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 .
DETAILED ACTION
2. Applicants’ arguments and amendments filed on 2/09/2026, overcomes the rejections of record, however, the new grounds of rejection as set forth below are necessitated by applicants’ amendment and therefore, the following action is Final.
Any objections and/or rejections made in the previous action, and not repeated below, are hereby withdrawn.
Status of the application
3. Claims 1-5, 7-14, 16-22 are pending in this office action.
Claims 1, 2, 4, 5, 8,10, and 12-14 have been amended.
Claim 6 is further cancelled.
Claims 16-22 are new.
Claims 1-5, 7-14, 16-22 have been rejected.
Claim Rejections - 35 USC § 103
4. 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.
5. 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.
6. 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.
7. Claim(s) 1-3, 5, 7-14, 16, 20, 21, are rejected under 35 U.S.C. 103 as being unpatentable over Martina et al. (US 2016/0002688 A1: SEE SEQ SEARCH RESULT POSTED 8/27/2025 for SEQ ID #5 under “Published Application 525 kb; 99.1% Query match) [SEE NPL SEQ alignment Search Result] and as evidenced by Siller et al. (WO 2020/254592 A 1).
8. Regarding claims 1-3, 5, 7-14, 16, 17, 21 Martina et al. discloses a method which provides engineered transaminase polypeptides useful for the synthesis of chiral amine compounds under industrially relevant conditions. The disclosure also provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds (at least in Abstract).
Martina et al. also discloses that Transaminase” or “aminotransferase” are used interchangeably herein to refer to a polypeptide having an enzymatic capability of transferring an amino group (—NH.sub.2), a pair of electrons, and a proton from the primary amine of an amine donor compound to the carbonyl group (C═O) of an amine acceptor compound, thereby converting the amine donor compound into its corresponding carbonyl compound and the carbonyl acceptor compound into its corresponding primary amine compound (See e.g., Scheme 1). Transaminases as used herein include naturally occurring (wild type) transaminase as well as non-naturally occurring engineered polypeptides generated by human manipulation (at least in [0062], [0065]).
Martina et al. discloses that at least the SEQ ID # 34, has “transaminating” property and the disclosed SEQ ID # 34 has 99.1% sequence identity with the claimed SEQ ID# 5 ( SEE Sequence search result posted on 8/27/2025: SEE Result 3 14-768-408-34 (i.e. Seq #34) matches with current application 18-029-365-5 i.e. (claimed Seq ID #5) under “Published Application 525 kb; 99.1% Query match posted on 8/27/2025) [For quick look, SEE NPL SEQ alignment Search Result] which meets claims 1-3, 5(c ), 8 (c ), 10 (c ), 12 (c ), 13 (d) , 14 (c ) and new claim 21.
It is to be noted that the disclosed SEQ ID # 34 is identical to claimed SEQ ID# 5 and therefore, having identical property of transaminating a keto moiety which would have obvious property to detoxify or reduce the toxicity of Type B Trichothecene to meet claims 1, 5. It is also to be noted that as the disclosed sequence is identical to the claimed sequence, therefore, it would have the identical claimed property of modifying Type B Trichothecene as claimed in claim 1 and also modifying C8-atom by transamination a keto moiety of Type B trichothecene as claimed in claims 1-2 and converting to 8-amino DON as claimed in claim 3, claim 7 and claim 9. It is known that C8 -atom for Trichothecene has keto moiety as evidenced by Siller et al. (WO 2020/254592 A 1) that Type B Trichothecene includes DON (having carbonyl group at C8 position) (at least on page 2 lines 5-10; e.g. Nivalenol, DON etc.) and also as evidenced by applicants’ own specification (at least Fig 7 e.g. DON).
9. Regarding claim 20, it is also to be noted that and as discussed above, Martina et al. discloses that SEQ ID # 34 is matching with claimed SEQ ID # 5 having identical G59 [i.e. at 59 position, it is glycine amino acid etc.] and is matching with disclosed SEQ ID # 34 of Martina et al. with all amino acids at their respective positions as claimed in claim 20 (SEE ABSS search result posted 9/8/2025 with last NF office action].
It is to be noted that this represents TAM-Ac (i.e. polypeptide (variant) of a wild type transaminase (TAM-Transaminase as evidenced by applicants specification (in PGPUB of a wild type transaminase (TAM-Transaminase) comprises one or more equivalent (or same) amino acid/s in position/s corresponding to claimed “one or more amino acid variants at respective positions as claimed in claim 20.
10. Regarding new claim 22, claim 22 depends on claim 21. Therefore, the rejection made for claim 21 above is applicable here. In addition, additional claim limitation of “expression vectors” and/or “transgenic plants as claimed I claim 22 (vi) is addressed below. The similar claim limitation as claimed for claims -5, 8, 10-14 which depend on claim 1, is addressed below.
Martina et al. discloses that the claimed “A recombinant host cell” is defined as Recombinant” or “engineered” or “non-naturally occurring” when used with reference to, e.g., a cell, nucleic acid, or polypeptide, refers to a material, or a material corresponding to the natural or native form of the material, that has been modified in a manner that would not otherwise exist in nature, or is identical thereto but produced or derived from synthetic materials and/or by manipulation using recombinant techniques. Non-limiting examples include, among others, recombinant cells expressing genes that are not found within the native (non-recombinant) form of the cell or express native genes that are otherwise expressed at a different level (at least in [0071]).
Martina et al. also discloses the genetic engineering method to make polypeptide from the respective isolated polynucleotide sequence and its insertion into an expression vector to express in a vector system to make polypeptide ([0176]) for its use. Martina et al. also discloses methods for modifying polynucleotides and nucleic acid sequences into polypeptide sequence by utilizing recombinant DNA methods which are well known in the art ([0176]). Martina et al. also disclosed the method ([0176]- [0180]) and mentioned that Guidance which is provided in Sambrook et al., 2001. Molecular Cloning: A Laboratory Manual, 3.sup.rd Ed., Cold Spring Harbor Laboratory Press, and Current Protocols in Molecular Biology, Ausubel. F, ed., Greene Pub. Associates, 1998, updates to 2010 ([0176]). it is within the skill of one of ordinary skill in the art to consider teachings of Martina et al. to perform genetic engineering method to make polypeptide from the Morimura’s sequence to use it for further use.
Martina et al. also discloses that it can be introduced into any host as desired and the recombinant expression vector may be designed depending on the type of “host” cell” ([0185]) with at least one process is the process of integration by homologous recombination ([0188]). Therefore, the broad disclosure includes plant cell as host cell which reads on “transgenic plant, transgenic seed etc. as claimed in claim 4.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Morimura et al. with the teaching of Martina et al. to include a method which provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds (at least in Abstract).
11. Claims 1-3, 7, 9, 16, 17, 18, 21 are rejected under 35 U.S.C. 103 as being unpatentable over Morimura H. et al. (Morimura H. et al., Sato I., Uesaka K.; Draft Genome sequence of the deoxynivalenol-degrading actinomycete Morimura H., Sato I., Uesaka K.; Draft Genome sequence of the deoxynivalenol-degrading actinomycete Nocardioides sp. strain LS1, isolated from wheat leaves in Japan."; Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases: SEE SEQ SEARCH RESULT for SEQ ID #3 Uniport 182 kb; POSTED 8/27/2025: FOR quick align) in view of Martina et al. (US 2016/0002688 A1) [For quick look, SEE NPL SEQ alignment Search Result] as evidenced by Siller et al. (WO 2020/254592 A 1).
12. Regarding claims 1-3, 7,9, 16, 17, 21, Morimura et al. has disclosed gene sequence whose translational protein is responsible for “deoxynivalenol-degrading actinomycete Nocardioides sp. strain LS1, isolated from wheat leaves in Japan and submitted in GenBank on NOV-2018 for its availability which matches with SEQ ID # 3 of the claimed SEQUENCE (SEE Search Result Under Uniport Result 1, 92.8% query match (182 kb)] which meets “at least 90% sequence identity of claims 1-3.
13. Regarding new claim 18, sequence alignment is shown to be perfectly matching with all individual amino acid positions as claimed in claim 18. For convenience, this is presented as separate attachment as NPL ‘Morimura et al. seq alignment’ document and attached with this office action. This is retrieved from prior ABSS SEARCH RESULT of Morimura et al. as mentioned above and attached separately with this office action for convenience in order to look and compare all matching amino acid positions as claimed in claim 19.
Morimura et al. also discloses the sequence sequence identity with the claimed SEQ ID# 3 ( SEE Sequence search result for Morimura et al. ) matches with current application 18-029-365-3 i.e. (claimed Seq ID #3). It is also to be noted that Morimura et al. discloses that the disclosed sequence at least matching one or more amino acid variations at positions corresponding to G 18 (i.e. glycine at position 18 etc. ) of claimed SEQ ID # 3 and including all amino acids as claimed in claim 18 (SEE Morimura et al. ABSS search report, (SEE Attached NPL Morimura et al. SEQ alignment retrieved from above ABSS search result of Morimura et al. RESULT POSTED 8/27/2025).
However, Morimura et al. is silent about a composition which is a polypeptide from this disclosed sequence which can be used to perform the modification of C8 -atom of a type B trichothecene.
Martina et al. discloses a method which provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds (at least in Abstract).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Morimura et al. with the teaching of Martina et al. to include a method which provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds (at least in Abstract).
It would have the identical claimed property of modifying Type B Trichothecene as claimed in claim 1 and also modifying C8-atom by transaminating a keto moiety of Type B trichothecene as claimed in claims 1-2 and converting to 8-amino DON as claimed in claims 1, 3, claim 7 and claim 9. It is known and as evidenced by Siller et al. that Type B Tricothecene includes DON (having carbonyl group at C8 position) (at least on page 2 lines 5-10; e.g. Nivalenol, DON etc.).
`Therefore, Morimura et al. in view of Martina et al. meet claims 1-3, 7, 9, 16-17, 21 .
14. Claim(s) 4-5, 8, 10-14, 22 are rejected under 35 U.S.C. 103 as being unpatentable over Morimura H. et al. (Morimura H. et al., Sato I., Uesaka K.; Draft Genome sequence of the deoxynivalenol-degrading actinomycete Morimura H., Sato I., Uesaka K.; Draft Genome sequence of the deoxynivalenol-degrading actinomycete Nocardioides sp. strain LS1, isolated from wheat leaves in Japan.";
Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases) in view of Martina et al. (US 2016/0002688 A1) as evidenced by Siller et al. (WO 2020/254592 A 1) as applied to claims 1, 21, and further in view of in view of Chapman et al. USPN 7199082 B1.
15. Regarding claims 4-5, 8, 10-14 depend on claim 1,and claim 22 depends on claim 21. Therefore, the rejection made for claim 1 is applicable here. In addition, additional claim limitation is addressed below.
As discussed above, Morimura et al. has disclosed gene sequence whose translational protein is responsible for “deoxynivalenol-degrading actinomycete Nocardioides sp. strain LS1, isolated from wheat leaves in Japan and submitted in GenBank on NOV-2018 for its availability. which matches with SEQ ID # 3 of the claimed SEQUENCE (SEE Search Result Under Uniport Result 1, 92.8% query match (182 kb)] which meets “at least 90% sequence identity of claims 4-5, 8, 10-14 and at least 93% sequence identity of claim 21 . It is known that C8 -atom for Trichothecene has keto moiety as evidenced by Siller et al. (WO 2020/254592 A 1) that Type B Trichothecene includes DON (having carbonyl group at C8 position) (at least on page 2 lines 5-10; e.g. Nivalenol, DON etc.) and also as evidenced by applicants’ own specification (at least Fig 7 e.g. DON).
However, Morimura et al. is silent about a composition which is a polypeptide from this disclosed sequence which can be used to perform the modification of C8 -atom of a type B trichothecene.
Martina et al. discloses that the claimed “A recombinant host cell” is defined as Recombinant” or “engineered” or “non-naturally occurring” when used with reference to, e.g., a cell, nucleic acid, or polypeptide, refers to a material, or a material corresponding to the natural or native form of the material, that has been modified in a manner that would not otherwise exist in nature, or is identical thereto but produced or derived from synthetic materials and/or by manipulation using recombinant techniques. Non-limiting examples include, among others, recombinant cells expressing genes that are not found within the native (non-recombinant) form of the cell or express native genes that are otherwise expressed at a different level (at least in [0071]).
Martina et al. also discloses the genetic engineering method to make polypeptide from the respective isolated polynucleotide sequence and its insertion into an expression vector to express in a vector system to make polypeptide ([0176]) for its use. Martina et al. also discloses methods for modifying polynucleotides and nucleic acid sequences into polypeptide sequence by utilizing recombinant DNA methods which are well known in the art ([0176]). Martina et al. also disclosed the method ([0176]- [0180]) and mentioned that Guidance which is provided in Sambrook et al., 2001. Molecular Cloning: A Laboratory Manual, 3.sup.rd Ed., Cold Spring Harbor Laboratory Press, and Current Protocols in Molecular Biology, Ausubel. F, ed., Greene Pub. Associates, 1998, updates to 2010 ([0176]). it is within the skill of one of ordinary skill in the art to consider teachings of Martina et al. to perform genetic engineering method to make polypeptide from the Morimura’s sequence to use it for further use.
Martina et al. also discloses that it can be introduced into any host as desired and the recombinant expression vector may be designed depending on the type of “host” cell” ([0185]) with at least one process is the process of integration by homologous recombination ([0188]). Therefore, the broad disclosure includes plant cell as host cell which reads on “transgenic plant, transgenic seed etc. as claimed in claim 4.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Morimura et al. with the teaching of Martina et al. to include a method which provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds (at least in Abstract).
(Additionally), Chapman et al. discloses a corresponding polynucleotide sequence that encodes phospholipase D (PLD) enzyme. Also, Chapman et al. disclosed methods for preparing recombinant host cells, vectors, virus, and expression constructs, and methods for making transgenic plants that over-express PLD-specific genes in the host cell (col 23 lines 40-46).
Even if Chapman et al. discloses PLD enzyme which is different enzyme , however, Chapman et al. is used to address a method for preparing recombinant host cells, vectors, virus, and expression constructs, and methods for making transgenic plants that over-express PLD enzyme which method can be considered by any one of ordinary skill in the art to express any ‘polynucleotide sequence” to make respective biologically functional protein/peptide including claimed peptide which modifies C8-atom of trichothecene of claims 4 (i), claim 22 (i) and 8 (i). Also, it meets claim limitation of claim 4 (ii), (iii) and claim 22 (ii)-(v) and claim 8 ((ii)- (iii) and claim 14 (e).
According to MPEP 2143.01, “Obviousness can be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so. In re Kahn, 441 F.3d 977, 986, 78 USPQ2d 1329, 1335 (Fed. Cir. 2006) (discussing rationale underlying the motivation-suggestion-teaching test as a guard against using hindsight in an obviousness analysis). Axonics, Inc. v. Medtronic, Inc., 73 F.4th 950, 957-58, 2023 USPQ2d 795”.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Morimura et al. in view of Martina et al. with the teaching of Chapman et al. to include a method for preparing recombinant host cells, vectors, virus, and expression constructs, and methods for making transgenic plants that over-express the gene to make the respective peptide including the peptide responsible to modify C8-atom of Type B Trichothecene.
Therefore, it meets claim limitation of “Type B trichothecene, or DON, or DON derivative” and optional steps having transgenic plant (See Martina et al. and /or Chapman et al. above) having seq ID # 3 as claimed in step (vi) of claims 4-5, 8, 10, 12, 13 and 14 and 22. It is to be noted that the claims recite “one or more”.
Therefore, it meets the above claims and the claimed invention.
16. Claims 1, 19 are rejected under 35 U.S.C. 103 as being unpatentable over NPL ‘SEQ ID 4 alignment’ ( Artificial Seq submitted 2011; Attached match result as retrieved from prior 8/27/2025 ABSS SEARCH Report : SEE 157 Kb, Pending Patents Result 1) in view of Martina et al. (US 2016/0002688 A1) [For quick look, SEE NPL SEQ alignment Search Result] as evidenced by Siller et al. (WO 2020/254592 A 1).
17. Regarding claims 1, 19, NPL ‘SEQ ID 4 alignment’ document is retrieved from prior Artificial Seq submitted (2011; Attached match result as retrieved from prior 8/27/2025 ABSS SEARCH Report : SEE 157 Kb, Pending Patents Result 1) and attached separately with this office action as NPL document as NPL ‘SEQ ID 4 alignment’ for convenience in order to look and compare all matching amino acid positions as claimed in claim 19.
It is to be noted that in addition to prior rejection made using applicants admitted prior art as presented above (item # ), examiner is also considering this additional NPL ‘SEQ ID 4 alignment’ result where NPL ‘SEQ ID 4 alignment’ matches with claimed SEQ ID # 4 (100% match) comprises one or more equivalent (or same) amino acid/s in position/s corresponding to claimed identical “one or more amino acid variants at respective positions (e.g. N114 which is Arg at position 114 etc.) as claimed in claim 19.
The rest of the rejection with Martina et al. as secondary prior art is identical to the rejection made above (item # 21 above ) and is applicable here also.
Response to arguments
18. Applicants’ arguments and amendments have been considered.
19. Upon further review, and further considering applicant’s arguments and amendments examiner agreed that it overcome 112 first paragraph rejections of record.
20. However, examiner is maintaining 35 USC 103 Obviousness Rejections of record. Applicant’s arguments and amendment do not overcome the rejections of record. The reasons are discussed below:
(a) Applicant’s arguments made for Martina et al. (Fifth page mid-section), that Martina et al. is non-analogous art. Applicants arguments are considered as a whole.
In response to applicant's argument that Martina et al. is non-analogous art, it has been held that a prior art reference must either be in the field of the inventor’s endeavor or, if not, then be reasonably pertinent to the particular problem with which the inventor was concerned, in order to be relied upon as a basis for rejection of the claimed invention. See In re Oetiker, 977 F.2d 1443, 24 USPQ2d 1443 (Fed. Cir. 1992).
In this case, it is to be noted that examiner does not agree. Martina et al. discloses at least SEQ ID #34 which is identical to the claimed SEQ ID # 5 (Last OA item #15) as discussed above also .Therefore, even if Martina et al. is directed to engineered transaminases for pharmaceuticals /fine -chemical ketones, for diabetes patients (in Remarks, fifth page, last line), and Martina does not test transaminase activity on a broader group of substrate (in Remarks sixth page), however, Martina’s disclosed identical transaminase will serve identical claimed Transaminase” or “aminotransferase” property of having an enzymatic capability of transferring an amino group (—NH.sub.2), a pair of electrons, and a proton from the primary amine of an amine donor compound to the carbonyl group (C═O) of an amine acceptor compound, thereby converting the amine donor compound into its corresponding carbonyl compound and the carbonyl acceptor compound into its corresponding primary amine compound which is applicable to modify C8-atom of the Type B Trichothecene to transaminate a keto moiety in order to detoxify and/or reducing the toxicity of the Type B trichothecene , DON or DON derivative.
(b) Similarly, the disclosed sequence of Morimura et al. matches SEQ ID # 3 (Last OA item #17).
Therefore, as the disclosed sequence matches an identical to the claimed sequence, it will have identical claimed property. However, Martina et al. also discloses the property which is claimed property to detoxify by modifying C8-atom of the Type B trichothecene , DON or a DON derivative.
(c ) Silleet al. is used as a reference and not as a secondary prior art.
(d) Applicant’s arguments made for Doerks et al, Brenner , and Borks (in Remarks, page 4), have been considered. However, these references are related to 112 first (Enablement) rejection. These references have not been used for 103 obviousness rejection. As because, without these references 112 first (Enablement) rejection can be maintained, examiner has deleted them to avoid confusion.
21. Applicants argued on second and third pages about the experimental result using altered sequences, variants from SEQ ID #1-5 (i.e. AKR I-III) etc. as presented in Table 1 (Fig 1, SEQ ID #1-3) , and Tables 2-7, that provides information about the activities of variants for the claimed seq ID #1-3 as presented in the applicants specification ([0073]-[0074], [0078], [0135]-[0137]).
In response, examiner has considered the arguments. However, the independent claim 1 claims anyone of the whole sequence of SEQ ID #1-5 while variant is in claim 1 (c ) as an alternative . In fact, claim 1 (a)-(d) is claimed as an alternative of any one of them. Therefore, it is addressed using the respective combined teachings of prior arts of record. For example, Martina et al. discloses at least SEQ ID #74 which is identical to the claimed SEQ ID # 5 (Last OA item #15).
Similarly, the disclosed sequence of Morimura et al. matches SEQ ID # 3 (Last OA item #17).
Therefore, as the disclosed sequence matches an identical to the claimed sequence, it will have identical claimed property. However, Martina et al. also discloses the property which is claimed property to detoxify by modifying C8-atom of the Type B trichothecene , DON or a DON derivative.
22. Applicants argued on pages 3-4, that Akr I-III have the properties of converting DON to epi-THS , including LC-MS parameters, under specific pH etc. as presented in the respective Examples , Figs etc. (in Remarks , page 3).
In response, it is to be noted that the Akr III (For SEQ ID # 3) addressed by Morimura et al., ADH -LK (For SEQ ID # 4) addressed by NPL SEQ ID #4 (for claim 19 addressed above) , TAM-Ac (For SEQ ID # 5) addressed by Martina et al., in the off#4ice action above. It is also recited in the applicants specification (in PGPUB [0019]-[0024]) which can be considered as applicants admitted prior art ([0019] : For Example, http://www.uniprot.org/, e.g., as available in UniProt KB release 2020_03 Published Jun. 17, 2020).
23. Applicants have presented that the polypeptides made from this artificial sequence having Akr I-III , ADH -LK and TAM-Ac having specific property to detoxify by modifying C8-atom of the Type B trichothecene , DON or a DON derivative is presented by the applicants in the respective examples, Tables , Figs etc. in applicants’ specification (in Remarks, page 3). However, it is to be noted that the artificial sequence, as published, in Uniport ([0019]) already disclosed that respective Akr I-III variant has aldo-keto reductase (i.e. Akr) ( [0019]-[0022]), and the artificial amino acid sequence of the “ADH-Lk” variant has alcohol dehydrogenase (ADH- Alcohol dehydrogenase) and the artificial amino acid sequence of the “TAM-Ac” variant of a wild type transaminase (TAM-Transaminase). Therefore, it would have been obvious and not unexpected that these disclosed properties of the respective artificial sequences which corresponds to respective variants of SEQ ID #1-5, will be capable of modifying the C8-atom of the type B trichothecene , DON, DON derivative to modify C8-atom of the Type B trichothecene , DON , or a DON derivative as mentioned in the office action above while addressing new claims 18-20.
24. It is to be noted that as claim 4 claims “expression vectors” in claim 4 (iii), therefore, claim 4 can be rejected along with new claim 22 as discussed above (Item #14). However, claim 4 was not considered using Martina et al. as primary prior art in the last office action. Therefore, claim 4 is not added in item #14, and only prior rejection of claim 4 is maintained (item # 18).
Therefore, the rejection is made as final.
Conclusion
25. 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 extension fee 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 date of this final action.
Any inquiry concerning the communication or earlier communications from the examiner should be directed to Bhaskar Mukhopadhyay whose telephone number is (571)-270-1139.
If attempts to reach the examiner by telephone are unsuccessful, examiner’s supervisor Erik Kashnikow, can be reached on 571-270-3475. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/BHASKAR MUKHOPADHYAY/
Examiner, Art Unit 1792
/ERIK KASHNIKOW/Supervisory Patent Examiner, Art Unit 1792
Prosecution Insights