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 10/27/2025 in which claims 1-3, 6, 8-10, 21-23 were amended is acknowledged. Claims 11-20 were previously withdrawn. Claims 4, 5, 7 were previously canceled.
Claims 1-3, 6, 8-10, 21-23 are under examination on the merits.
Claim Objections
(Previous objections, withdrawn as to claims 1). Applicant’s amendments to claim 1 have overcome previous objections to claim 1.
(New objection, necessitated by amendment as to claims 1, 3, 9, and 10) Claims 1, 3, 9, and 10 are objected to because of the following informalities:
The recitation on amended claim 1 of “of human IL-16” should read “of a human IL-16”. Further the recitation of “no statistically significant increase” (in quotations) should not be in quotations.
The recitation on amended claims 3, 10 of “amino-acid” should read “amino acid” without the hyphen.
Amended claims 1, 3, and 9 are objected to because they fail to make reference to amino acid sequences by use of sequence identifiers (“SEQ ID NO:” or the like) in accordance to 37 CFR § 1.823(a)(5). Specifically, the recitation on claims 1 and 9 of “linker GSGSGSGGSS”, and on claim 3 the recitation of “an HA tag having the amino acid sequence YPYDVPDYA” fail to include a sequence identifier for the linker sequence. See MPEP 2422. Further it is noted that none of these sequences are part of the originally filed sequence listing. For purposes of compact prosecution and applying prior art, claims 1 and 9 were interpreted herein as referring to a linker, and claim 3 was interpreted herein as referring to an HA tag.
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.
(Previous rejections, withdrawn as to claims 1-3, 6, 8-10, 21-23) Claims 1-3, 6, 8-10, 21-23 were rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being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.
See claims 1-3, 6, 8-10, 21-23 as submitted on 10/27/2025.
Applicant’s amendment to claim 1 has overcome previous rejection to the instant claims.
(new rejection, necessitated by amendment as to claim 10) Claim 10 is 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.
See claim 10 as submitted on 10/27/2025.
Amended claim 10 recites “wherein the HIV-1 Tat polypeptide comprises the Tat amino-acid sequence of SEQ ID NO: 15 fused at its C-terminus to the c-Myc nuclear localization signal PAAKRVKLD (SEQ ID NO: 2)” This recitation is unclear because of the following. The amino acid sequence in SEQ ID NO: 15 is 111 amino acid residues long. Residues 102 to 110 at the C-terminus of the sequence comprise the sequence “YPYDVPDYA” which is an HA tag (Specification, pages 16-17). Claim 1 recites the order of elements comprising an HIV-1 Tat, as “in order from the N-terminus to the C-terminus, comprises: (i) an N-terminal hemaqqlutinin (HA) tag; (ii) a peptide sequence encoded N- terminal to the Tat coding sequence within the single open reading frame that targets the HIV-1 Tat polypeptide to the interior exosomal membrane such that the HIV-1 Tat polypeptide is localized within the exosome; (iii) a Tat sequence that includes the basic region RKKRRQRRR (SEQ ID NO: 28); and (iv) a C-terminal c-Myc nuclear localization signal consisting of PAAKRVKLD (SEQ ID NO: 2)”. Therefore, the sequence in SEQ ID NO: 15 does not follow the description recited in claim 1 because the HA tag appears at the C-terminal of an HIV-1 Tat sequence, where the c-Myc nuclear localization signal consisting of PAAKRVKLD (SEQ ID NO: 2) should be. Therefore, it is unclear in claim 10 if the c-Myc nuclear localization signal PAAKRVKLD (SEQ ID NO: 2) should be placed at the end of the HA tag of SEQ ID NO: 15 (contrary to the description of claim 1) or it should replace the HA tag, or other interpretation. For purposes of compact prosecution and applying prior art, claim 10 was interpreted herein consistent with independent claim 1 as referring to an HIV-1 Tat polypeptide fused at its C-terminus to the c-Myc nuclear localization signal PAAKRVKLD (SEQ ID NO: 2).
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.
(Previous rejection, withdrawn as to claims 1-3, 6, and 8-10) Claims 1-3 and 6-10 were rejected under 35 U.S.C. 103 as being unpatentable over Leonard, in view of Keane. (Prior art of record).
See claims 1-3, 6, and 8-10 as submitted on 10/27/2025.
Applicant’s amendments to claims 1, 6, and 8 have overcome the previous rejection to claims 1-3, 6, and 8-10.
Applicant’s cancelation of claim 7 has overcome the previous rejection to claim 7.
(new rejection, necessitated by amendments as to claims 1-3, 6, 9-10 and new claims 22-23) Claims 1-3, 6, 9-10, 22 and 23 are rejected under 35 U.S.C. 103 as being unpatentable over Leonard, Keane, and Donahue (prior art of record), in view of GenBank: CCD30449.1 and Rosenecker (Prior art of record).
Prior art of record.
See claims 1-3, 6, 9-10, 22 and 23 as submitted on 10/27/2025.
Regarding claim 1, the teachings of Leonard, Keane, and Donahue are described in detail in the previous Office Actions mailed on 03/12/2024, 01/29/2025, and 07/28/2025. The teachings of these references are summarized below:
Leonard teaches exosomes that include a packaging protein and a cargo RNA in which the packaging protein binds specifically to the cargo RNA (Fig. 3, Abstract). Leonard also teaches LAMP2b fusion proteins for expressing a protein of interest on the exosome surface, or exosome lumen (¶ [0014]). Leonard also teaches that exosomes are extracellular vesicles in the 30-200 nanometer (nm) diameter range (¶ [0073]). Leonard also teaches that a ligand that targets the exosomes to target cells may be present at the N-terminus of the fusion protein and expressed or present on the surface of the exosome where the ligand binds specifically to a receptor on the surface of the target cells (¶ [0007]). Leonard further teaches that such fusion vectors may serve one or more purposes, such as: to promote localization of the recombinant protein to a specific area of the cell (e.g., where the protein is fused to a nuclear localization signal (NLS), such as a c-myc domain at its N-terminus or C-terminus (¶ [0068]).
Keane teaches that CD4 serves as a receptor for IL-16 and that IL-16 induces a variety of responses in CD4+ cells through signal transduction (Page 5945, ¶ 1). Keane also teaches that the peptide RRKS (SEQ ID NO: 1 of instant application) is present in human IL-16 (Page 5946, col. 1, ¶ 4).
Donahue teaches a wild type HIV Tat protein which when delivered by a vector can cause reactivation of HIV in latently infected, CD4+ Jurkat cells (Abstract; Fig. 6; Page 3262, col. 1, ¶ 2). Specifically, the vast majority of latent viruses are potentially able to be reactivated when additional Tat is delivered (Pages 3261-3262). Donahue also teaches that latently infected resting memory CD4+ T cells are critical in HIV infection as they serve as the major source of viral rebound yet are not susceptible to antiretroviral therapy or host immune attack; thus, additional strategies to combat HIV-1 latency would be invaluable (Page 3258; col., 2., ¶ 2). Donahue further teaches that HIV-1 Tat protein might counteract many mechanisms involved in HIV-1 latency establishment (Page 3258; col., 2., ¶ 2). Donahue further teaches a vector comprising the Tat protein fused to a His tag at its C-terminus wherein the His tag did not affect Tat’s biological activities (Page 3255; col., 2., ¶ 1).
The amendment to claim 1 as submitted on 10/27/2025 recites the following features:
a) the exosome presents, on its surface, a Lamp2b/IL-16 fusion protein in which an interleukin-16 (IL-16) domain consists of the C-terminal 20 amino acids of human IL-16 (SEQ ID NO: 7; TIVIRRKSLQSKETTAAGDS) and is fused to the N-terminus of Lamp2b via a peptide linker GSGSGSGGSS, wherein the lL-16 domain comprises the RRKS motif (SEQ ID NO: 1) required for CD4 binding;
b) the exosome comprises, within its lumen, an HIV-1 Tat polypeptide that is encoded in a single open reading frame and, in order from the N-terminus to the C-terminus, comprises: (i) an N-terminal hemaqqlutinin (HA) tag; (ii) a peptide sequence encoded N- terminal to the Tat coding sequence within the single open reading frame that targets the HIV-1 Tat polypeptide to the interior exosomal membrane such that the HIV-1 Tat polypeptide is localized within the exosome; (iii) a Tat sequence that includes the basic region RKKRRQRRR (SEQ ID NO: 28); and (iv) a C-terminal c-Myc nuclear localization signal consisting of PAAKRVKLD (SEQ ID NO: 2); wherein the features recited in elements (a) and (b) above are present in the same exosome; and
c) when tested by flow cytometry as described herein on resting human CD4+ T lymphocytes after a 48-hour incubation with the composition, the percentage of cells expressing CD25, CD69, or HLA-DR does not show a statistically significant increase relative to cells treated with control exosomes prepared in the same manner but lacking the Lamp2b/IL-16 fusion of element (a) and the HIV-1 Tat polypeptide of element (b), as determined by an unpaired two-tailed t-test with a significance threshold of p <0.05 such that "no statistically significant increase" corresponds top ≥ 0.05.
As discussed previously these limitations are already taught by the cited prior art as follows:
a) Leonard and Keane already teach an IL-16/Lamp2b gene fusion for expressing a protein of interest on the exosome surface, or exosome lumen, wherein the IL16 is fused to the N-terminus of Lamp2b (Leonard, ¶ [0014]; Keane, page 5945). Leonard further teaches linkers joining the two coding regions (Leonard, ¶ [0064]). Keane further teaches that the peptide RRKS (SEQ ID NO: 1 of instant application) is present in human IL-16 and it is required for CD4 receptor binding (page 5946, col. 1). Keane further teaches a 16 amino acid residue long (RRKSLQSKETTAAGDS) which is responsible for physically associating with a CD4 receptor (pages 5943, col. 1; 5950, col. 1). With respect to the sequence in instant SEQ ID NO: 7 (TIVIRRKSLQSKETTAAGDS) it is noted that this sequence contains 4 additional amino acids at its N-terminus prior to the RRKS motif relative to the Keane’s sequence. The addition of four amino acids (which are also taught by Keane, Fig. 1) to the peptide taught by Keane is considered to be one determined by routine optimization within prior art conditions or through routine experimentation according to one of skill in the art in view of the teachings of Keane and Leonard. The addition of 4 amino acid residues to the fragment taught by Keane is considered routine optimization because those 4 residues (which are also taught by Keane) precede the crucial RRKS motif which is required for binding and because optimizing the length of individual fragments in a fusion protein to achieve proper expression is recognized routine practice in the art (See Keane, see Nicolls et al. 1999 [cited in Applicant’s IDS]). Such embodiment, consisting of SEQ ID NO: 7 is therefore an obvious variant and/or routine optimization of the peptide taught by Keane. Further, it is noted that there is no indication that the peptide of SEQ ID NO: 7 presents advantageous features over Keane’s peptide given that both comprise the crucial RRKS motif necessary for CD4 receptor binding. It would have been a matter of routine experimentation using standard laboratory techniques available before the effective filing date to determine the optimal length of a human IL-16 C-terminal fragment to achieve CD4 receptor binding with a reasonable expectation of success.
b) Leonard and Donahue already teach an exosome comprising the elements as recited in b). Specifically, Donahue teaches a sequence consisting of a wild type HIV-1 Tat polyprotein which when delivered by a vector can cause reactivation of HIV-1 in latently infected, CD4+ Jurkat cells (Abstract; Fig. 6; Page 3262, col. 1, ¶ 2). Leonard further teaches multiple tags and localizations signals, specifically Leonard teaches (i) an HA tag at the N-terminus of the fusion proteins, (ii) a localization signal to promote localization of the fusion protein to a specific area of the cells, and (iii) a nuclear localization signal (NLS), such as a C-myc domain, at a N-terminus or a C-terminus of a packaging protein which functions to direct localization of the packaging protein to the nucleus of the cell and can be fused to a packaging protein at its N-terminus or C-terminus (Leonard, ¶ [0068]). GenBank: CCD30449.1 is cited for teaching the sequence of a HIV-1 Tat protein which is a well-known sequence in the art and it comprises instant SEQ ID NO: 28. See alignment below (Qy is instant SEQ ID NO: 28; Db is GenBank: CCD30449.1). As previously explained, Rosenecker teaches an amino acid sequence which serves as a nuclear localization sequence (NLS) and can be used for transferring a molecule into eukaryotic cells (Abstract), Rosenecker’s NLS consists of a protein sequence which shares 100% sequence identity to SEQ ID NO: 2, alignment of record.
PNG
media_image1.png
156
690
media_image1.png
Greyscale
c) with respect to the recitations in “c)”, these limitations do not impart any additional structural features to the exosomes as recited in claim 1 (a-b), therefore they are considered to flow from the features already present in the exosomes as recited in claim 1 (a-b). Accordingly, any composition comprising the exosome of claim 1 (a-b) in the prior art having the all of the structural limitations recited in claim 1 (a-b) would be capable of not showing a statistically significant increase in the percentage of cells expressing CD25, CD69, or HLA-DR relative to control cells as recited in claim 1 c).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to have modified the targeted exosome of Leonard to incorporate IL-16 to target exosomes to CD4+ cells via a linker as taught by Keane, and further to comprise a latency reversal agent, HIV Tat polypeptide as taught by Donahue with an HA tag, a localization peptide and a C-myc nuclear localization signal as taught by Leonard to formulate the embodiment as recited in claim 1 (a-b). It is noted that all of the sequences recited in amended claim 1 were known in the art.
One of ordinary skill in the art would have been motivated to combine the teachings of Leonard, Keane, Donahue, GenBank: CCD30449.1 and Rosenecker to create compositions that can deliver the latency reversal agent HIV Tat polypeptide fused to a C-myc nuclear localization signal to CD4+ cells to induce transcriptional activation of latent HIV-1.
One of ordinary skill in the art would have had a reasonable expectation of success for formulating such an embodiment as recited above given that the methods of molecular cloning and exosome expression are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding amended claim 2, as indicated previously, Leonard already teaches that exosomes are extracellular vesicles in the 30-200 nanometer (nm) diameter range (¶ [0073]). In view of MPEP 2131.03, the range of 30-200 nm falls within the range of instant claim 2. Therefore, the diameters taught by Leonard meet the limitations of claims 2.
Regarding amended claim 3, as indicated above, Leonard teaches an HA tag at the N-terminus of the fusion proteins (¶ [0068]) and Donahue teaches a sequence consisting of a wild type HIV-1 Tat polyprotein.
Regarding amended claim 6, as explained above all of these elements are taught by Donahue, Leonard, GenBank: CCD30449.1, and Rosenecker. With respect to the configuration or order of the elements recited in claim 6, Leonard teaches placing amino acid sequences in a functional relationship to each other, for example operatively linked to a promoter (¶ [0064]). Leonard further teaches placement of the HA tag, and other localizations signals at the N-terminus or the C-terminus (¶ [0068]). Therefore, the configuration or order of the elements recited in claim 6 is considered to be one determined by routine optimization within prior art conditions or through routine experimentation according to one of skill in the art in view of the teachings of Leonard. It would have been a matter of routine experimentation using standard laboratory techniques available before the effective filing date to determine the optimal configuration or order of the elements recited in claim 6 to achieve efficient expression with a reasonable expectation of success.
Regarding amended claim 8, Leonard already teaches Lamp2b fusion proteins comprising full length Lamp2b (¶¶ [0014], [0076]).
Regarding amended claim 9, as indicated above Leonard further teaches linkers joining the two coding regions (Leonard, ¶ [0064]). Keane teaches a 16 amino acid residues long (RRKSLQSKETTAAGDS) which is responsible for physically associating with a CD4 receptor (pages 5943, col. 1; 5950, col. 1; ). With respect to the sequence in instant SEQ ID NO: 7 (TIVIRRKSLQSKETTAAGDS) it is noted that this sequence contains 4 additional amino acids at its N-terminus prior to the RRKS motif relative to the Keane’s sequence. The addition of four amino acids (which are also taught by Keane, Fig. 1) to the peptide taught by Keane is considered to be one determined by routine optimization within prior art conditions or through routine experimentation according to one of skill in the art in view of the teachings of Keane and Leonard. The combination of the teachings of Keane and Leonard meet the limitations of amended claim 9.
Regarding amended claim 10, as indicated above, Donahue teaches a sequence consisting of a wild type HIV-1 Tat polyprotein which when delivered by a vector can cause reactivation of HIV-1 in latently infected, CD4+ Jurkat cells (Abstract; Fig. 6; Page 3262, col. 1, ¶ 2). Leonard further teaches multiple tags and localizations signals, specifically Leonard teaches (i) an HA tag at the N-terminus of the fusion proteins, (ii) a localization signal to promote localization of the fusion protein to a specific area of the cells, and (iii) a nuclear localization signal (NLS), such as a C-myc domain, at a N-terminus or a C-terminus of a packaging protein which functions to direct localization of the packaging protein to the nucleus of the cell and can be fused to a packaging protein at its N-terminus or C-terminus (Leonard, ¶ [0068]). As previously explained, Rosenecker teaches an amino acid sequence which serves as a nuclear localization sequence (NLS) and can be used for transferring a molecule into eukaryotic cells (Abstract), Rosenecker’s NLS consists of a protein sequence which shares 100% sequence identity to SEQ ID NO: 2, alignment of record.
Regarding amended claims 21-23, the recitations of “wherein the exosome is positive for exosomal markers CD63 and TSG101 as detected by an immunoblot” (in claim 21); “when tested by flow cytometry on resting human CD4+ T lymphocytes after a 48-hour incubation with the composition, does not show a statistically significant increase in Annexin V-positive cells relative to cells treated with control exosomes prepared in the same manner, as determined by an unpaired two-tailed t-test with a significance threshold of p < 0.05, such that "no statistically significant increase" corresponds to p > 0.05” (in claim 22); and “when evaluated relative to control exosomes prepared in the same manner, exhibits no statistically significant increase (p > 0.05 by unpaired two-tailed t-test) in levels of one or more cytokines selected from IL--2,IL--4, IL-6, IL-8, IL-10, IL-17a, IFN-y, TNF-a, and GM-CSF” (in claim 23), respectively do not impart any additional structural features to the exosomes as recited in claim 1, therefore they are considered to flow from the features already present in the exosomes as recited in claim 1. Accordingly, any composition comprising the exosome of claim 1 (a-b) in the prior art having the all of the structural limitations recited in claim 1 (a-b) would be capable of generating the experimental results as recited in claims 21-23.
Response to Arguments
Applicant's arguments filed 10/27/2025 have been fully considered but they are not persuasive.
Applicant contends on page 13 of the Remarks submitted on 10/27/2025:
It is respectfully submitted that claim 1 is now limited to a specific, sequence- defined architecture that the cited art neither teaches nor suggests. Leonard discusses exosome engineering and LAMP fusions in general but does not disclose (i) a Lamp2b/IL-16 fusion in which the IL-16 domain is exactly the C-terminal 20 aa (SEQ ID NO:7) with the RRKS motif and (ii) fusion to the N-terminus of Lamp2b via the precise linker GSGSGSGGSS. Keane addresses IL-16 biology/CD4 binding, but not presenting only the 20-aa IL-16 fragment on exosomes via Lamp2b with that specific linker. Donahue identifies Tat as a latency-related factor, yet provides no teaching to package Tat intraluminally while, in the same exosome, displaying the IL-16/Lamp2b construct on the surface.
It is respectfully presented that further, claim 1 requires the Tat polypeptide to be encoded in a single ORF in a fixed order-N-terminal HA tag -- interior-exosomal-membrane targeting peptide -- Tat (including RKKRRQRRR) -> C-terminal c-Myc NLS (PAAKRVKLD)-a non-routine construct absent from the art and not rendered obvious by generic mentions of tags or NLSs. The art provides no motivation to assemble this particular arrangement to achieve the claimed trafficking and compartmentalization.
In response:
The Examiner acknowledges the Remarks submitted by Applicant in regards to the amend of claim 1. The instant rejection is in view of instant claim language. Although the claims are interpreted in light of the Specification, limitations from the Specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). It is herein maintained that the cited prior art provides clear teachings, suggestions and motivation to arrive at the claimed invention. Specifically, an exosome comprising a fusion protein comprising Lamp2b and IL-16 are explicitly taught by the combined cited prior art. As to the C-terminal 20 aa (SEQ ID NO:7), as explained above the C-terminal fragment of an IL-16 is well known and its CD4 binding function is well recognized in the art (See Keane, see Nicolls et al. 1999 [cited in Applicant’s IDS]). The addition of 4 amino acid residues to the fragment taught by Keane is considered routine optimization because those 4 residues (which are also taught by Keane) precede the crucial RRKS motif which is required for binding and because optimizing the length of individual fragments in a fusion protein to achieve proper expression is recognized routine practice in the art (See Keane, see Nicolls et al. 1999 [cited in Applicant’s IDS]). It would have been a matter of routine experimentation using standard laboratory techniques available before the effective filing date to determine the optimal length of a human IL-16 C-terminal fragment to maximize proper folding, solubility, etc. while maintaining function (in this case, CD4 receptor binding) with a reasonable expectation of success.
As explained above, such embodiment, consisting of SEQ ID NO: 7 is therefore an obvious variant and/or routine optimization of the 16 aa peptide taught by Keane. Further, it is noted that there is no indication that the peptide of SEQ ID NO: 7 presents advantageous features over Keane’s peptide given that both comprise the crucial RRKS motif necessary for CD4 receptor binding. With respect to packaging Tat intraluminally, as explained previously this feature does not impart any additional structural features to the exosomes as recited in claim 1, therefore intraluminal packaging is considered to flow from the features already present in the exosomes as recited in claim 1. Therefore, Applicant’s arguments regarding the individual elements discussed above are unpersuasive.
Conclusion
No claims are allowed.
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 MARLENE V BUCKMASTER whose telephone number is (703)756-5371. The examiner can normally be reached M-F 8-5.
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, Thomas J Visone can be reached at (571) 270-0684. 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.
/MARLENE V BUCKMASTER/Examiner, Art Unit 1671
/THOMAS J. VISONE/Supervisory Patent Examiner, Art Unit 1672