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 .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 09/30/2025 has been entered.
Claims 14-17, 19-22 and 25 are pending in the application. Claims 14, 20, 25 were amended. Claims 1-13, 18, 23 and 24 were previously canceled.
Claims 14-17, 19-22 and 25 are currently under examination on the merits.
Information Disclosure Statement
The information disclosure statement (IDS) was submitted on 10/11/2021, 01/23/2023, 07/11/2023, 11/16/2023, 03/07/2024, 10/28/2024 and 04/17/2025. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
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(Previous rejections, withdrawn as to claims 14-17, 19-22 and 25) Claims 14-17, 19-22, and 25 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being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.
See claims 14-17, 19-22 and 25 as submitted 09/05/2025.
The previous rejection of claims 14-17, 19-22 and 25 is moot in view of Applicant’s amendments submitted on 09/05/2025.
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.
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 14, 19, and 22 are rejected under 35 U.S.C. 103 as being unpatentable over He et al. in view of Zhu et al. and Fan et al. (prior art of record), as evidenced by Telles and Seto, Thermo Fisher 293A cell line User Guide 2016., and Lv et al. (prior art of record), further in view of Zhang et al. (prior art of record).
See claims 14, 19 and 22 as submitted on 09/05/2025.
As to claim 14, it is noted that the amendment of “wherein the produced PCV2 VLPs are present inside or outside the mammalian cells” was made to overcome the previous rejections under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph set forth in the Final Office Action mailed 06/05/2025. However, this new limitation is already taught by the cited prior art. Specifically the method of He et al. comprises producing PCV2 VLPs wherein the produced particles are present in the cytoplasm or the nucleus of mammalian cells as verified by immunofluorescence (page 5, ¶ 9).
With respect to all of the other limitations of claim 14, as previously explained, He et al. teach a method for producing porcine circovirus type 2 (PCV2) virus-like particles (VLPs) (Abstract; page 3, ¶ 1) comprising the following steps:
Providing HEK-293A cells (cultured mammalian cells, as recited in claim 14) (page 4, ¶ 7, 8)
Transfecting HEK-293A cells with a recombinant plasmid pAD-ΔCap-ΔVp2 comprising the PCV2 gene encoding the capsid protein of PVC2 (page 4, ¶ 4, 5, 7, 8)
Washing and centrifuging the HEK-293A cells after they have been transfected (page 6, ¶ 2)
Resuspending the HEK-293A cells in a phosphate buffered saline (PBS) solution after centrifuging (page 6, ¶ 2)
Subjecting the HEK-293A cells to ultrasonic lysis (performing sonication, as recited in claim 14) (page 6, ¶ 2)
Performing two more centrifugation cycles after the HEK-293A cells were sonicated, one cycle for 24000 r/min for 15 min followed by a second cycle 20000 r/min for 10 min (page 6, ¶ 2)
He et al. do not teach the steps of (a) adding valproic acid (VPA) sodium salt to the transfected mammalian cells, wherein the addition of the VPA sodium salt inhibits cell proliferation, (b) performing multiple freeze and thaw cycles on the mammalian cells, and wherein the capsid protein is modified with a secretion signal sequence introduced at an NH2 terminal of the capsid protein.
However, Fan et al. teach the step (a) of adding valproic acid (VPA) sodium salt to mammalian cells for the benefit of enhancing viral gene expression, wherein the addition of the VPA sodium salt inhibits histone deacetylases (HDACs) thereby modifying gene transcription (Abstract; page 1, ¶ 2). As evidenced by Telles and Seto, HDACs act to promote cell cycle progression and proliferation, therefore HDAC inhibitors potently inhibit cell proliferation (Abstract; page 2, ¶ 1).
Zhu et al. teach a method for enhanced replication of porcine circovirus type 2 (PCV2) in mammalian cells (a porcine kidney cell line termed PK15) (Abstract, page 1), comprising the step (b) of performing three freeze-thawed cycles for retrieval of produced viral particles (page 7, ¶ 1).
Zhang et al. teach a method of secreted expression of CPV2 particles comprising a vector comprising the PCV2 capsid protein and the N-terminal secretion signal peptide for increased extracellular expression of a PCV2 capsid protein, wherein the vector induces an antibody response (Abstract, page 2, ¶ 5; page 9, ¶ 2).
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date to have included the teachings of Fan et al., Zhu et al., and Zhang et al. in a method for producing PCV2 viral particles for the benefit of enhancing intracellular and extracellular viral gene expression and later for effective retrieval of produced viral particles, as taught by Fan et al., Zhu et al., and Zhang et al.
One of ordinary skill in the art would have had a reasonable expectation of success for introducing a step of adding VPA sodium salt to mammalian cells and another step for performing three freeze-thaw cycles to retrieve intracellular and extracellular virus particles given that the methods of virus production, viral gene expression, and viral particle retrieval are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claim 19, He et al., Zhu et al., Fan et al., and Zhang et al. in combination teach the method of claim 14. It is noted that no amendments were introduced to claim 19. As previously explained, He et al. further teach HEK-293 A cells (page 6, ¶ 2) which is a subcloned cell line of HEK-293 cells, as evidenced by Thermo Fisher 293A cell line User Guide (page 4, ¶ 1). Hence, HEK-293 A cells constitute a species within the HEK-293 genus. Accordingly, the teachings of He et al. meet the limitations of claim 19.
Regarding claim 22, He et al., Zhu et al., Fan et al., and Zhang et al. in combination teach the method of claim 14. It is noted that no amendments were introduced to claim 22. As previously explained, Zhu et al. further teach the VLPs from the PCV2 strain BJW which correspond to the group PCV2b VLPs as evidenced by Lv et al. (Table 2, 3rd row).
Accordingly, claims 14, 19 and 22 were prima facie obvious to one of ordinary skill in the art before the effective filing date, especially in the absence of evidence to the contrary.
Claims 15-17 are rejected under 35 U.S.C. 103 as being unpatentable over He et al., Zhu et al., Fan et al., and Zhang et al. as applied to claims 14, 19 and 22 above, and further in view of Khayat, et al. (2011) as evidenced by, Thermo Fisher Tech Tip #40, and Beckman Coulter 2025 (prior art of record).
See claims 15-17 as submitted on 09/05/2025.
Regarding claim 15, He et al., Zhu et al., Fan et al., and Zhang et al. in combination teach the method of claim 14. It is noted that there was no amendment to claim 15. As previously explained, He et al. further teach washing mammalian cells previously transfected with PBS and centrifuging at 1000 r/min for 15 min and at 24000 r/min for 10 minutes. (page 6, ¶ 2). The centrifuging speed taught by He et al. can be expressed in units of gravity (g) depending on the size of the rotor. As evidenced by Thermo Fisher Tech Tip # 40, the centrifuging speeds taught by He et al. can range between 45 x g and 168 x g for the first centrifuging cycle and between 26,000 x g and 96,600 x g for the second centrifuging cycle, depending on the size of the rotor used.
He et al. does not teach the size of the rotor used, therefore the precise centrifuging speeds are not indicated.
However, Khayat et al. 2011 teach a method for producing purified PCV2 VLPs for the purpose of purifying and further solving the crystal structure of such particles (Abstract). Khayat et al. 2011 further teach PCV2 VLP purification comprising centrifuging the cells at 15,300 x g for 15 min, 184,048 x g for 2.5 hours, and 16,100 x g for 10 min (page 3, column 1, ¶ 6).
In view of the teachings of He et al. and Khayat et al 2011, the claimed centrifuging speeds and times as recited in claim 15 are considered to be those determined by routine optimization according to one of ordinary skill in the art.
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have optimized the centrifuging speeds and times for the benefit of maximizing PCV2 viral particle retrieval and achieving a high degree of purification.
One of ordinary skill in the art would have had a reasonable expectation of success for optimizing the centrifuging speeds and times to maximize PCV2 viral particle retrieval and later purification given that the methods of virus production, viral particle retrieval, and viral particle purification are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claim 16, He et al., Zhu et al., Fan et al., and Zhang et al. in combination teach the method of claim 14. It is noted that there was no amendment to claim 16. As previously explained, Zhu et al. further teach incubating mammalian cells at 37 °C, and storing at −80 °C (page 7, column 1, ¶ 2; page 4, column 1, ¶ 1). Therefore, the teachings of Zhu et al. on freezing and thawing temperatures meet the limitations of claim 16.
Regarding claim 17, He et al., Zhu et al., Fan et al., and Zhang et al. in combination teach the method of claim 14. It is noted that there was no amendment to claim 17. As previously explained, the cited prior art teaches a wide range of centrifuging speeds and times. Khayat et al. 2011 further teach a step of clarifying the pellet by centrifugation at 16,100 x g for 10 min at 4°C (page 3, column 1, ¶ 6), demonstrating that adding a step of centrifuging after the VLPs have been pelleted is well known and commonly practiced in the art. Accordingly, the centrifuging speeds and times recited in claim 17 are considered to be those determined by routine optimization according to one of skill in the art in view of the teachings of the cited prior art.
Accordingly, claims 15-17 were prima facie obvious to one of ordinary skill in the art before the effective filing date, especially in the absence of evidence to the contrary.
Claims 20 and 21 are rejected under 35 U.S.C. 103 as being unpatentable over He et al., Zhu et al., Fan et al., and Zhang et al. as applied to claims 14, 19 and 22 above, and further in view of Invitrogen pcDNA3.4 (prior art of record) and GenBank Accession number: AHX25876.1. Published on 11/04/2014 (See PTO-892: Notice of References Cited).
See claims 20 and 21as submitted on 09/05/2025.
Regarding claim 20, He et al., Zhu et al., Fan et al., and Zhang et al. in combination teach the method of claim 14. It is noted that the amendment of “wherein the plasmid includes…” was made to overcome the previous rejections under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph set forth in the Final Office Action mailed 06/05/2025. Given that no other new limitations were introduced to claim 20, the rejection set forth previously still applies to claim 20.
As previously explained, Invitrogen teaches the commercially available construct pcDNA3.4 and it further teaches including a kozak sequence in addition to the gene of interest for optimal expression in mammalian cells (page 4, page 8).
Invitrogen does not teach a PCV2 gene sequence.
However, GenBank Accession number: AHX25876.1 teaches a gene sequence for the PCV2 capsid protein. See MPEP 2144.07. The selection of a known material based on its suitability for its intended use supported a prima facie obviousness determination in Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945).
As to the recognition sites recited in claim 20, NheI and NotI, He et al. teach the use of KpnI and NotI recognition sites (page 5, ¶ 5). However, one of ordinary skill in the art would have been able to use any recognition sites available within the vector to clone the PCV2 capsid gene sequence into the pcDNA3.4 construct. NheI and NotI are merely examples of restriction sites commonly used to clone target genes into vectors. See MPEP 2144.06. Substituting Equivalents Known For The Same Purpose: In order to rely on equivalence as a rationale supporting an obviousness rejection, the equivalency must be recognized in the prior art, and cannot be based on applicant’s disclosure or the mere fact that the components at issue are functional or mechanical equivalents. In re Ruff, 256 F.2d 590, 118 USPQ 340 (CCPA 1958).
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have included the PCV2 capsid gene sequence within the pcDNA3.4 construct given that the pcDNA3.4 construct was commercially available, the inclusion of a kozak sequence was taught by Invitrogen, and the PCV2 capsid gene sequence was known in the art before the effective filing date. One of ordinary skill in the art would have been motivated to do so for the benefit of formulating a construct for optimal expression in mammalian cells comprising the PCV2 capsid gene sequence.
One of ordinary skill in the art would have had a reasonable expectation of success for including the PCV2 capsid gene sequence within the pcDNA3.4 construct given that the methods of vector cloning are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Therefore, such a plasmid pcDNA3.4-PCV2 as recited in claim 21 and described in claim 20 was an obvious embodiment to one of ordinary skill in the art before the effective filing date in view of the teachings of the cited prior, especially in the absence of evidence to the contrary.
Claim 25 is rejected under 35 U.S.C. 103 as being unpatentable over He et al., Zhu et al., Fan et al., and Zhang et al. as applied to claims 14, 19 and 22 above, and further in view of GenBank Accession number: AHX25876.1. Published on 11/04/2014 and PG Pub US 2020/0046824 A1 to Luo. Filed on 10/19/2017 (See PTO-892: Notice of References Cited).
See claim 25 as submitted on 09/05/2025.
Regarding claim 25, He et al., Zhu et al., Fan et al., and Zhang et al. in combination teach the method of claim 14. It is noted that claim 25 was amended to recite “wherein the capsid protein comprises the amino acid of SEQ ID NO: 4 and/or the capsid protein is encoded by the nucleotide sequence of SEQ ID NO: 3”. It is noted that the amended recitation is being interpreted herein as requiring the entire length of the amino acid sequence of instant SEQ ID NO: 4 and/or the nucleotide sequence of instant SEQ ID NO: 3. The amino acid sequence of instant SEQ ID NO: 4 is 249 residues long. The sequence consists of the following:
Amino acid residues 1-16 – secretion signal peptide
Amino acid residues 17-249 – PCV2 capsid protein
As explained above, GenBank Accession number: AHX25876.1 teaches a gene sequence for the PCV2 capsid protein which shares 100% sequence identity with amino acid residues 17-249 in instant SEQ ID NO: 4. See alignment below (Qy is instant SEQ ID NO: 4; Db is AHX25876.1).
PNG
media_image1.png
401
780
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Greyscale
GenBank Accession number: AHX25876.1 does not teach amino acid residues 1-16 encoding a secretion signal peptide.
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169
882
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Greyscale
However, Luo teaches a method of producing VLPs in mammalian cells wherein the VLPs comprise fusion proteins (¶¶ [0031]-[0039]). Luo further teaches said fusion protein comprises a signal peptide to facilitate secretion of the VLPs. Said signal peptide may comprise a hemagglutinin (HA) signal peptide (¶¶ [0031]-[0039]). Luo further teaches an HA signal peptide SEQ ID NO: 96 which shares 100% sequence identity with amino acid residues 1-16 in instant SEQ ID NO: 4. See alignment below (Qy is instant SEQ ID NO: 4; Db is Luo’s HA secretion signal peptide).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to have incorporated the secretion signal peptide of Luo to the PCV2 capsid protein sequence in GenBank Accession number: AHX25876.1 for the benefit of facilitating secretion of the VLPs thereby maximizing VLP yields. See MPEP 2144.07. The selection of a known material based on its suitability for its intended use supported a prima facie obviousness determination in Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945).
One of ordinary skill in the art would have had reasonable expectation of success in incorporating the secretion signal peptide of Luo into the PCV2 capsid protein sequence in GenBank Accession number: AHX25876.1 given that the sequences are well known in the art and the methods of fusing signal peptide sequences to viral proteins are well known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Therefore, such a sequence comprising the entire length of the amino acid sequence of instant SEQ ID NO: 4 was an obvious embodiment to one of ordinary skill in the art before the effective filing date in view of the teachings of the GenBank Accession number: AHX25876.1 and Luo, especially in the absence of evidence to the contrary.
Response to Arguments
Applicant's arguments filed 09/05/2025 have been fully considered but they are not persuasive.
Applicant contends on page 6 of the Remarks submitted on 09/05/2025:
“Applicant respectfully submits that the citations of record, whether view alone or in combination, do not disclose or suggest all of the features of claim 14. Specifically, the citations of record fail to disclose or suggest at least the recitation "wherein the capsid protein is modified with a secretion signal sequence introduced at an NH2 terminal of the capsid protein…
The study by Zhang et al. utilizes two different peptides-one from ubiquitin-specific peptidase and another from prolactin. These peptides were added to the N-terminus of PCV2 capsid genes lacking the nuclear localization signal (NLS), along with additional sequences at both the N- and C-termini, and the expression of the capsid protein gene of the recombinant viruses was determined. While this combination of modifications to the recombinant viruses appears to allow some release of the PCV2 capsid protein into the culture medium, it is not clear from the results of Zhang et al. whether this is due to the removal of the NLS, the addition of the above peptides, or a combination of both. Indeed, the study of Zhang et al. concludes that NLS on the N-terminus of the capsid gene may impede secretion expression, but does not conclude that the inclusion of ubiquitin-specific peptidase itself provides enhanced secretion expression. See Zhang et al., page 9, fifth paragraph. Notably, the authors did not include a construct that lacks both the NLS and signal peptides, which would have helped determine the specific contribution of each element to capsid localization. Moreover, the role of the other terminal sequences added to the PCV2 capsid protein in intracellular trafficking is not addressed.”
In response: As evidenced by the cited prior art (see Zhang et al., see Luo), addition of signal peptides to constructs comprising viral capsid proteins for the purpose of redirecting localization of particles has been extensively studied in the art and further it is routinely practiced. In the instant case, the teachings of Zhang et al. demonstrate that such addition of a signal peptides can indeed boost secretion of the produced PCV2 VLPs and maximize yields (see Zhang et al. Fig. 3), regardless of whether this effect was due to “removal of the NLS, the addition of the above peptides, or a combination of both.” It is noted that teasing apart the culprit behind such effect is not required by instant claims. Therefore, Applicant’s argument that “it is not clear from the results of Zhang et al. whether this is due to the removal of the NLS, the addition of the above peptides, or a combination of both” is unpersuasive. Further, it is noted that the enhanced secretion by inclusion of a ubiquitin-specific peptidase observed by Zhang et al. is shown in, for example, Fig. 3. Accordingly, it is herein maintained that Zhang et al. provide a clear teaching and motivation for adding a secretion signal peptide to the N-terminus of a PCV2 capsid protein.
Applicant contends on page 7 of the Remarks submitted on 09/05/2025:
“Finally, it is noted that Zhang et al. discloses a study of the expression of the capsid gene of porcine circovirus type 2 in recombinant viruses and the implications on developing viral vectors. This is a very different from the presently claimed method of producing PCV2 virus-like particles. Indeed, virus-like particles as produced by the claimed method are distinct from both recombinant viruses and viral vectors as discussed in Zhang et al. Accordingly, Applicant respectfully submits that the proposed combination of teachings in Zhang et al., He et al, Zhu et al., and Fan et al. could only result in the method of claim 14 with the help of the teachings of the present application, and thus the proposed combination is the result of impermissible hindsight reconstruction.
In response: As evidenced by the cited prior art (see He et al., Zhu et al., Zhang et al.) production of recombinant viral particles and VLPs follow the same principles wherein the viral particle, be it a recombinant virus or a VLP, is formed by a viral capsid protein bearing the appropriate regulatory sequences. The most important difference between the two types of particles is that recombinant virus carries viral genetic material and VLPs typically do not (see He et al., Zhu et al., Zhang et al.). However, as indicated above both, recombinant viral particles and VLPs, are comprised by a viral outer shell or in the instant case, a capsid protein. Therefore, absent evidence to the contrary, it is herein maintained that the teachings of Zhang et al. about producing recombinant viral proteins comprising a PCV2 capsid protein can be naturally applied to producing VLPs with the same PCV2 capsid protein. Further, it is noted that the capsid protein of PCV2 has been extensively characterized for producing both recombinant viruses and VLPs (see He et al., Zhu et al., Zhang et al.).
Applicant contends on page 7 of the Remarks submitted on 09/05/2025:
“Applicant respectfully submits that at least the above features of amended claim 25 are not taught or suggested by the citations of record. Specifically, none of the citations of record teach or suggest that said capsid protein "comprises the amino acid sequence of SEQ ID NO: 4 and/or the capsid protein is encoded by the nucleotide sequence of SEQ ID NO: 3." While the Examiner points to GenBank Accession number: ABX71783.1 as disclosing a gene sequence for the PCV2 capsid protein that has a region of 33 amino acids that is identical to positions 150 to 183 of instant SEQ ID NO: 4, this reference only discloses a portion of the amino acid sequence of SEQ ID NO: 4 and thus does not recite "the amino acid sequence of SEQ ID NO: 4" as now recited in claim 14. The remaining citations of record also fail to disclose or suggest at least this feature.”
In response: As explained in detail above, a new rejection of amended claim 25 which combines the teachings of GenBank Accession number: AHX25876.1 and Luo is herein set forth. It is noted that the amino acid sequence in instant SEQ ID NO: 4 is a fusion protein of a known PCV2 capsid protein (see GenBank Accession number: AHX25876.1 published in 2014) and a well-known secretion signal peptide which derives from the HA of an influenza virus (see Luo). As evidenced by the cited prior art, both sequences have been known and widely used in the art. Accordingly, it is herein submitted that the entire length of instant SEQ IF NO: 4 has been previously reported and its combination represents an obvious embodiment of the cited teachings as explained above in detail.
Conclusion
No claims are allowed.
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.
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/MARLENE V BUCKMASTER/Examiner, Art Unit 1672
/THOMAS J. VISONE/ Supervisory Patent Examiner, Art Unit 1672
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