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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 02/11/2026 has been entered.
Withdrawal of Rejections
The response and amendments filed on 02/11/2026 are acknowledged. Any previously applied minor objections and/or minor rejections (i.e., formal matters), not explicitly restated here for brevity, have been withdrawn necessitated by Applicant’s formality correction and/or amendments. For the purposes of clarity of the record, the reasons for the Examiner’s withdrawal, and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner’s Response to Arguments section.
Briefly, the previous rejections under 35 U.S.C. 103 for obviousness have been withdrawn; however, new grounds of rejection are set forth below.
The following rejections and/or objections are either reiterated or newly applied. They constitute the complete set presently being applied to the instant application.
Claim Rejections - 35 USC § 103, Obviousness
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-4, 6-10, and 22-25 are rejected under 35 U.S.C. 103 as being unpatentable over Gao (Stepwise metabolic engineering of Gluconobacter oxydans WSH-003 for the direct production of 2-keto-L-gulonic acid from D-sorbitol; 2014 – previously cited) in view of Hoshino (WO 2005/075658; Date of Publication: August 18, 2005 – previously cited), Kim (A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilization; 2016 – newly cited), and Yodice (WO 1987/000839; Date of Publication: February 12, 1987 – previously cited).
Gao’s general disclosure relates to a one-step fermentation process for vitamin C production by expressing L-sorbose dehydrogenases and L-sorbosone dehydrogenases from Ketogulonicigenium vulgare in Gluconobacter oxydans (see, e.g., Gao, abstract). Gao discloses that a one-step production method for producing 2-keto-gulonic acid through expression of dehydrogenases within a single bacterial strain results in improvement in the production of 2-keto-gulonic acid, compared to independent expression of the dehydrogenases (see, e.g., Gao, abstract). Moreover, Gao discloses that these methods pave the way for one-step industrial-scale production of vitamin C (see, e.g., Gao, abstract).
Regarding claims 1-4 and 23 pertaining to synthesizing L-ascorbic acid, Gao teaches Gluconobacter oxydans as a host cell (see, e.g., Gao, abstract), wherein G. oxydans is an industrial strain used for the conversion of D-sorbitol to L-sorbose (see, e.g., Gao, abstract). Moreover, polyol dehydrogenase is responsible for the conversion of D-sorbitol to L-sorbose (see, e.g., Gao, abstract); therefore, since G. oxydans is used for conversion of D-sorbitol to L-sorbose, then G. oxydans inherently has and expresses a polyol dehydrogenase. Furthermore, Gao teaches that the conversion of D-sorbitol to L-sorbose is performed by sorbitol dehydrogenase (see, e.g., Gao, Introduction, pg. 30). Sorbitol dehydrogenase is the same as polyol dehydrogenase and expressed by the SldBA gene (see, e.g., Art of Record, Shinjoh). Furthermore, Gao teaches expression of sorbose dehydrogenase, KVU_2142, and sorbosone dehydrogenase, KVU_0095, from K. vulgare within G. oxydans (see, e.g., Gao, “Overexpression of SDH and SNDH in G. oxydans WSH-003”, pg. 31). Moreover, KVU_2142 and KVU_0095 are inherently expressed in Ketogulonicigenium vulgare and expression of sorbose dehydrogenase and sorbosone dehydrogenase would inherently lead to production of 2-keto-gulonic acid. Therefore, Gao is isolating sorbose dehydrogenase, KVU_2142, and sorbosone dehydrogenase, KVU_0095, from K. vulgare and expressing these genes in G. oxydans (see, e.g., Gao, “Overexpression of SDH and SNDH in G. oxydans WSH-003”, pg. 31), wherein G. oxydans inherently expresses a polyol dehydrogenase. Therefore, based on the teachings of Gao, the polyol dehydrogenase, sorbose dehydrogenase, and sorbosone dehydrogenase are expressed by a single, engineered bacterial strain. Furthermore, Gao teaches “Batch fermentation was performed in a 3-L bioreactor (BioFlo 115, New Brunswick Scientific Co., Edison, NJ), and the temperature of the reactor was maintained at 30 1C, the agitation speed was controlled at 400 rpm, and the aeration rate was 1.5 vvm” (see, e.g., Gao, Section 2.2, pg. 31). Additionally, Gao teaches “D-sorbitol, 2-KLG, and intermediate metabolites in the fermentation broth were determined by high performance liquid chromatography” (see, e.g., Gao, Section 2.7, pg. 32). Gao teaches “The time course of D-sorbitol oxidation by G. oxydans/pGUC-k0203–k0095 revealed that 4.9 g/L of 2-KLG was accumulated after 72 h of fermentation (Fig. 5)” (see, e.g., Gao, Section 3.3, pg. 32). Therefore, based on the teachings of Gao, the G. oxydans strain expressing sorbose dehydrogenase, KVU_2142, and sorbosone dehydrogenase, KVU_0095, from K. vulgare, as well as inherently expressing its polyol dehydrogenase, was grown in a single batch fermenter.
However, Gao does not teach: wherein the engineered bacterial strain is an engineered Ketogulonicigenium sp. strain (claim 1, step (b)); or the conversion of the 2-keto-gulonic acid to L-ascorbic acid (vitamin C) (claims 1 and 23, step (c)); or isolation of said L-ascorbic acid (vitamin C) synthesized in the method (claim 1, step (d)); or wherein the engineered bacterial strain is an engineered Ketogulonicigenium vulgare strain (claim 6 and 24-25); or wherein said engineered bacterial strain is a Ketogulonicigenium vulgare strain naturally expressing the sorbose dehydrogenase and sorbosone dehydrogenase and engineered to express the polyol dehydrogenase, wherein said polyol dehydrogenase is a heterologous polyol dehydrogenase (claim 7); or wherein the conversion step (c) is carried out in the same fermentation vessel as steps (a)-(b) (claim 10).
Hoshino’s general disclosure relates to the production of vitamin C from L-sorbosone using a microorganism belonging to the genius Ketogulonicigenium (see, e.g., Hoshino, abstract). Moreover, Hoshino discloses a process for producing vitamin C from L-sorbosone by contacting K. vulgare with L-sorbosone, and isolating and purifying vitamin C from the reaction mixture (see, e.g., Hoshino, pg. 2, lines 16-20). Hoshino discloses that the invention is performed to reduce the number of steps necessary for production of vitamin C from L-sorbosone (see, e.g., Hoshino, pg. 4, lines 32-34). Furthermore, Hoshino discloses “Conversion of the substrate into vitamin C means that the conversion of the substrate resulting in vitamin C is performed by the microorganism belonging to the genus Ketogulonicigenium, i.e. the substrate may be directly converted into vitamin C. Said microorganism is cultured under conditions which allow such conversion from the substrate as defined above, e.g. directly contacting the microorganism with the substrate” (see, e.g., Hoshino, pg. 1, lines 13-17).
Regarding claims 1, 6-7, and 24-25 pertaining to the Ketogulonicigenium sp. strain, Hoshino teaches that the microorganism is Ketogulonicigenium vulgare which can be used to produce vitamin C from L-sorbosone (see, e.g., Hoshino, abstract & pg. 2, line 14). Moreover, Hoshino teaches that the microorganism is Ketogulonicigenium vulgare (see, e.g., Hoshino, pg. 2, line 14), which inherently expresses sorbose dehydrogenase and sorbosone dehydrogenase. Therefore, one of ordinary skill in the art would readily understand that using K. vulgare as the bacterial strain would result in inherent expression of sorbose dehydrogenase and sorbosone dehydrogenase.
Regarding claims 1 and 23 pertaining to isolation of L-ascorbic acid, Hoshino teaches isolating and purifying vitamin C from the reaction mixture (see, e.g., Hoshino, pg. 2, lines 16-20 & Example 1).
Kim’s general disclosure relates to “A sorbitol dehydrogenase (GoSLDH) from Gluconobacter oxydans G624 (G. oxydans G624) was expressed in Escherichia coli BL21(DE3)-CodonPlus RIL” (see, e.g., Kim, abstract). Moreover, Kim discloses “GoSLDH exhibited Km and kcat values of 38.9 mM and 3820 s−1 toward L-sorbitol, respectively. The enzyme exhibited high preference for NADP+ (vs. only 2.5% relative activity with NAD+). GoSLDH sequencing, structure analyses, and biochemical studies, suggested that it belongs to the NADP+-dependent polyol-specific long-chain sorbitol dehydrogenase family. GoSLDH is the first fully characterized SLDH to date, and it is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry showed that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirmed a higher turnover rate. The high oxidation potential of GoSLDH for D-sorbitol was confirmed by cyclovoltametric analysis. Further, stability of GoSLDH significantly improved (up to 13.6-fold) after cross-linking of immobilized enzyme on silica nanoparticles and retained 62.8% residual activity after 10 cycles of reuse. Therefore, immobilized GoSLDH may be useful for L-sorbose production from D-sorbitol” (see, e.g., Kim, abstract).
Regarding claims 1 and 7-8 regarding isolating SldBA from G. oxydans and expression in a heterologous host cell, Kim teaches that “A sorbitol dehydrogenase (GoSLDH) from Gluconobacter oxydans G624 (G. oxydans G624) was expressed in Escherichia coli BL21(DE3)-CodonPlus RIL” (see, e.g., Kim, abstract). Therefore, Kim teaches isolation of SldBA from G. oxydans, and subsequent cloning and expression of this gene in a heterologous host cell.
Yodice’s general disclosure relates to a method of producing L-ascorbic acid by converting 2-keto-gulonic acid to L-ascorbic acid by acid catalysis of 2-keto-L-gulonic acid under substantially anhydrous conditions (see, e.g., Yodice, abstract). Moreover, Yodice discloses that this conversion process for production of L-ascorbic acid from 2-keto-gulonic acid substantially decreases the reaction time and substantially increases the total yield of L-ascorbic acid (see, e.g., Yodice, pg. 2, paragraph 2).
Regarding claims 1, 10, and 23 pertaining to conversion of 2-keto-gulonic acid to L-ascorbic acid, Yodice teaches the production of L-ascorbic acid from 2-keto-gulonic acid by acid catalysis under anhydrous conditions (see, e.g., Yodice, abstract). Therefore, one of ordinary skill in the art would understand that expression of 2-keto-gulonic acid by the engineered host cell would result in L-ascorbic acid production by acid catalysis under anhydrous conditions.
Regarding claim 22 regarding hydrous conditions, Yodice teaches substantially anhydrous conditions, which one of ordinary skill in the art recognizes that the conditions contain minimal water (i.e., hydrous conditions). Furthermore, Yodice teaches conditions which involve the presence of minimal water, wherein Yodice teaches “the reaction will proceed well with very small amount of water present such as water due to processing conditions” (see, e.g., Yodice, “Description of the Preferred Embodiments”, pg. 3). Additionally, Yodice teaches that the method uses a hydrate of 2-keto-l-gluconic acid (see, e.g., Yodice, Summary of the Invention, pgs. 2-3).
It would have been first obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to express a polyol dehydrogenase, encoded by the SldBA gene, obtained from G. oxydans, as taught by Gao and Kim, within K. vulgare, which in inherently expresses sorbose dehydrogenase and sorbosone dehydrogenase, as taught by Hoshino. One would have been motivated to do so because Hoshino teaches that K. vulgare can be used as a microorganism to produce vitamin C from D-sorbitol, L-sorbose, or L-sorbosone (see, e.g., Hoshino, pg. 2, lines 7-8). Moreover, Gao teaches that engineered bacterial strains to express polyol dehydrogenase, sorbose dehydrogenase, and sorbosone dehydrogenase results in an efficient one-step fermentation process for the production of 2-keto-L-gulonic acid (see, e.g., Gao, Introduction, pg. 31 & Discussion, pg. 35). Furthermore, Gao teaches that a one-step production method for producing 2-keto-gulonic acid through expression of dehydrogenases within a single bacterial strain results in improvement in the production of 2-keto-gulonic acid, compared to independent expression of the dehydrogenases (see, e.g., Gao, abstract). Moreover, Kim teaches that the polyol dehydrogenase isolated from G. oxydans “exhibited Km and kcat values of 38.9 mM and 3820 s−1 toward L-sorbitol, respectively. The enzyme exhibited high preference for NADP+ (vs. only 2.5% relative activity with NAD+). GoSLDH sequencing, structure analyses, and biochemical studies, suggested that it belongs to the NADP+-dependent polyol-specific long-chain sorbitol dehydrogenase family. GoSLDH is the first fully characterized SLDH to date, and it is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry showed that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirmed a higher turnover rate. The high oxidation potential of GoSLDH for D-sorbitol was confirmed by cyclovoltametric analysis. Further, stability of GoSLDH significantly improved (up to 13.6-fold) after cross-linking of immobilized enzyme on silica nanoparticles and retained 62.8% residual activity after 10 cycles of reuse. Therefore, immobilized GoSLDH may be useful for L-sorbose production from D-sorbitol” (see, e.g., Kim, abstract). Additionally, Kim teaches “recombinant GoSLDH is more catalytically efficient than other SLDH or MDH due to the close proximity of D-sorbitol to the catalytic residue, along with high binding affinity” (see, e.g., Kim, “Conclusions”, pg. 7). Furthermore, Kim teaches that it is possible to isolate SldBA from G. oxydans, and clone and express this gene in a heterologous organism for expression (see, e.g., Kim, Materials and Methods, pg. 7 & abstract). Therefore, based on the teachings of Gao, Hoshino, and Kim, it would have been obvious to produce an engineered K. vulgare strain that expresses polyol dehydrogenase from G. oxydans, as well as inherently expresses sorbose dehydrogenase and sorbosone dehydrogenase, in order to produce 2-keto-L-gulonic acid in a one-step fermentation process. One would have expected success because Gao, Hoshino, and Kim both teach pathways for vitamin C production and 2-keto-gluonic acid.
It would have been secondly obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine Gao’s one-step production of 2-keto-gluonic acid in a single fermentation vessel with Yodice’s method of producing L-ascorbic acid from 2-keto-gluconic acid. One would have been motivated to do so because Yodice teaches that L-ascorbic acid can be produced from 2-keto-gluonic acid under anhydrous conditions (see, e.g., Yodice, abstract). Furthermore, Yodice discloses that this conversion process for production of L-ascorbic acid from 2-keto-gulonic acid substantially decreases the reaction time and substantially increases the total yield of L-ascorbic acid (see, e.g., Yodice, pg. 2, paragraph 2). Moreover, Gao teaches that the one-step fermentation process of producing of 2-keto-gluonic acid in a single fermentation vessel allows for “final one-step industrial-scale production of vitamin C” (see, e.g., Gao, abstract). Therefore, based on the teachings of Gao and Yodice, it would have been obvious to produce vitamin C from 2-keto-gluonic acid, following a one-step fermentation process of producing the 2-keto-gluonic acid, because this would allow for one-step industrial-scale production of vitamin C. One would have expected success because Gao and Yodice both teach vitamin C production and 2-keto-gluonic acid.
Examiner’s Response to Arguments
Applicant's arguments filed 02/04/2026 have been fully considered but they are not persuasive.
Regarding Applicant’s arguments that Gao teaches the opposite of the present invention, as well as Yodice and Hoshino not teaching an engineered G. oxydans strain (remarks, page 10), this argument is not persuasive for multiple reasons:
First, Applicant states that their invention is the opposite of what Gao teaches; however, it would be obvious to one of ordinary skill in the art to merely take the prior art teachings of Gao and perform the opposite of it (see, e.g., MPEP 2143(I)(D,E)).
Secondly, Hoshino was cited as prior art to teach that K. vulgare can be used to produce vitamin C from L-sorbosone (see, e.g., Hoshino, abstract & pg. 2, line 14). Moreover, Hoshino teaches that the microorganism is Ketogulonicigenium vulgare (see, e.g., Hoshino, pg. 2, line 14), which inherently expresses sorbose dehydrogenase and sorbosone dehydrogenase. Moreover, Hoshino teaches that K. vulgare can be used as a microorganism to produce vitamin C from D-sorbitol, L-sorbose, or L-sorbosone (see, e.g., Hoshino, pg. 2, lines 7-8). Therefore, Hoshino was used as prior art to teach K. vulgare as a host cell, wherein K. vulgare already inherently expresses sorbose dehydrogenase and sorbosone dehydrogenase for production of 2-keto-gulonic acid. Hoshino was not used as prior art to teach G. oxydans because Gao was used to teach these limitations.
Thirdly, Yodice was cited as prior art to teach a method of producing L-ascorbic acid by converting 2-keto-gulonic acid to L-ascorbic acid by acid catalysis of 2-keto-L-gulonic acid under substantially anhydrous conditions (see, e.g., Yodice, abstract). Therefore, Yodice was used as prior art to merely teach production of vitamin C from 2-keto-gulonic acid under substantially anhydrous conditions. Yodice was not used as prior art to teach G. oxydans because Gao was used to teach these limitations.
Fourthly, regarding Applicant’s individual arguments pertaining to Hoshino and Yodice, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). As discussed above, Gao was used to teach the limitations regarding to G. oxydans, while Hoshino was used to teach the limitations pertaining to K. vulgare, and Yodice was used to teach the limitations pertaining to conversion of 2-keto-gulonic acid to vitamin C. Moreover, Gao, Hoshino, and Yodice are all analogous art because they all teach the same pathway for production of vitamin C, wherein this pathway involves oxidation of D-sorbitol to L-sorbose, followed by oxidation of L-sorbose to 2-keto-gulonic acid, followed by conversion of 2-keto-gulonic acid to vitamin C.
Fifthly, the newly cited art of Kim was cited as motivation of one of ordinary skill in the art to isolate SldBA from G. oxydans and express this in a heterologous microorganism for expression of a polyol dehydrogenase for the process of vitamin C production. Kim teaches “A sorbitol dehydrogenase (GoSLDH) from Gluconobacter oxydans G624 (G. oxydans G624) was expressed in Escherichia coli BL21(DE3)-CodonPlus RIL” (see, e.g., Kim, abstract). Moreover, Kim discloses “GoSLDH exhibited Km and kcat values of 38.9 mM and 3820 s−1 toward L-sorbitol, respectively. The enzyme exhibited high preference for NADP+ (vs. only 2.5% relative activity with NAD+). GoSLDH sequencing, structure analyses, and biochemical studies, suggested that it belongs to the NADP+-dependent polyol-specific long-chain sorbitol dehydrogenase family. GoSLDH is the first fully characterized SLDH to date, and it is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry showed that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirmed a higher turnover rate. The high oxidation potential of GoSLDH for D-sorbitol was confirmed by cyclovoltametric analysis. Further, stability of GoSLDH significantly improved (up to 13.6-fold) after cross-linking of immobilized enzyme on silica nanoparticles and retained 62.8% residual activity after 10 cycles of reuse. Therefore, immobilized GoSLDH may be useful for L-sorbose production from D-sorbitol” (see, e.g., Kim, abstract). Therefore, Kim teaches that it is possible to isolate and clone SldBA from G. oxydans into a heterologous microorganism, as well as teaches that the polyol dehydrogenase isolated from G. oxydans has high activity and substrate specificity. This is motivation for one of ordinary skill in the art to isolate a polyol dehydrogenase from G. oxydans and express it in a heterologous microorganism.
Regarding Applicant’s argument that Gao teaches alterations will lead to loss of enzyme function or expression failure (remarks, page 10), this argument is not persuasive because it pertains to the production and expression of fusion proteins, which has nothing to do with the claimed invention. Moreover, Gao’s discussion of fusion proteins in the Discussion section pertains to improving the catalytic efficiency of enzymes by integrating different catalytic domains, thereby strengthening the enzyme spatial proximity (see, e.g., Gao, Discussion, pg. 35). This discussion by Gao does not pertain to the instantly claimed invention.
Regarding Applicant’s argument pertaining to unexpected beneficial result (remarks, page 10), this argument is not persuasive because these results are not commensurate in scope with the claimed invention. Applicant is relying on methods (see, e.g., Instant Specification, Examples 1-2) involving amplification of the sldBA gene from G. oxydans along with the 5’-UTR by PCR using a Phusion DNA polymerase, followed by cloning the amplicon into a pBBR1 p452 plasmid to create pSldBA and transformation of the plasmid into E. coli S17-1 by electroporation. Applicant is relying on growing the cultures of K. vulgare and E. coli in lysogeny broth, followed by plating them on agar containing 4% or 5% NaCl and 50 µg/mL kanamycin. Applicant is relying on testing for positive K. vulgare transformants by PCR, followed by growth on D-sorbitol, followed by quantification of vitamin C (see, e.g., Instant Specification, Example 1). Moreover, Applicant is relying on growing transformed K. vulgare on medium containing 20 g/L of either sorbitol or sorbose, growing batch cultures for 48 h at 28-30oC and shaking at 250 rpm. Furthermore, Applicant is relying on conversion of 2-keto-L-gulonic acid to ascorbic acid by adding 8M HCL in a 1:3 (v/v) ratio within the fermentation broth, followed by heating the mixture for 30 min at 90oC (see, e.g., Instant Specification, Example 2). These conditions that result in the stated unexpected beneficial results are not part of the claimed invention; therefore, these results are not commensurate in scope with the claimed invention.
Regarding Applicant’s argument pertaining to the teaching of Yodice (remarks, page 10), this argument is not persuasive for multiple reasons. First, Yodice teaches a method of producing L-ascorbic acid by converting 2-keto-gulonic acid to L-ascorbic acid by acid catalysis of 2-keto-L-gulonic acid under substantially anhydrous conditions (see, e.g., Yodice, abstract). Based on the teaching of Yodice, one of ordinary skill in the art would recognize that the conditions contain minimal water (i.e., hydrous conditions). Furthermore, Yodice teaches conditions which involve the presence of minimal water, wherein Yodice teaches “the reaction will proceed well with very small amount of water present such as water due to processing conditions” (see, e.g., Yodice, “Description of the Preferred Embodiments”, pg. 3). Secondly, Applicant’s argument that Yodice teaches “increasing the amount of free water increases the reaction time and/or decreases yield” (see, e.g., Yodice, page 3), this would result in an enablement issue for the present invention since the present invention claims that the method would take place under hydrous conditions, and based on the teachings of Yodice, this would result in increased time and/or decreased yield of vitamin C, which is undesirable.
Conclusion
Claims 1-4, 6-10, and 22-25 are rejected.
No claims are allowed.
Art of Record
Shinjoh M, Tomiyama N, Miyazaki T, Hoshino T. Main polyol dehydrogenase of Gluconobacter suboxydans IFO 3255, membrane-bound D-sorbitol dehydrogenase, that needs product of upstream gene, sldB, for activity. Biosci Biotechnol Biochem. 2002 Nov;66(11):2314-22. doi: 10.1271/bbb.66.2314. PMID: 12506966.
Correspondence Information
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/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653