DETAILED ACTION
Applicant's submission filed on September 5, 2025 has been entered.
Claims 1-20, 23-24, 26-29, 31-59, 61-63, 65-172, 174-227 and 229-243 are cancelled.
Claim 21 is currently amended.
Claim 22 is withdrawn.
Claims 21-22, 25, 30, 60, 64, 173 and 228 are pending.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
All previous objections and rejections not set forth below have been withdrawn.
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 .
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 21, 25, 30, 60, 64, 173 and 228 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The claims as currently amended are drawn to methods for protecting any type of plant from any type of pathogen comprising applying a free enzyme to a plant growth medium,
In contrast the specification does not describe the application of a phospholipase, a lipase, a lactonase, a chitosanase, an ACC deaminase, or combinations of any thereof to any type of plant growth medium, plant, or area surrounding a plant, wherein the plant exhibits decreased susceptibility to a pathogen as compared to a plant grown in the absence of the free enzyme under the same conditions.
At the time of filing it was understood in the art that the effect of applying an enzyme to a plant growth medium or a plant on the susceptibility of a plant to a plant pathogen is unpredictable, because multiple variables could impact the enzyme’s activity.
See, for example, Rosas Gajardo et al., U.S. Patent Application Publication No. 2016/0326068, published Nov. 10, 2016, who teach that the enzyme activity of acid phosphatase varies depending on the manner in which it is added to soil (paragraph [0013]). Rosas Gajardo et al. teach that one of the first studies on the addition of enzymes to soils to accelerate mineralization processes was carried out by Neumann et al. (1999), who showed that adding the enzyme acid phosphatase to soils in order to accelerate the mineralization of organic phosphorous (P) led to a low liberation of P from the organic fraction because the activity of the enzyme was significantly reduced due to denaturation, suggesting that the strategy of using enzymes for accelerated mineralization can only be effective if the enzyme is active and immobilized in a support. Rosas Gajardo et al. also teach that studies have been carried out on the artificial immobilization of acid phosphatase and arylsulfatase using supports such as humic substances, 2:1 clays, and Al and Mn oxides, and that, in these cases, enzymatic activity decreased because certain supports acted as enzymatic inhibitors or lost protein during the artificial immobilization process of the enzymes, according to results obtained by Rao & Gianfreda, 2000; Kelleher et al., 2004; Whalen & Warman, 1996b. In contrast, the immobilization of the acid phosphatase in clay minerals from an Andisol increased the specific activity of the enzyme by 89% to 144%, and did not lead to a loss of protein, according to results obtained by Rosas et al. (2008), López and Rosas (2008), and Rao & Gianfreda, 2000. Rosas Gajardo et al. additionally teach that the addition of immobilized phosphatase to soils was determined by Pant and Warman (2000) to increase the available phosphorus (extracted with water and NaOH) by 49%, and that an increase in available P (Olsen P) of up to 150% with acid phosphatase immobilized in Andisol clays and very low levels of enzymatic protein was reported by López and Rosas (2008).
See also, for example, Lessl et al., U.S. Patent Application Publication No. 2016/0340658, published Nov. 24, 2016, who teach that phytase enzymes obtained from different organisms exhibit different activities in the presence of soil (paragraphs [0149]-[0152]). Lessl et al. teach that while phytase obtained from Pteris vittate(PV) was not significantly impacted after mixing with soils, retaining 94, 93, and 98% of their activities in Soil 1, 2 and 3, respectively, phytase obtained from Pteris ensiformis (PE) and wheat retained only about 6% activity in all soils after 2 h. Lessl et al. also teach that after 6 h, PV phytase activity declined 25%, where it was stable through 24 h, and that PV phytase extracts mixed in the three soils, which retained 77, 86, and 97% of the control activity between 6 and 24 h for soil 1, 2 and 3 respectively. Lessl et al. additionally teach that while in previous soil studies logarithmic decline of phytase activity was typically observed within minutes of soil addition, the PV phytase extracts of Lessl et al. retained about 64% of their original activity following 24 h of mixing, which mirrored the decline in activity in the soil-less control. Lessl et al. further teach that while soils with greater clay content, organic matter and cation/anion exchange capacity are known to more rapidly inhibit phytase activity, Soil 3 did not effectively diminish PV phytase activity even though Soil 3 had the greatest clay content and cation exchange capacity (CEC).
At the time of filing it was also understood in the art that the effect of applying an enzyme to a plant growth medium or a plant on the susceptibility of a particular plant to a particular plant pathogen is unpredictable, because interactions between plants and pathogens are known to be complex, involving multiple biochemicals produced by both the plant and the pathogen, and can vary depending on the species of both the plant and the pathogen.
See, for example, Misas-Villamil et al. (Enzyme-inhibitor interactions at the plant-pathogen interface. Curr. Opin. Plant Biol. 2008 Aug;11(4):380-8.Epub 2008 Jun 10), who teach that during plant-pathogen interactions, the plant apoplast holds a range of attacking enzymes and counteracting inhibitors, including pathogen enzymes such as xylanases and polygalacturonases that are inhibited by plant proteins, and plant enzymes such as glucanases and proteases which are targeted by pathogen proteins (abstract). Misas-Villamil et al. also teach that pathogens secrete a broad range of inhibitors of plant defensive enzymes, such as GIP1 secreted by Phytophthora sojae that targets endo-beta-1,3 glucanase A in soybean, EP11 and EP110 secreted by Phytophthora infestans that targets a subtilisin-like Ser protease in tomato, EPIC2B secreted by Phytophthora infestans that targets a papain-like protease in tomato, and AVR2 secreted by Cladosporium fulvum that targets a papain-like protease in tomato (page 384 column 2 second full paragraph through page 386 column 1 first paragraph).
Given the breadth of the claims which encompass methods wherein a free enzyme comprising any phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof, obtained from any source, is applied to any type of plant growth medium or any type of plant or an area surrounding any type of plant wherein the plant exhibits decreased susceptibility to any type of pathogen, given that the effect of applying an enzyme to a plant growth medium or a plant on the susceptibility of a plant to a plant pathogen is unpredictable, and given the absence of any disclosure of any method wherein a plant exhibits decreased susceptibility to a pathogen as a consequence of the application of a phospholipase, a lipase, a lactonase, a chitosanase, an ACC deaminase, or combinations of any thereof to a plant growth medium or a plant or an area surrounding a plant, one skilled in the art would not recognize that the applicant was in possession of the claimed invention as a whole at the time of filing.
Response to Arguments
Applicant's arguments filed September 5, 2025 have been fully considered but they are not persuasive.
Applicants respectfully traverse the rejection, but note that claim 21 is amended herein to recite applying a free enzyme to a plant growth medium, a plant, or an arca surrounding a plant, wherein the enzyme is selected from a phospholipase, a lipase, a chitosanase, an ACC deaminase, and combinations of any thereof. Applicants also note that to the extent that the rejection relies on application to a plant seed no longer covered by the claims, the rejection is moot in view of the amendments.
Applicants maintain that all of the claims comply with the written description requirement because a person having ordinary skill in the art upon reading the instant Specification, would reasonably conclude that, at the time the application was filed, Applicants had possession of the claimed subject matter. In the instant case, Applicants point out that the specification describes phospholipases, lipases, chitosanases, and ACC deaminases, as well as their benefit towards decreasing susceptibility to a pathogen when applied to a plant growth medium, a plant, or an area surrounding a plant. In this regard Applicants point to the specification, at paragraphs [0003], [0047], [00102], [00210], [00236], [00292], [00503], and [00844]; as well as the Sequence Listing. Applicants maintain that those skilled in the art would clearly recognize that the application as a whole describes exemplary applications a phospholipase, a lipase, a chitosanase, or an ACC deaminase to a plant growth medium, a plant, as well as an area surrounding a plant; and clearly guides those skilled in the art to carry out the claimed methods.
Regarding the Lessl, Rosas, and Misas-Villamil references cited by the Examiner, Applicants note that Lessl is directed to an entirely different class of enzymes (phytases); and
discloses the particular activity of an isolated Pteris vittata phytase. Applicants also note that Rosas is similarly directed to acid phosphatase enzymes and further teaches that immobilization of enzymes is essential to their effectiveness. Applicants additionally note that Misas-Villamil
focuses on the molecular mechanisms of enzyme-inhibitor interactions at the plant-pathogen
interface, primarily discussing endogenous plant enzymes and pathogen effectors, and provide no disclosure related to the exogenous application of a phospholipase, a chitosanase, or
an ACC deaminase, and only generally identifies lipases as enzymes secreted by both plants and
fungi. Applicants further maintain that the disclosure of varying activities of phytase enzymes, assertions that acid phosphatase enzyme preparations are only effective when immobilized in a support, or the dynamics of other protein classes, does not render the claimed methods unpredictable as alleged in the Action.
Applicants maintain that in view of the present disclosure and knowledge in the art, it is respectfully submitted that Applicants were clearly in possession of the claimed invention, and the application as-filed more than sufficiently guides those of ordinary skill in the art regarding the application of the recited enzymes for the benefit of decreasing susceptibility to a pathogen.
Applicant's arguments are not persuasive.
With respect to Applicant’s assertion that the application as a whole describes exemplary applications of a phospholipase, a lipase, a chitosanase, or an ACC deaminase to a plant growth medium, a plant, as well as an area surrounding a plant; and clearly guides those skilled in the art to carry out the claimed methods, in particular at paragraphs [0003], [0047], [00102], [00210], [00236], [00292], [00503], and [00844]; as well as the Sequence Listing, this is not persuasive. The Examiner maintains that the specification does not provide any specific description of the use any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof wherein the susceptibility of any particular plant species to any particular type of pathogen is decreased when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
In particular, the Examiner maintains paragraphs [0003], [0047], [00102], [00210], [00236], [00292], [00503], and [00844], alone or in combination, do not provide any specific description of the claimed methods. With respect to paragraph [0003], while this this paragraph generally` asserts that the actions of enzymes in the rhizosphere influence bacteria, fungi, and the root system of plants, and that the overall populations of beneficial soil bacteria and fungi provide for the protection of plants against certain bacterial and fungal pathogens, this paragraph does not describe with any specificity the application of any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
With respect to paragraph [0047], while this this paragraph generally` asserts that the term “promoting plant health” refers to any beneficial effect on the health of a plant, including but not limited to, decreased susceptibility to a pathogen, this paragraph does not describe with any specificity the application of any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
With respect to paragraph [00102], while this this paragraph generally` asserts that ACC deaminases can also protect plants from pathogens as well as abiotic stresses, this paragraph does not describe with any specificity the application of any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
With respect to paragraph [00210], while this this paragraph generally` asserts that phospholipases can be used for any of the plant growth stimulating or plant health promoting purposes described herein, this paragraph does not describe with any specificity the application of any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
With respect to paragraph [00236], while this this paragraph generally` asserts that lipases can be used for any of the plant growth stimulating or plant health-promoting purposes described herein, this paragraph does not describe with any specificity the application of any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
With respect to paragraph [00292], while this this paragraph generally` asserts that chitosanases are useful for protecting plants from pathogens, this paragraph does not describe with any specificity the application of any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
With respect to paragraph [00503], while this this paragraph generally` asserts that in any of the methods described herein, plants grown in the presence of the enzyme or the microorganism can exhibit decreased susceptibility to a pathogen as compared to plants grown in the absence of the enzyme or the microorganism, under the same conditions, this paragraph does not describe with any specificity the application of any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
Further, there is no paragraph [00844] of record.
With respect to Applicant’s assertion that the Lessl, Rosas, and Misas-Villamil references do not render the claimed methods unpredictable as alleged in the Action because the cited references are not directed to the specific enzymes recited in the claims, this is not persuasive. The references were cited to raise the general issue of the unpredictability of enzymatic activity under different types of conditions that are germane to those under which the claimed methods would be practiced. Given the absence of any disclosure of any method wherein a plant exhibits decreased susceptibility to a pathogen as a consequence of the application of a phospholipase, a lipase, a lactonase, a chitosanase, an ACC deaminase, or combinations of any thereof to a plant growth medium or a plant or an area surrounding a plant, the Examiner maintains that the citation of references generally directed to the unpredictability of enzymatic activity under different types of germane conditions is appropriate, even though the exemplary enzymes in the cited references are different from the enzymes recited in the claims.
Claims 21, 25, 30, 60, 64, 173 and 228 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
The claims as currently amended are drawn to methods for protecting any type of plant from any type of pathogen comprising applying a free enzyme to a plant growth medium,
In contrast the specification does not disclose how to use a phospholipase, a lipase, a lactonase, a chitosanase, an ACC deaminase, or combinations of any thereof to decrease the susceptibility of a plant to a pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant.
The claimed invention is not enabled because the effect of applying an enzyme to a plant growth medium, a plant, or an area surrounding a plant on the susceptibility of a plant to a plant pathogen is unpredictable, since multiple variables could impact the enzyme’s activity.
See, for example, Rosas Gajardo et al., U.S. Patent Application Publication No. 2016/0326068, published Nov. 10, 2016, who teach that the enzyme activity of acid phosphatase varies depending on the manner in which it is added to soil (paragraph [0013]). Rosas Gajardo et al. teach that one of the first studies on the addition of enzymes to soils to accelerate mineralization processes was carried out by Neumann et al. (1999), who showed that adding the enzyme acid phosphatase to soils in order to accelerate the mineralization of organic phosphorous (P) led to a low liberation of P from the organic fraction because the activity of the enzyme was significantly reduced due to denaturation, suggesting that the strategy of using enzymes for accelerated mineralization can only be effective if the enzyme is active and immobilized in a support. Rosas Gajardo et al. also teach that studies have been carried out on the artificial immobilization of acid phosphatase and arylsulfatase using supports such as humic substances, 2:1 clays, and Al and Mn oxides, and that, in these cases, enzymatic activity decreased because certain supports acted as enzymatic inhibitors or lost protein during the artificial immobilization process of the enzymes, according to results obtained by Rao & Gianfreda, 2000; Kelleher et al., 2004; Whalen & Warman, 1996b. In contrast, the immobilization of the acid phosphatase in clay minerals from an Andisol increased the specific activity of the enzyme by 89% to 144%, and did not lead to a loss of protein, according to results obtained by Rosas et al. (2008), López and Rosas (2008), and Rao & Gianfreda, 2000. Rosas Gajardo et al. additionally teach that the addition of immobilized phosphatase to soils was determined by Pant and Warman (2000) to increase the available phosphorus (extracted with water and NaOH) by 49%, and that an increase in available P (Olsen P) of up to 150% with acid phosphatase immobilized in Andisol clays and very low levels of enzymatic protein was reported by López and Rosas (2008).
See also, for example, Lessl et al., U.S. Patent Application Publication No. 2016/0340658, published Nov. 24, 2016, who teach that phytase enzymes obtained from different organisms exhibit different activities in the presence of soil (paragraphs [0149]-[0152]). Lessl et al. teach that while phytase obtained from Pteris vittate(PV) was not significantly impacted after mixing with soils, retaining 94, 93, and 98% of their activities in Soil 1, 2 and 3, respectively, phytase obtained from Pteris ensiformis (PE) and wheat retained only about 6% activity in all soils after 2 h. Lessl et al. also teach that after 6 h, PV phytase activity declined 25%, where it was stable through 24 h, and that PV phytase extracts mixed in the three soils, which retained 77, 86, and 97% of the control activity between 6 and 24 h for soil 1, 2 and 3 respectively. Lessl et al. additionally teach that while in previous soil studies logarithmic decline of phytase activity was typically observed within minutes of soil addition, the PV phytase extracts of Lessl et al. retained about 64% of their original activity following 24 h of mixing, which mirrored the decline in activity in the soil-less control. Lessl et al. further teach that while soils with greater clay content, organic matter and cation/anion exchange capacity are known to more rapidly inhibit phytase activity, Soil 3 did not effectively diminish PV phytase activity even though Soil 3 had the greatest clay content and cation exchange capacity (CEC).
The claimed invention is also not enabled because the effect of applying an enzyme to a plant growth medium or a plant or an area surrounding a plant on the susceptibility of a particular plant to a particular plant pathogen is unpredictable, since interactions between plants and pathogens are known to be complex, involving multiple biochemicals produced by both the plant and the pathogen, and can vary depending on the species of both the plant and the pathogen.
See, for example, Misas-Villamil et al. (Enzyme-inhibitor interactions at the plant-pathogen interface. Curr. Opin. Plant Biol. 2008 Aug;11(4):380-8.Epub 2008 Jun 10), who teach that during plant-pathogen interactions, the plant apoplast holds a range of attacking enzymes and counteracting inhibitors, including pathogen enzymes such as xylanases and polygalacturonases that are inhibited by plant proteins, and plant enzymes such as glucanases and proteases which are targeted by pathogen proteins (abstract). Misas-Villamil et al. also teach that pathogens secrete a broad range of inhibitors of plant defensive enzymes, such as GIP1 secreted by Phytophthora sojae that targets endo-beta-1,3 glucanase A in soybean, EP11 and EP110 secreted by Phytophthora infestans that targets a subtilisin-like Ser protease in tomato, EPIC2B secreted by Phytophthora infestans that targets a papain-like protease in tomato, and AVR2 secreted by Cladosporium fulvum that targets a papain-like protease in tomato (page 384 column 2 second full paragraph through page 386 column 1 first paragraph).
In the instant case, the specification does not provide sufficient guidance with respect to how to use a phospholipase, a lipase, a lactonase, a chitosanase, an ACC deaminase, or combinations of any thereof to decrease the susceptibility of a plant to a pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant. Absent such guidance one skilled in the art would have to test a variety of different phospholipases, lipases, a lactonases, chitosanases, ACC deaminases, or combinations of any thereof from a variety of different sources on a variety of different plant species under a variety of different conditions against a variety of different plant pathogens in order to determine which set of conditions, if any, would result in a decrease in the susceptibility of a plant to a pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant. Such a trial and error approach to practicing the claimed invention would constitute undue experimentation.
Response to Arguments
Applicant's arguments filed September 5, 2025 have been fully considered but they are not persuasive.
Applicants maintain that the claimed invention is fully enabled because only routine experimentation would be required for one of ordinary skill in the art to make and use the full scope of claimed subject matter. Applicants note that some experimentation and routine screening does not preclude enablement, particularly when a reasonable amount of guidance with respect to the direction in which the experimentation should proceed is provided. Applicants maintain that the specification provides ample guidance regarding application techniques, concentrations, and use rates for applying a phospholipase, a lipase, a chitosanase, or an ACC deaminase in order to decrease susceptibility to a pathogen (i.e. promote plant health), and that a person of ordinary skill in the art may readily rely on the application as-filed to carry out the claimed methods. Applicants further maintain that all experimental procedures to practice the claimed subject matter are either described in the Specification or known to persons having ordinary skill in the art, and that such a person could therefore practice the claimed subject matter without undue experimentation.
Applicant's arguments are not persuasive.
With respect to Applicant’s assertion that undue experimentation would not be required to practice the claimed subject matter in light of the guidance provided by the specification, this is not persuasive, because the specification does not provide any specific guidance with respect to how to use any particular phospholipase, lipase, lactonase, chitosanase, ACC deaminase, or combinations of any thereof to decrease the susceptibility of any particular plant species to any particular type of pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant. Such guidance is necessary because the effect of applying an enzyme to a plant growth medium, a plant, or an area surrounding a plant on the susceptibility of a plant to a plant pathogen is unpredictable, since multiple variables could impact the enzyme’s activity, and because the effect of applying an enzyme to a plant growth medium or a plant or an area surrounding a plant on the susceptibility of a particular plant to a particular plant pathogen is unpredictable, since interactions between plants and pathogens are known to be complex, involving multiple biochemicals produced by both the plant and the pathogen, and can vary depending on the species of both the plant and the pathogen. Absent such guidance one skilled in the art would have to test a variety of different phospholipases, lipases, a lactonases, chitosanases, ACC deaminases, or combinations of any thereof from a variety of different sources on a variety of different plant species under a variety of different conditions against a variety of different plant pathogens in order to determine which set of conditions, if any, would result in a decrease in the susceptibility of a plant to a pathogen when the free enzyme is applied to a plant growth medium, a plant, or an area surrounding a plant. Such a trial and error approach to practicing the claimed invention would constitute undue experimentation.
Conclusion
THIS ACTION IS MADE FINAL. 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.
Remarks
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CYNTHIA E COLLINS whose telephone number is (571)272-0794. The examiner can normally be reached M-F 8:30 am - 5:00 pm.
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/CYNTHIA E COLLINS/Primary Examiner, Art Unit 1662