Patent Application 17638756 - IMPROVED POLYPEPTIDES CAPABLE OF CONVERTING

Title: IMPROVED POLYPEPTIDES CAPABLE OF CONVERTING SUBSTRATE 3-KETO- DEOXYNIVALENOL INTO 3-EPI- DEOXYNIVALENOL

Application Information

Invention Title: IMPROVED POLYPEPTIDES CAPABLE OF CONVERTING SUBSTRATE 3-KETO- DEOXYNIVALENOL INTO 3-EPI- DEOXYNIVALENOL
Application Number: 17638756
Submission Date: 2025-05-16T00:00:00.000Z
Effective Filing Date: 2022-02-25T00:00:00.000Z
Filing Date: 2022-02-25T00:00:00.000Z
National Class: 435
National Sub-Class: 189000
Examiner Employee Number: 98565
Art Unit: 1652
Tech Center: 1600

Rejection Summary

102 Rejections: 0
103 Rejections: 2

Cited Patents

No patents were cited in this rejection.

Office Action Text

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 .
Amendments Received
Amendments to the claims were received and entered on March 18, 2025.
Status of Claims
Claims 15, 17-18, 27 and 19 are cancelled and new claims 30-38 have been added.
Claims 14, 19-26, 28, and 30-38 are currently pending and under consideration.

Priority
The present application claims status as a 371 (National Stage) of PCT/EP2020/074056 filed on August 28, 2020 and claims priority to foreign application EP19194632.6 filed on August 30, 2019. Acknowledgment is made of applicant’s claim for foreign priority and papers submitted under 35 U.S.C. 119(a)-(d). The present application and all claims are being examined with an effective filing date of August 30, 2019.
Withdrawn Objections
In view of Applicant’s amendments, objection to claim 14 is hereby withdrawn.

Claim Objections
Claim 19 is objected to because of the following informalities:
The claim recites “wherein the step of contacting the one or more polypeptide(s) are added along with a carrier to an agrarian composition comprising a plant or parts of a plant, said agrarian composition comprising the trichothecene comprising the 3-oxo group. For improved clarity, it is suggested that the limitations regarding the agrarian composition be combined. For example, the claim could be amended to recite, “wherein the step of contacting the one or more polypeptide(s) are added along with a carrier to an agrarian composition, said agrarian composition comprising a plant or parts of a plant, and the trichothecene comprising the 3-oxo group”.

Appropriate correction is required.

Maintained/Modified Rejections Necessitated by Amendment

Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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, 20-25, 30-38 are rejected under 35 U.S.C. 103 as being unpatentable over Hassan et al. (The enzymatic epimerization of deoxynivalenol by Devosia mutans proceeds through the formation of 3-keto-DON intermediate, 2017, Scientific Reports 7: 6929, cited in the IDS), Carere et al. (The Identification of DepB: An Enzyme Responsible for the Final Detoxification Step in the Deoxynivalenol Epimerization Pathway in Devosia mutans 17-2-E-8, 2018, Front. Microbiol. 9:1573, cited in the IDS), and A0A0F5LPU3 (UniProt Database, 2015, cited in the IDS).
Regarding claim 14, Hassan et al. teaches that the epimerization of the mycotoxin deoxynivalenol (DON) proceeds by a two-step catalysis with 3-keto-DON as an intermediate, wherein DON is oxidized into 3-keto-DON and 3-keto-DON is reduced to the non-toxic 3-epi-DON and wherein the enzyme responsible for reducing 3-keto-DON to 3-epi-DON is physically separate from the enzyme responsible for oxidizing DON to 3-keto-DON (Abstract and pg. 2, Fig. 1). It is noted that DON and 3-epi-DON are trichothecenes comprising a 3-hydroxy group, and 3-keto-DON is a trichothecene comprising a 3-oxo-group (Specification, pg. 2, para 005-007). Hassan et al. further teaches that 7 Devosia species (i.e., D. mutans 17-2-E-8, D. chinhatensis, D. subaequaris, D. soli, D. limi, D. epidermidihirudinis, and D. riboflavina) demonstrate the ability to reduce 3-keto-DON to 3-epi-DON (pg. 5, bottom section, “All tested Devosia species reduce 3-keto-DON to 3-epi-DON but only few are capable of epimerizing DON” and pg. 6, Fig. 6), while unsuccessfully completing the full epimerization of DON, confirming the two-step process. It is noted that the specific strain used for D. limi is D. limi (DSM17137). Specifically, Hassan et al. teaches the contact of chemically synthesized 3-keto-DON with each of the species listed above, wherein “one mL of the actively growing culture was spiked with 100 ug/mL of DON or 3-keto-DON…” (pg. 9, top section, “Transformations of DON and 3-keto-DON by different Devosia species”). While the teachings of Hassan et al. suggest that the disclosed Devosia species, including D. limi and D. mutans 17-2-E-8, possess the specific enzyme responsible for the reduction of 3-keto-DON, Hassan et al. does not teach a specific polypeptide having at least 75% sequence identity to SEQ ID NO: 3 (elected sequence).
Carere et al. teaches that in D. mutans 17-2-E-8, a pathway designated “Dep” completes the two step reaction of detoxifying DON to 3-epi-DON, where the enzyme responsible for the 2nd step (i.e., the reduction of 3-keto-DON to 3-epi-DON) is designated “DepB” (Abstract). Carere et al. discloses comparative genomic analysis, wherein predicted CDSs from 19 strains of Devosia, including D. limi, were aligned against D, mutans 17-2-E-8. “BLAST comparisons of the depB regions with 19 other Devosia strains demonstrates that the CDSs in this region are mostly conserved among different strains” (pg. 5, left column, first para). Carere et al. further teaches that DepB is annotated as a putative oxidoreductase by RAST, and an aldo/keto reductase in NCBI (pg. 6, right column, last para).
A0A0F5LPU3 discloses an aldo/keto reductase and putative oxidoreductase from Devosia limi 17137 having 89.5% sequence identity to instant SEQ ID NO: 3 (see previous office action for sequence alignment).

An invention would have been obvious to a person of ordinary skill in the art if some teaching in the prior art would have led that person to combine prior art reference teachings to arrive at the claimed invention. Before the effective filing date of the claimed invention, the teachings of Hassan et al., that both D. mutans 17-2-E-8 and D. limi 17137 demonstrate the ability to reduce 3-keto-DON to 3-epi-DON, and the teachings of Carere et al., that the enzyme responsible for carrying out said conversion in D. mutans 17-2-E-8 is a putative oxidoreductase or aldo/keto reductase, wherein the coding sequence thereof is conserved in D. limi, would have led said practitioner to expect that the polypeptide disclosed in A0A0F5LPU3 would also convert 3-keto-DON to 3-epi-DON, because the A0A0F5LPU3 polypeptide was known at the time of present invention to be a putative oxidoreductase or aldo/keto reductase from D. limi 17137, a strain known to reduce 3-keto-DON to 3-epi-DON. Moreover, it would be obvious to use or substitute the known aldo/keto reductase in such a method and expect predictable results, since Hassan et al. and Carere et al. teach or suggest use of aldo/keto reductase in such a conversion method, and A0A0F5LPU3 already teaches a known aldo/keto reductase, in view of the findings that the A0A0F5LPU3 aldo/keto reductase is from a species that has successfully performed the desired function (See MPEP 2144.06 – Substituting equivalents known for the same purpose).
A person of ordinary skill in the art would have had a reasonable expectation of success for converting a trichothecene comprising a 3-oxo group into a trichothecene comprising a 3-hydroxy group using the aldo/keto reductase disclosed in A0A0F5LPU3. Given that Hassan et al. demonstrate a successful method of converting 3-keto-DON to 3-epi-DON by contacting 3-epi-DON with D. limi 17137, and given that Carere et al. establishes that an aldo/keto reductase, or putative oxidoreductase is the enzyme responsible for said conversion in D. mutans and the coding sequence of said enzyme is conserved across various Devosia species including D. limi 17137, said practitioner would have readily predicted that the combination of teachings would successfully result in a method of converting a trichothecene comprising a 3-oxo group into a trichothecene comprising a 3-hydroxy group by contacting the trichothecene comprising the 3-oxo group with a polypeptide having at least 75% sequence identity with instant SEQ ID NO: 3, with a reasonable expectation of success.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
Regarding claim 20, as indicated above, A0A0F5LPU3 is disclosed an aldo/keto reductase and putative oxidoreductase from Devosia limi 17137, a strain that, as evidenced by Hassan et al., has the ability to reduce 3-keto-DON to 3-epi-DON.
Regarding claim 21, the polypeptide disclosed in A0A0F5LPU3 comprises a sequence of VHEWDGMTP, beginning at amino acid position 125, wherein, according to claim 21, X1 is not M; X2 is not A; X3 is not A; and X4 is not V.
Regarding claim 22, the polypeptide disclosed in A0A0F5LPU3 comprises a sequence of SPLAGGLLSG, beginning at amino acid position 211, wherein, according to claim 22, X5 is A, V, L, G or I; X6 is L, I, V, M, A, Y, F, Norleucin, or W; and X7 is S or T.
Regarding claim 23, the polypeptide disclosed in A0A0F5LPU3 comprises a sequence of SPLAGGLLSG, beginning at amino acid position 211, wherein, according to claim 23, X5 is A; X6 is L; and X7 is S.
Regarding claim 24, the polypeptide disclosed in A0A0F5LPU3 comprises a sequence of LGRSGLKVST, beginning at amino acid position 6, wherein, according to claim 24, X8 is G, R, K, Q, N, A, V, L, I, S, T, E, or D; X9 is not M or G; X10 is not E; X11 is not S; X12is not Y; X13 is not G or A; X14 is not P; X15 is R, K, Q, N, P, A, Y, W, F, T, S, or H; and X16 is not N.
Regarding claim 25, the polypeptide disclosed in A0A0F5LPU3 comprises a sequence having several amino acid substitutions, compared to instant SEQ ID NO: 3, such as D2Q.
Regarding claims 30-31, as indicated above, the polypeptide disclosed in A0A0F5LPU3 has 89.5% sequence identity with instant SEQ ID NO: 3.
Regarding claim 28, Carere et al. teaches a process for investigating 6 potential candidates responsible for the transformation of 3-keto-DON to 3-epi DON, wherein “the genes were then codon optimized for synthesis in E. coli, synthesized and cloned into pET28A by Genscript” and “were inserted to pET28a using NdeI and BamHI restriction sites to produce proteins with N-terminal polyhistidine tags. Each construct was transformed separately into E. coli BL21; a single colony was selected for protein expression”. Carere et al. further teaches “E. coli BL21 containing each synthesized construct (see above) was propagated at 37°C in 500 ml of LB medium supplemented with 34 mg l-1 kanamycin while shaking at 175 rpm. When the cultures reached an optical density of approximately 0.7, 150 μM of isopropyl β-d-1-thiogalactopyranoside (IPTG) was added to initiate protein expression. The cultures were incubated overnight at 18°C and harvested by centrifugation at 8,000 × g for 10 min and frozen at -20°C. Each pellet was thawed and resuspended in 5 ml of 50 mM Tris, pH 8.0, 150 mM NaCl. The cells were then lysed by sonication…”. Samples were tested for enzymatic activity, identified and purified (pg. 3, “Expression and Purification of Recombinant Proteins”).
An invention would have been obvious to a person of ordinary skill in the art if some teaching in the prior art would have led that person to combine prior art reference teachings to arrive at the claimed invention. It would be obvious for a person of ordinary skill in the art to employ/apply techniques for recombinant protein expression that are well known in the art, and taught by Carere et al., using the polypeptide disclosed in A0A0F5LPU3, and expect predictable results. There is a reasonable expectation of success because Carere et al. demonstrates the successful production of depB in E. coli. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
Regarding claim 32, as indicated above, in the method disclosed by Hassan et al., several Devosia species reduced 3-keto-DON into 3-epi-DON (i.e., a trichothecene comprising a 3-hydroxy group), also discussed and illustrated in Fig. 7 and “Molecular modeling and thermodynamic stability of 3-keto-DON and 3-epi-DON” (pg. 7-8).
Regarding claim 33, as indicated above, Hassan et al. teaches several species of Devosia capable of reducing 3-keto-DON to 3-epi-DON. Hassan et al. further teaches that “most of the investigated Devosia species were also able to reduce 3-keto-DON back to DON”. Specifically, D. limi 17137, which is the subject of the polypeptide disclosed in A0A0F5LPU3, demonstrated great ability to produce 3-epi-DON, with a much lesser amount of DON production (Fig. 6, bottom graph, pg. 6).
Regarding claims 34-36, Hassan et al. discloses percentage of products formed in a reaction using 3-keto-DON as the substrate with each of the several Devosia species previously discussed above, as well as using D. mutans against various media preparations, demonstrating mixed results with respect to the enzymatic activity in separately oxidizing DON and reducing 3-keto-DON ( Fig. 6,. Bottom and Fig. 4, bottom). For example, D. mutans demonstrates 100% conversion to 3-epi-DON from 3-keto-DON, which correlates to an amount greater than DON of at least 25:1 or greater, as recited by claim 34, whereas D. limi appears to convert approx. 65% (Fig. 6). Carere et al. teaches that in D. mutans, DepB was shown to be “moderately thermostable” and “function at a range of pH-values (5-9) and functions equally well in multiple common buffers” (Abstract). Specifically, Carere et al. discloses amounts of 3-epi-DON produced using 3-keto-DON as a substrate, at various pH values over a 15 minutes reaction period (Fig. 3, pg. 5). While neither Hassan et al. nor Carere et al. explicitly disclose values for the specific activity of the enzymes responsible for the reduction of 3-keto-DON to 3-epi-DON, the combined teachings of Hassan et al. and Carere et al., in particular the pH and temperature dependent results disclosed by Carere et al., suggest that reaction conditions play a significant role in determining the specific activity of the enzyme. The specific activities claimed are clearly a result specific parameter that a person of ordinary skill in the art would routinely optimize. Optimization of parameters is a routine practice that would be obvious for a person of ordinary skill in the art to employ. It would have been customary for an artisan of ordinary skill to determine the optimal pH and/temperature and/or other reaction conditions needed to achieve the desired results. Thus, an ordinary skilled artisan would have been motivated to modify any one or more reaction condition(s), such as those taught in Carere et al., for increasing or decreasing the specific activity of the enzyme responsible for the reduction of 3-keto-DON to 3-epi-DON in the results observed in any of the Devosia species that demonstrated the ability to complete the conversion of 3-keto-DON to 3-epi-DON, including D. limi 13717, to achieve higher activity and the production of a greater ration of 3-epi-DON to DON, with a reasonable expectation of success. (see MPEP 2144.05 II., “Routine Optimization”).
Regarding claim 37, as indicated above, Hassan et al. teaches several species of Devosia capable of reducing 3-keto-DON to 3-epi-DON. In the method used to test the ability of said species, including D. limi, Hassan et al. further teaches “one mL of the actively growing culture (OD600 > 1) was spiked with 100 µg/mL (as final concentration) of either DON or 3-keto-DON in triplicates and incubated at 28 °C with shaking at 150 rpm” (pg. 9, first para).
Regarding claim 38, as indicated above, in the method disclosed by Hassan et al., several Devosia species reduced 3-keto-DON (i.e., a trichothecene comprising a 3-oxo group) into 3-epi-DON (i.e., a trichothecene comprising a 3-hydroxy group), also illustrated in Fig. 1 (top of pg. 2) and Fig. 7 (pg. 7).

Claims 19 and 26 are rejected under 35 U.S.C. 103 as being unpatentable over Hassan et al., Carere et al., and A0A0F5LPU3 as applied to claim 14 above, and further in view of Ito et al. (A novel actinomycete derived from wheat heads degrades deoxynivalenol in the grain of wheat and barley affected by Fusarium head blight. 2012, Appl Microbiol Biotechnol 96, pg. 1059–1070, cited in PTO-892).
The combined teachings of Hassan et al., Carere et al., and A0A0F5LPU3 as they apply to claim 14, have already been discussed above. Briefly, Hassan et al. teaches that the epimerization of the mycotoxin DON to non-toxic 3-epi-DON occurs in two steps, using two separate enzymes, with 3-keto-DON as an intermediate. Hassan et al. further teaches 7 Devosia species that successfully convert 3-keto DON to 3-epi DON. Carere et al. identifies the enzyme in D. mutans responsible for the conversion of 3-keto-DON to 3-epi-DON as a putative oxidoreductase or aldo/keto reductase, which A0A0F5LPU3 discloses from D. limi 17137, one of the species disclosed by Hassan et al. that successfully performed the conversion to 3-epi-DON. Neither Hassan, Carere or A0A0F5LPU3 teach wherein the polypeptide or enzyme responsible for the conversion from 3-keto DON to 3-epi DON (i.e., the reductase) are added to an agrarian composition with a carrier, wherein said agrarian composition comprises a plant or plant parts and the trichothecene comprising the 3-oxo group (e.g., 3- keto DON).
Ito et al. teaches a DON-utilizing actinomycete, Marmoricola sp. strain MIM116, from wheat heads through a novel isolation procedure including an in situ plant enrichment step, wherein the strain had background degradation activity, and the activity was enhanced twofold by the consumption of DON. Ito et al. further teaches the utilization of “Tween 80 as a spreading agent of strain MIM116 because it promoted DON degradation and the growth of strain MIM116 in the presence of DON”. Ito et al. reports “the inoculation of MIM116 cell suspension plus 0.01% Tween 80 into 1,000 harvested kernels of wheat and barley resulted in a DON decrease from approximately 3 mg kg−1 to less than 1 mg kg−1 of dry kernels” (Abstract).

An invention would have been obvious to a person of ordinary skill in the art if some teaching in the prior art would have led that person to combine prior art reference teachings to arrive at the claimed invention. Before the effective filing date of the claimed invention, given the teachings of Ito et al. above, and given that DON epimerization is a 2 step process, as taught by Hassan et al., with 3-keto DON being an intermediate that requires a separate enzyme, such as the one disclosed in A0A0F5LPU3, for the conversion to the non-toxic trichothecene 3-epi DON, it would be obvious for a person of ordinary skill in the art to use a liquid such as Tween 80 as a spreading agent, or carrier, for the polypeptide disclosed in A0A0F5LPU3, an aldo/keto reductase from D. limi that is capable of converting 3-keto Don to 3-epi-DON, according to Hassan et al. and Carere et al. Said practitioner would be motivated to do so for the benefit of being able to facilitate the inoculation and treatment of infected crops commonly affected by the mycotoxin DON. There is a reasonable expectation of success because Ito et al. demonstrates the successful inoculation of harvested infected kernels of wheat and barley, using Tween 80 as a spreading agent for a DON degrading bacteria, and demonstrates the successful widespread degradation of DON as a result. Therefore, said practitioner would have readily predicted that the combination of teachings would successfully result in a method of converting a trichothecene comprising a 3-oxo group into a trichothecene comprising a 3-hydroxy group, by contacting a polypeptide according to claim 14 with a carrier to an agrarian composition comprising the trichothecene with the 3-oxo group. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.

Response to Arguments for Rejections under 35 USC § 103
In the response filed on March 18, 2025, Applicant argues that ”Carere does not provide any incentive or motivation to choose an enzyme other D. mutans DepB because Carere teaches DepB works well in various buffers and a broad pH range”. Applicant also argues “there is nothing in UniProt AOAOF5LPU3 about mycotoxins, reducing trichothecene contamination of foods, or conversion of DON to 3-epi- DON” and that “there is no experimental evidence or reasoning otherwise provided in the Office action to support the assumption that an enzyme from D. limi would have been expected to function identically to DepB from D. mutans”. With respect to all of the above, it is noted in the MPEP 2143.02 II., “obviousness does not require absolute predictability, but at least some degree of predictability is required. Evidence showing there was no reasonable expectation of success may support a conclusion of nonobviousness. In re Rinehart, 531 F.2d 1048, 189 USPQ 143 (CCPA 1976)”. Absent evidence to the contrary, there is a reasonable expectation of success that the aldo/keto reductase disclosed in AOAOF5LPU3 from D. limi 17137, the same strain that successfully converted 3-keto DON to 3-epi DON in Hassan et al., would function similar to the aldo-keto reductase of D. mutans that also converted 3-keto DON to 3-epi DON in Hassan et al., both of which at the time of invention being “putative”. Pursuant to MPEP 2143.02 I., “Conclusive proof of efficacy is not required to show a reasonable expectation of success. OSI Pharm., LLC v. Apotex Inc., 939 F.3d 1375, 1385, 2019 USPQ2d 379681 (Fed. Cir. 2019) ("To be clear, we do not hold today that efficacy data is always required for a reasonable expectation of success. Nor are we requiring ‘absolute predictability of success.’"); Acorda Therapeutics, Inc. v. Roxane Lab., Inc., 903 F.3d 1310, 1333, 128 USPQ2d 1001, 1018 (Fed. Cir. 2018) ("This court has long rejected a requirement of ‘[c]onclusive proof of efficacy’ for obviousness." (citing to Hoffmann-La Roche Inc. v. Apotex Inc., 748 F.3d 1326, 1331 (Fed. Cir. 2014); PharmaStem Therapeutics, Inc. v. ViaCell, Inc., 491 F.3d 1342, 1364 (Fed. Cir. 2007); Pfizer, Inc. v. Apotex, Inc., 480 F.3d 1348, 1364, 1367–68 (Fed. Cir. 2007) (reasoning that "the expectation of success need only be reasonable, not absolute")”. Additionally, regarding the choice between DepB from D. mutans and the enzyme from D. limi, Applicant stated there was no motivation to replace DepB but the rationale above does not require motivation and does not cite motivation to do so. The teaching or suggestion is based on a combination of MPEP 2144.06 – Substituting equivalents known for the same purpose and MPEP 2143 B. Simple Substitution of One Known Element for Another To Obtain Predictable Results. Lastly, in regards to the function of the aldo/keto reductase disclosed in AOAOF5LPU3, Carere et al. already establishes that an aldo keto/reductase (from D. mutans) is responsible for the conversion of 3-keto DON to 3-epi DON. Considering that there were only 3 aldo/keto reductases known at the time of the invention for D. limi 17137 (see screenshot below from NCBI database), the strain that demonstrated the ability to perform the conversion of 3-keto DON to 3-epi DON in Hassan et al., it would “obvious to try” one of the three aldo/keto reductase enzymes belonging to D. limi 17137 , and it would obvious to make these substitutions and expect predictable results. Applicants arguments have been considered in full and have not been found to be persuasive, and therefore the rejections have been maintained.

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Conclusion
No claim is on condition for allowance.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.

Any inquiry concerning this communication or earlier communications from the examiner should be directed to NAGHMEH NINA MOAZZAMI whose telephone number is (703)756-4770. The examiner can normally be reached Monday-Friday, 9:00-5:00.
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/NAGHMEH NINA MOAZZAMI/Examiner, Art Unit 1652

/ROBERT B MONDESI/Supervisory Patent Examiner, Art Unit 1652