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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 6/12/2026 has been entered.
Claim Status
Claims 1-29 are pending.
Claims 1-13 are withdrawn from examination being part of the nonelected group.
Claims 14-29 are being examined.
All previous objections and rejections not set forth below are withdrawn herewith.
However, there is no amendment of any claim.
Claim Rejections - 35 USC § 103
Claims 14-29 remain rejected under 35 U.S.C. 103 as being unpatentable over Margolin et al. (Co-expression of human calreticulin significantly improves the production of HIV gp140 and other viral glycoproteins in plants, 2020, Plant Biotechnology Journal, 18:2109-2117) in view of Castilho et al. (An oligosaccharyltransferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana, 2018, Plant Biotechnology Journal, 16:1700–1709), Steinkellner et al. (US 20200080100 A1) and Gutternigg et al. (Biosynthesis of Truncated N-Linked Oligosaccharides Results from Non-orthologous Hexosaminidase-mediated Mechanisms in Nematodes, Plants, and Insects, 2021, J. of Biol. Chem., 282: 7825–27840) and in evidence of Keith et al. (Monocot and dicot pre-mRNAs are processed with different efficiencies in transgenic tobacco, 1986, The EMBO Journal, 5:2419 -2425). Applicant’s arguments.
Claim 14 is drawn to a plant cell which is transformed with at least one expression vector, comprising:
a first nucleic acid encoding a mammalian chaperone protein;
a second nucleic acid encoding a polypeptide which increases glycan occupancy;
a third nucleic acid which interferes with an enzyme which is responsible for the formation of truncated glycans in the plant cell; and
a fourth nucleic acid encoding a heterologous polypeptide of interest.
Margolin et al. teaches a promising approach for production of high yields of appropriately processed and cleaved mammalian viral glycoproteins (Abstract, last 3 lines) and, thus, improving the production of viral glycoprotein-based vaccines in plants (page 2114. Right column, para 1, last 2 lines) to be used in animals/mammals. Margolin et al. describes transforming Nicotiana benthamiana plants (Abstract, line 10) with at least one expression vector (page 2112, Fig. 2) comprising nucleic acids to efficiently produce heterologous glycoproteins (Abstract, line 9-10 and 14-15; page 2112, Fig. 2). It is understood by an ordinarily skilled artesian that transforming a plant implies transforming cells in the plant.
Margolin et al. describes that coexpression of the mammalian chaperone Calreticulin (CRT) (abstract, line 11), which reads on the “first nucleic acid”, as recited in the claim 14, helped in chaperone-mediated folding (page 2110, left column, para 1, last 4 lines) and enabled production of various appropriately processed and cleaved heterologous glycoproteins (Abstract, last 3 lines).
Margolin et al. describes that following translation, nascent glycoproteins translocate into the ER where an oligosaccharide precursor is transferred to the asparagine residue of the N-X-S/T sequon (where X is any amino acid other than proline) which is mediated by the oligosaccharyltransferase complex comprising the oligosaccharyltransferase (OST) enzyme (p2110, para 2, line 1-6). Margolin et al. teaches that oligosaccharyltransferase (OST) enzyme adds an oligosaccharide precursor to its polypeptide substrate (page 2110, left column, para 2, line 1-5), and, thus, increases glycan occupancy in its target or substrate polypeptide.
The polynucleotide sequences encoding viral glycoproteins (“polypeptide of interest”) comprising HIV gp140 (title; abstract, line 10 and 18), glycoproteins from Epstein-Barr virus (EBV), Rift Valley fever virus (RVFV), and chikungunya virus (CHIKV) (abstract, line 12-13) reads on the “fourth nucleic acid”, as recited in the instant claim 14. The plant cell is transformed with all the three polynucleotide sequences.
However, Margolin et al. does not explicitly describes any expression vector comprising the “second nucleic acid” encoding a polypeptide which increases glycan occupancy or the “third nucleic acid” which interferes with an enzyme which is responsible for the formation of truncated glycans in the plant cell.
Castilho et al. teaches that not all potential N-glycosylation sites are recognized in-vivo by various enzymes present in a specific cell and the site occupancy can vary in different expression systems, resulting in under-glycosylation of specific heterologous glycoproteins (abstract, line 4-6). A polynucleotide sequence, which reads on the “second nucleic acid” (as recited in the instant claim 14) encoding an oligosaccharyltransferase enzyme, LmSTT3D, from the protozoan Leishmania major (as recited in claims 17-18) have been expressed in Nicotiana benthamiana, to overcome that specific limitation of under-glycosylation (page 1700, abstract, line 4-8).
Steinkellner et al. describes reducing or abolishing plant specific N-glycan residues by using RNAi (page 6, para 0087) to silence or inhibit different beta-hexosaminidase genes (page 6, para 0086) in tobacco (Nicotiana benthamiana) plants (page 8, para 0107 and para 0108). It also teaches that inactivation of beta-hexosaminidase 3 (HEXO3) increases the amount of complex N-glycans in substrate polypeptides (page 6, para 0088). Beta-hexosaminidase 3 enzyme is responsible for formation of truncated glycans, and since the nucleic acid comprising the RNAi construct interferes with this enzyme, this nucleic acid comprising the RNAi construct reads on the “third nucleic acid” recited in claim 14. It is known in the art that hexosaminidases are responsible for producing truncated or paucimannosidic N-linked oligosaccharides in plants (Gutternigg et al., page 27825, right column, para 1, last 4 lines; page 27835, left column, last para; page 27839, left column, para 3, line 3-5), in contrast to mammalian and other vertebrate specific “complex N-glycans”.
Before the effective filing date of the invention, it would have been obvious to an ordinarily skilled artisan to express a nucleic acid encoding a mammalian chaperone protein, a nucleic acid encoding a polypeptide which increases glycan occupancy, and another nucleic acid encoding a heterologous polypeptide of interest, while co-expressing one more nucleic acid encoding an RNAi construct to silence hexosaminidase 3 (HEXO3) gene (which produces plant specific N-linked oligosaccharides in a glycoprotein) with a realistic goal to reduce or abolish plant specific N-glycan residues, as described by Steinkellner et al., in the heterologous glycoprotein(s) being expressed in the plant cell. Expressing these nucleotide sequences in a plant cell would have been obvious to an ordinarily skilled artisan with a reasonable expectation of success for production of appropriately processed and cleaved viral glycoproteins for development of viral glycoprotein-based vaccines in plants to be used as vaccines in animals.
Before the effective filing date, an ordinarily skilled artisan would have been motivated to express: (i) a nucleic acid encoding a mammalian chaperone protein in a plant cell along with (ii) a nucleic acid encoding a polypeptide which increases glycan occupancy, iii) a third nucleic acid encoding an RNAi construct to silence hexosaminidase 3 (HEXO3) gene and iv) another (forth) nucleic acid encoding a heterologous polypeptide of interest (the viral protein against which the vaccine needs to be raised), with reasonable expectation of success to reduce or abolish plant specific N-glycan residues in the heterologous glycoprotein intended to be used as a therapeutic agent including as a vaccine which is intended to be used vaccines in animals. It is noted here that the ordinarily skilled artisan would have acknowledged that the glycosylation pattern of the native viral or mammalian glycoprotein (the heterologous glycoprotein encoded by the “fourth nucleic acid”, as recited in instant claims 14 and 21) does not comprise plant specific glycosylation and/or would have altered biological function(s) including immunogenicity in a mammalian system due to plant specific glycosylation in a native plant that does not have the four nucleic acids being expressed.
Regarding claims 15-16, Margolin et al. describes human chaperones including calreticulin (title; abstract, line 9-11).
Regarding claim 17, Margolin et al. describes oligosaccharyltransferase complex which contains oligosaccharyltransferase enzyme that increases glycan occupancy, as discussed above (page 2110, left column, para 2).
Regarding claims 19-20, Steinkellner et al. describes use of different techniques including RNAi to reduce or abolish plant specific N-glycan residues (page 6, para 0087) by mutating or silencing specific genes including beta-hexosaminidase 3 (page 6, para 0088). Beta-hexosaminidase 3 enzyme is responsible for formation of truncated glycans, and since the nucleic acid comprising the RNAi construct interferes with this enzyme, this nucleic acid comprising the RNAi construct reads on the “third nucleic acid”, as discussed above.
Regarding claims 21-22, Margolin et al. describes expressing several heterologous glycoproteins in plants including viral glycoproteins (title; abstract, line 13-15).
Regarding claim 23, Margolin et al. describes expressing various nucleotide sequences using an expression vector pEAQ (Fig. 2). Clearly, there must be a promoter and other regulator(s) (e.g. transcription terminator sequence) operably linked to the nucleic acid sequences to express the nucleotide sequences, as described above, in the host plant cells.
Regarding claims 24-27 and 29, Margolin et al. describes transforming plant cells in tobacco, Nicotiana benthamiana, plants (page 2109, abstract), as described above. It is well known in the art that tobacco is dicotyledonous plant (Keith et al., Abstract).
Regarding claim 28, Steinkellner et al. describes N. benthamiana plants (page 8, para 0108) containing mutations to silence or inhibit glycosylation for plant specific N-glycan residues (page 6, para 0086; para 0087, line 1-6, line 18-20, line 25-29; and para 0088, line 6-11).
Response to Applicant’s Arguments:
The argument set forth in the Applicant’s replies on 6/12/2026 has been fully considered but is not found persuasive.
Regarding U.S.C. 103 rejections, the Applicant argues, “the Examiner has failed to establish a reasonable expectation of success for combining the teachings of Margolin and Steinkellner” (response, p.8, para 2, last 3 lines) as “the disclosures of Margolin and Steinkellner are directed to entirely different purposes” (response, p.7, para 3, line 4-5). The Applicant also argues, “the present inventors surprisingly discovered that integration of all four nucleic acid components reduces aggregation” (response, p.7, last para, first 2 lines).
To support the argument of “unexpected (synergistic) results” (response, p.9, last para, line 1), the Applicant asserts, “In order to produce well-folded and appropriately glycosylated complex glycoproteins, chaperone co-expression is necessary to support folding, glycan occupancy needs to be increased, and the activity of endogenous hexosaminidase enzymes needs to be mitigated to prevent formation of truncated (paucimannosidic) glycans” (response, p.8, para 2, line 4-7) and discussed Example 3 (response, p.8, para 3).
Regarding rejection of claim 18, the Applicant alleges, "the Examiner cites Castilho as allegedly disclosing the use of LmSTT3D to increase glycan occupancy. However, it would not have been obvious to combine the disclosure of Castilho with Margolin and/or Steinkellner” (response, p.9, para 3, last 3 lines) and “Castilho does not address the problem of protein aggregation or the need for chaperone co-expression to support proper folding” (response, p.9, para 4, last 2 lines).
The Examiner disagrees. Glycosylation in different viral and mammalian glycoproteins differ in its pattern of glycosylation. Margolin et al. produced specific glycoprotein, HIV gp140 (abstract) and taught that co-expression of mammalian chaperone (calreticulin, CRT) resulted in producing appropriately processed and cleaved the specific viral (HIV) glycoprotein (gp140), and solved the challenge of “expression yields and appropriate posttranslational modifications along the plant secretory pathway (which) remain(s) a challenge for certain proteins” (abstract, line 3-5).
It is noted here that, before the effective filing date of the invention, an ordinarily skilled artisan would have acknowledged that the glycosylation pattern of the native viral or mammalian glycoprotein (the heterologous glycoprotein encoded by the “fourth nucleic acid”, as recited in instant claims 14 and 21), does not comprise plant specific glycosylation and/or would have altered biological function(s) including immunogenicity in a mammalian system due to plant specific glycosylation observed in a native plant that does not have the four nucleic acids being expressed. Using any specific OST enzyme would depend on the target vaccine protein (i.e., the heterologous glycoprotein being expressed in a plant expression system) that need specific glycosylation pattern to invoke specific immunogenic response in the target animal/mammalian system for which the vaccine is being developed.
Example 3, as discussed by the Applicant in its response, expressed all three polynucleotide sequences (as described by the 103 rejections above) to observe reduced aggregation. The alleged (increased) aggregation occurred for under-glycosylated proteins (spec, p.14, last para, line 7-9), apparently when the Applicant did not express the second nucleic acid encoding a polypeptide (OST) which increases glycan occupancy. The Applicant does not provide any evidence to support its opinion regarding reduction in aggregation (as described in examples of this invention) by comparing similar situations in the prior art. The claims are not limited to any specific glycosylation state of the target polypeptide of interest. Thus, the result of the invention is neither unexpired nor surprising, as the Applicant alleges.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 14-18, 21, 23-26 and 29 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claim 6-7 and 10-14 of U.S. Patent No. 11555196B2, in view of Margolin et al. (Co-expression of human calreticulin significantly improves the production of HIV gp140 and other viral glycoproteins in plants, 2020, Plant Biotechnology Journal, 18:2109–2117), Castilho et al. (An oligosaccharyltransferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana, 2018, Plant Biotechnology Journal, 16:1700–1709) and Steinkellner et al. (US 20200080100 A1).
Instant claim 14 is drawn to a plant cell which is transformed with at least one expression vector, comprising:
a first nucleic acid encoding a mammalian chaperone protein;
a second nucleic acid encoding a polypeptide which increases glycan occupancy;
a third nucleic acid which interferes with an enzyme which is responsible for the formation of truncated glycans in the plant cell; and
a fourth nucleic acid encoding a heterologous polypeptide of interest.
Claim 6 of U.S. Patent No. 11555196B2 (hereafter referred to as ‘196B2) recites a plant cell which is transformed with at least one expression vector, comprising:
a first nucleic acid encoding a mammalian chaperone protein; and
a second nucleic acid encoding a heterologous polypeptide of interest,
wherein the mammalian chaperone protein is selected from calnexin and/or calreticulin.
Claim 7 of ‘196B depends from claim 6, wherein the heterologous polypeptide of interest is a glycoprotein. Thus, claim 6-7 of recite the “first” and the “forth” nucleic acid of instant claims 14 and 21.
However, claims 6-7 of ‘196B2 do not recite any nucleic acid (the “third nucleic acid” of instant claim 14 of ‘1986B) which interferes with an enzyme which is responsible for the formation of truncated glycans in the plant cell. The claims also do not recite any nucleic acid (the “second nucleic acid” of instant claim 14 of ‘1986B) encoding a polypeptide which increases glycan occupancy.
Margolin et al. describes a promising approach for production of high yields of appropriately processed and cleaved viral glycoproteins (page 2109, Abstract) to improve production of viral glycoprotein-based vaccines in plants (page 2114. right column, para 1, last 2 lines). Margolin et al. describes oligosaccharyltransferase complex adding oligosaccharide precursors to its substrate glycoproteins (page 2110, left column, para 2, line 1-5), and, thus, increases glycan occupancy in the glycoprotein.
Castilho et al. teaches that not all potential N-glycosylation sites are recognized in-vivo by various enzymes present in a specific cell and the site occupancy can vary in different expression systems, resulting in under-glycosylation of specific heterologous glycoproteins (abstract, line 4-6). A polynucleotide sequence, which reads on the “second nucleic acid” (as recited in the instant claim 14) encoding an oligosaccharyltransferase enzyme, LmSTT3D, from the protozoan Leishmania major (as recited in claims 17-18) have been expressed in Nicotiana benthamiana, to overcome that specific limitation of under-glycosylation (page 1700, abstract, line 4-8).
Steinkellner et al. describes plant and plant cells (page 1, para 0001) with mutated, silenced, or inhibited beta-hexosaminidases (page 6, para 0086) to reduce or abolish plant specific N-glycan residues using RNAi (page 6, para 0087). It also describes that inactivation of beta-hexosaminidase 3 increases the amount of (mammal specific) complex N-glycans in the glycoproteins (page 6, para 0088). It is known in the art that hexosaminidases are responsible for producing plant specific truncated or paucimannosidic N-linked oligosaccharides, as described above. The nucleic acid sequences encoding RNAi constructs targeting beta-hexosaminidase enzymes including beta-hexosaminidase 3 (HEXO3) reads on the third nucleic acid sequence, as recited in claim 14. Therefore, beta-hexosaminidase 3 enzyme is the enzyme that is responsible for the formation of truncated glycans, and since the nucleic acid comprising the RNAi construct interferes with this enzyme, this nucleic acid comprising the RNAi construct reads on the “third nucleic acid” recited in instant claim 14.
Before the effective filing date of the invention, it would have been obvious to an ordinarily skilled artisan to modify the method described by claims 6-7 of ‘196B2 and express: (i) a nucleic acid encoding a mammalian chaperone protein, (ii) a nucleic acid encoding a heterologous glycoprotein of interest, as recited by claims 6-7 of ‘196B2; and co-expressing (i)-(ii), with (iii) one more nucleic acid encoding the oligosaccharyl-transferase enzyme to increases glycan occupancy in its target glycoprotein(s), as described by Castilho et al. and Margolin et al., and (iv) a nucleic acid to silence hexosaminidase gene(s), with a realistic goal to reduce or abolish plant specific N-glycan residues in the heterologous glycoprotein(s), as described by Steinkellner et al. Expressing these 4 nucleotide sequences in a plant cell would have been a promising approach (“obvious to try”) with a reasonable expectation of success for the production of appropriately processed and cleaved viral glycoproteins for producing viral glycoprotein-based vaccines in plants to be used in animals/mammals.
Before the effective filing date, an ordinarily skilled artisan would have been motivated to express:
(i) a nucleic acid encoding a mammalian chaperone protein in a plant cell,
(ii) a nucleic acid encoding a heterologous glycoprotein of interest,
(iii) a nucleic acid to silence hexosaminidase gene(s) with the realistic goal to reduce or abolish plant specific N-glycan residues in the heterologous glycoprotein, and
(iv) one more nucleic acid encoding the oligosaccharyltransferase enzyme would increases glycan occupancy in its target glycoprotein, to produce of appropriately processed and cleaved viral glycoproteins for development of viral glycoprotein-based vaccines in plants.
It is noted here that the ordinarily skilled artisan would acknowledge that the glycosylation pattern of the native viral or mammalian glycoprotein (the heterologous glycoprotein encoded by the “fourth nucleic acid”, as recited in instant claims 14 and 21) does not comprise plant specific glycosylation and/or would have alerted biological function(s) including immunogenicity in a mammalian system due to plant specific glycosylation in a native plant that does not have the four nucleic acids being expressed.
Regarding instant claims 15-16, claim 6 of ‘196B2 recites “calnexin and/or calreticulin”.
Regarding instant claim 21, claim 7 of ‘196B2 recites, “the heterologous polypeptide of interest is a glycoprotein”.
Regarding instant claim 23, claim 10 of ‘196B2 recites, “at least one expression vector includes promoters and/or other regulators, operably linked to the first nucleic acid and to the second nucleic acid”. It is well known and widely practiced to operably link several nucleic acid sequences, including the 4 nucleotide sequences described above to reject instant claim 14, with a promoter in expression vector(s) to express it in the host plant.
Regarding instant claim 24, claim 11 of ‘196B2 recites, “the plant cell is from a monocotyledonous or dicotyledonous plant”.
Regarding instant claim 25, claim 12 of ‘196B2 recites, “maize, rice, sorghum, wheat, cassava, barley, oats, rye, sweet potato, soybean, alfalfa, tobacco, sunflower, cotton, and canola”.
Regarding instant claim 26, claim 13 of ‘196B2 recites, “the plant cell is from a tobacco plant”.
Regarding instant claim 29, claim 14 of ‘196B2 recites, “A plant comprising the plant cell of claim 6.”
Response to Applicant’s Arguments:
Regarding Double Patenting rejection, the Applicant argues, “the present claims are patentably distinct from the claims of the '196 patent for at least the same reasons set forth above” (response, p.10, para 4, line 1-2) including “there is no reasonable expectation of success for combining the teachings of the '196 patent with Steinkellner and Margolin to arrive at the claimed combination. Margolin and Steinkellner are directed to entirely different purposes” (response, p.10, para 6, line 1-3). The applicant also alleges, “the specification demonstrates unexpected synergistic results when all components are combined… resulting in an antigen comparable to mammalian cell-produced protein (response, p.11, para 2, line 1-7)
The Examiner disagrees. Claims 6-7 of U.S. Patent No. 11555196B2 recites a heterologous glycoprotein being co-expressed with a mammalian chaperone comprising calnexin and/or calreticulin. An ordinarily skilled artisan would have known that many viral/mammalian glycoproteins having a different glycosylation pattern would not respond similarly to the methods of Margolin et al. and/or Steinkellner et al. Steinkellner et al. did not express gp140 glycoprotein but expressed specific “therapeutically interesting (glyco) proteins” (page 10, para 0134, line 1), for which silencing endogenous beta-hexosaminidase genes (page 6, para 0086) using methods including RNAi (page 6, para 0087) were accomplished in tobacco plants, as discussed above. Silencing of any beta-hexosaminidase gene was not needed for successful production of biologically active gp140 glycoprotein, as described by Margolin et al.
The result of the invention, as claimed, is neither surprising nor unexpected, as discussed above in response to Applicant’s arguments regarding 103 rejections.
Conclusion
No claim is allowed.
Communication
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JAY CHATTERJEE whose telephone number is (703)756-1329. The examiner can normally be reached (Mon - Fri) 8.30 am to 5.30 pm..
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, Bratislav Stankovic can be reached at (571) 270-0305. 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.
Jay Chatterjee
Patent Examiner
Art Unit 1662
/Jay Chatterjee/Examiner, Art Unit 1662
/BRATISLAV STANKOVIC/ Supervisory Patent Examiner, Art Units 1661 & 1662
Prosecution Insights