound is a dipeptide. Powers teaches peptidyl and peptidomimetic vinyl sulfone inhibitors, including dipeptide-based scaffolds, as established irreversible inactivators of cysteine-nucleophile enzymes (Powers, pp. 4683–4687, Figures 67–68). Ashburn further teaches dipeptide-containing biaryl framework synthesis applied to enzyme inhibitor scaffold design (Ashburn, pp. 856–865). It would have been obvious to incorporate a dipeptide structural element into the vinyl sulfone/sulfonyl acrylamide compounds of the Dahal-Powers combination, consistent with Powers's established peptidyl vinyl sulfone design approach.
Regarding claim 8, for purposes of this rejection, claim 8 is treated as requiring a vinyl sulfone wherein the sulfonyl group is configured as an isostere of a mixed phosphoric carboxylic anhydride (see § 112(b) rejection above). Dahal establishes that ASADH's natural substrate is aspartyl phosphate, containing a phosphoryl group, with structural complementarity to this phosphoryl-containing intermediate being important to inhibitor potency (Dahal, pp. 521–525). Powers discloses that sulfonyl groups function as established bioisosteres of phosphoryl groups in covalent inhibitor design (Powers, pp. 4683, 4687). It would have been obvious to design a vinyl sulfone in which the sulfonyl group serves as an isostere of the phosphoryl-containing mixed phosphoric carboxylic anhydride intermediate of the ASADH catalytic cycle.
Regarding claim 9, Claim 9 depends from claim 7 and additionally recites that the dipeptide compound is configured to match a binding pocket of the enzyme target. Dahal teaches molecular docking studies of lead inhibitors into the ASADH active site to identify structural elements serving as critical binding determinants (Dahal, p. 522, right col.; p. 523). Combined with Powers's teaching of dipeptide-based vinyl sulfone scaffolds designed to access the extended substrate-binding architecture of cysteine-nucleophile enzymes (Powers, pp. 4683–4687), it would have been obvious to design the dipeptide compound of claim 7 with structural elements, guided by routine docking analysis of the type taught by Dahal, configured to complement the ASADH binding pocket.
Regarding claim 10: Claim 10 recites the compound comprises an amino acid. Powers teaches amino acid– and peptidomimetic-based vinyl sulfone inhibitor scaffolds as established tools for irreversible cysteine-enzyme inactivation (Powers, pp. 4683–4687, including amino acid–derived vinyl sulfone structures).
Regarding claim 11: Claim 11 recites the compound comprises a trifluoromethyl functional group. Powers specifically teaches that trifluoromethyl ketones function as potent, selective mechanism-based inactivators of serine and cysteine enzymes, and describes the incorporation of trifluoromethyl groups into inhibitor scaffolds as a known strategy for modulating the electrophilicity and reactivity of covalent warheads targeting active-site nucleophiles (Powers, pp. 4700–4703; ¶ Trifluoromethyl Ketones; Table 3.1). It would have been obvious to one of ordinary skill in the art to incorporate a trifluoromethyl functional group into a vinyl sulfone or sulfonyl acrylamide scaffold targeting ASADH, given this established precedent in covalent inhibitor design for cysteine-nucleophile enzymes.
Regarding claim 12, the claim depends from claim 11 (trifluoromethyl functional group) and recites that the compound comprises a carbonyl group. Powers teaches carbonyl-containing irreversible inhibitor scaffolds for cysteine and serine enzyme targets (Powers, Figure 39; p. 4667, left col. ¶ 1). Dahal's lead inhibitor compounds also include carbonyl-bearing structures (Dahal, pp. 524–525). It would have been obvious to combine a carbonyl group with the trifluoromethyl-substituted vinyl sulfone/sulfonyl acrylamide compounds of claim 11.
Regarding claim 13 (new), the claim recites that irreversible inhibition is not reversed by displacement upon exposure to excess exogenous cysteine or glutathione. Powers teaches that vinyl sulfones are also stable toward circulating thiols such as glutathione, as the second-order rate constant for Mu-Phe-Lys-VS-Ph (Mu ) 4-morpholinecarbonyl) with glutathione was only 5.5 x 10-4 M-1 s-1 for a representative peptidyl vinyl sulfone (p. 4684 right column ¶ specificity), reflecting the negligible reactivity of the covalently-formed adduct toward displacement by exogenous thiol nucleophiles. Testing an ASADH inactivator of the Dahal-Powers combination for resistance to thiol-mediated displacement is a routine confirmatory characterization of the covalent, irreversible mechanism the combination already renders obvious, and is the expected and predictable result of that mechanism rather than a separate inventive contribution.
Regarding claim 14 (new), the claim recites selective inactivation of fungal ASADH relative to bacterial ASADH ortholog via a compound comprising a 4-substituted benzyl group interacting with an arginine residue of the fungal ASADH absent in the bacterial ortholog.
Dahal establishes that species-selective inhibition between fungal and bacterial ASADH orthologs is achievable through substituent chemistry, reporting differential inhibitor potency across fungal (C. albicans, A. fumigatus, C. neoformans, B. dermatitidis) and bacterial (S. pneumoniae) ASADH forms despite high conservation of active-site architecture (Dahal, Table 1; pp. 523–524).
Viola '168 teaches a design strategy for species-selective ASADH inhibition using benzyl-substituted inhibitor scaffolds, in which introducing substituents at a defined position on a benzyl ring exploits a species-specific difference in a residue near the ASADH active site to achieve differential affinity between orthologs from different microbial species — a hydrophobic residue (Val14) in the more sensitive ortholog corresponding to charged residues, including arginine, in the less sensitive ortholog (Viola '168, Abstract; ¶ [0069], [0115], [0119]–[0121], [0132]).
It would have been obvious to apply the benzyl-substituent-based species-selectivity design strategy of Viola '168 to the fungal/bacterial ASADH pair of Dahal, with a reasonable expectation of success, given Dahal's independent demonstration that fungal/bacterial selectivity via substituent chemistry is achievable in this enzyme family. Routine docking analysis and optimization of substituent position and identity — the same approach used in Viola '168 to identify the residue basis for its own observed selectivity — would predictably lead to identification of a residue difference (here, an arginine present in the fungal form, absent in the bacterial form) responsible for observed selectivity, and to a 4-substituted benzyl group configured to exploit that difference.
Response to Arguments
Applicant’s arguments filed 9/1/2026 have been fully considered but are not found persuasive for the following reasons.
Regarding Dahal's alleged teaching away and the distinction between "teaching away" and "reasonable expectation of success":
Applicant argues that Dahal teaches away from the claimed invention because the compounds actually tested in Dahal showed freely reversible inhibition, and that the Office's prior response addressed only teaching-away without separately establishing a reasonable expectation of success. This argument is not persuasive.
Applicant is correct that these are distinct inquiries, and the Examiner does not conflate them. Dahal does not need to demonstrate that its own tested compounds behave covalently in order to supply a reasonable expectation of success for the claimed method. Dahal affirmatively discloses that the ASADH active site contains a cysteine nucleophile susceptible to covalent modification (Dahal, p. 524, right col. ¶ 2), and separately teaches that exploiting the full active-site environment could yield more potent inhibitors (Dahal, p. 525, left col. ¶ 2–3). The reasonable expectation of success arises from combining this disclosure of a covalently modifiable nucleophile with Powers's independent and well-established teaching that vinyl sulfones and sulfonyl-containing Michael acceptors reliably form covalent bonds with cysteine nucleophiles generally, across enzyme classes. Dahal's own reversible results with its own tested compounds — none of which were vinyl sulfones or sulfonyl acrylamides — simply reflect that Dahal did not test the claimed class of warhead; it does not undermine the expectation that a different, purpose-built covalent warhead applied to the same identified nucleophile would succeed. Applicant's cited authority, In re O'Farrell, 853 F.2d 894, 903–04 (Fed. Cir. 1988), is consistent with this analysis and does not compel a different result on these facts.
Regarding the "shared active-site cysteine chemistry" bridge and Powers's histidine-mediated mechanism:
Applicant argues that Powers ties vinyl sulfone reactivity specifically to a protonated active-site histidine characteristic of cysteine protease architecture, and that this mechanistic requirement is not shown to be met by ASADH, such that the Office's reliance on "shared active-site cysteine chemistry" alone improperly disregards the specific catalytic architecture Powers identifies as necessary.
This argument is not persuasive. Dahal's own molecular docking studies of the ASADH active site place a histidine residue (His-256) in direct proximity to the catalytic cysteine nucleophile (Cys-156) (Dahal, Fig. 1; Fig. 2; p. 527). This is the same class of active-site architecture — a cysteine nucleophile positioned near a histidine capable of participating in proton transfer to a resulting adduct — that Powers identifies as governing vinyl sulfone reactivity toward cysteine nucleophiles generally (Powers, p. 4645, right col. ¶ 2). Applicant has not identified any teaching in Dahal, or elsewhere of record, establishing that ASADH's histidine is incapable of the proton-transfer role Powers describes; to the contrary, Dahal's own disclosed active-site structure places the necessary catalytic elements — cysteine and histidine — in the same spatial relationship relied upon in Powers. A person of ordinary skill, reviewing Dahal's active-site structure alongside Powers's mechanistic teaching, would have had a reasonable expectation that ASADH's active site architecture supports the same reactivity, without resort to hindsight reconstruction from the claims.
Regarding the optimization/predictability argument and Dahal's fragment-screening methodology:
Applicant argues that Dahal's fragment-library screening and docking methodology is not comparable to iterative structure-guided optimization, and that the optimization criteria for covalent inhibitors (second-order rate constants for inactivation) differ fundamentally from those for the noncovalent inhibitors Dahal actually developed, such that Dahal's approach cannot supply the required predictability under KSR.
This argument does not address the rejection as framed and is not persuasive. The rejection does not rely on Dahal's fragment-screening or optimization methodology to render the claimed compounds obvious. It relies on the combination of (i) Dahal's identification of ASADH and its covalently modifiable active-site cysteine as a viable target, with (ii) Powers's independent, well-established teaching of vinyl sulfone and sulfonyl acrylamide chemistry as a known, predictable class of covalent cysteine-nucleophile inactivators, developed and characterized in enzyme systems entirely apart from Dahal's own fragment-library approach. The predictability required by KSR is predictability that combining these known elements — a known reactive target nucleophile and a known class of warheads for reacting with such nucleophiles — according to their established functions would succeed; it is not a requirement that Dahal's own optimization method be equivalent to covalent-inhibitor optimization practice.
Regarding claim 6 and the alleged mismatch between protease and ASADH active sites:
Applicant argues that the active sites of cysteine proteases (e.g., papain) and ASADH differ meaningfully despite sharing a cysteine-histidine pair — citing differences in cysteine pKa (protease cysteine anionic/conjugate base; ASADH cysteine neutral/conjugate acid) and in histidine protonation state — such that the design strategies applicable to one cannot be assumed transferable to the other.
This argument is addressed by, and does not overcome, the response above regarding the shared cysteine-histidine mechanism. Whatever quantitative differences exist in pKa or protonation state between the specific protease examples of Powers and ASADH, the qualitative mechanistic architecture relevant to vinyl sulfone reactivity — a nucleophilic cysteine positioned near a histidine capable of protonating the resulting adduct — is present in both enzyme systems, including ASADH via its own established catalytic mechanism. Applicant has not shown that the specific pKa or protonation differences identified would prevent, rather than merely modulate, the rate or efficiency of the covalent reaction; at most such differences bear on degree of reactivity, which is a matter of routine optimization, not a bar to the reasonable expectation of success required for obviousness.
Regarding claim 7 and Powers's relevance to a cleavable dipeptide:
Applicant argues that the dipeptide of claim 7 is fundamentally different in kind from the "intact" peptide inhibitors Powers discusses, because the claimed dipeptide is contemplated to be cleaved into its constituent amino acids, whereas Powers's peptidyl vinyl sulfones function as intact peptide inhibitors; Applicant further notes that Powers does not disclose amino acid vinyl sulfones.
This argument is not persuasive. Claim 7 recites only that "the compound is a dipeptide" — it does not recite cleavage of the dipeptide, a mechanism by which cleavage would occur, or any functional consequence of cleavage, and no such limitation is properly imported from the specification into the claim for purposes of this comparison. As claimed, a dipeptide-containing vinyl sulfone or sulfonyl acrylamide compound, whether or not later cleaved in vivo, is structurally encompassed by Powers's teaching of dipeptide-based and peptidomimetic vinyl sulfone scaffolds as established irreversible cysteine-enzyme inactivators (Powers, pp. 4683–4687, Figures 67–68). Applicant's observation that Powers does not separately disclose "amino acid vinyl sulfones" is addressed by claim 10 rather than claim 7 and does not bear on the dipeptide limitation of claim 7.
Regarding claim 7 and Ashburn's noncovalent, threonine-based TMC-95 mechanism:
Applicant argues that Ashburn's TMC-95 compound is a noncovalent inhibitor acting through a threonine nucleophile (the 20S proteasome catalytic residue), rather than a cysteine, and is therefore not pertinent to the presently claimed covalent, cysteine-directed chemistry.
This argument is not persuasive because it addresses a purpose for which Ashburn is not relied upon. Ashburn is cited solely for its teaching of dipeptide-containing biaryl framework synthesis as applied generally to enzyme inhibitor scaffold design (Ashburn, pp. 856–865), not for any covalent-mechanism or cysteine-targeting teaching. Ashburn's noncovalent, threonine-directed mechanism of action for its own TMC-95 target compound does not detract from Ashburn's relevance to the narrower structural teaching — dipeptide/biaryl scaffold construction — for which it is actually cited in combination with Powers's dipeptide vinyl sulfone teaching.
Regarding claim 11 and the alleged mismatch between trifluoromethylketones and trifluoromethylsulfones:
Applicant argues that trifluoromethylketones (which Powers discusses) function by nucleophilic addition to the carbonyl carbon, whereas trifluoromethylsulfones (encompassed by claim 11 in combination with claim 1's vinyl sulfone) cannot be attacked at sulfur in an analogous manner, such that the Office's reliance on Powers's trifluoromethylketone teaching to support claim 11 is chemically unsound despite the shared trifluoromethyl moiety.
This argument is not persuasive. Claim 11 recites only that "the compound comprises a trifluoromethyl functional group" and does not require that the trifluoromethyl group itself be the site of nucleophilic attack, or that it function by the same mechanism as a trifluoromethylketone. In the context of claim 1's vinyl sulfone, the site of nucleophilic attack remains the vinyl carbon, consistent with the mechanism taught by Powers and Dahal generally; the trifluoromethyl group of claim 11 functions instead as an electron-withdrawing substituent that modulates the electrophilicity of the adjacent reactive vinyl group. Powers's teaching that trifluoromethyl substitution is a known strategy for modulating electrophilicity and reactivity in covalent warhead design (Powers, pp. 4700–4703, ¶ Trifluoromethyl Ketones; Table 3.1) supports the obviousness of incorporating a trifluoromethyl substituent for this reactivity-modulating purpose in a vinyl sulfone context, regardless of whether the specific bond-forming step at the trifluoromethyl-bearing carbon differs between the two functional group classes.
Regarding claim 8 and the corrected construction of "isostere":
Applicant's correction of the prior Office Action's erroneous construction of "isostere" as "isomer" is accepted, and the § 103 rejection of claim 8 is maintained on the corrected grounds set forth above, which additionally note that Applicant's own Remarks acknowledge that the sulfonyl group in the claimed compounds is designed as a mimic of the phosphoryl group of the ASADH substrate (Remarks, p. 7), confirming that this design rationale flows directly from the combined teachings of Dahal and Powers.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ANDRE MACH whose telephone number is (571)272-2755. The examiner can normally be reached 0800 - 1700 M-F.
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, Robert A Wax can be reached at 571-272-0323. 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.
/ANDRE MACH/Examiner, Art Unit 1615
/Robert A Wax/Supervisory Patent Examiner, Art Unit 1615
Prosecution Insights