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
Election/Restrictions
Applicant's election of Group I, claims 1, 3, 6-9, 11-12, 15-17 and 44, and SEQ ID NO: 23 and 31 in the reply filed on 6/13/2007 is acknowledged (response, page 1, 2nd paragraph).
Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.03(a)).
As a result, claims 7-8, 18-19, 21, 23-24, 27, 32, 36 and 40 are withdrawn from consideration because they are drawn to non-elected invention or species.
Claims 1, 3, 6, 9, 11-12, 15-17 and 44, and SEQ ID NO: 23 and 31
The requirement is deemed proper and is therefore made FINAL.
Specification
2. The abstract of the disclosure is objected to because the abstract should be in narrative form and generally limited to a single paragraph within the range of 50 to 150 words. See MPEP § 608.01(b).
3.. The specification is objected to under 37 CFR 1.821(d) as failing to refer to a sequence by use of its sequence identifier preceded by “SEQ ID NO:”. The nucleotide sequences in Figures 3 and 5 should be identified as SEQ ID NOs. Alternatively, the brief descriptions of those figures on pages 5-6 can be amended to recite the identifiers.
4. The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code. See MPEP § 608.01. See, for example, pages 32, 36, 41-43.
5. The disclosure is objected to because the status of U.S. application needs to be updated. For example, U.S. application is recited on page 1.
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.
Written Description
6. Claim 11 is rejected under 35 U.S.C. 112, 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(s), at the time the application was filed, had possession of the claimed invention.
The claims are drawn to a CBM having at least 75% sequence identity to SEQ ID NO: 31.
The specification teaches CBM comprising SEQ ID NO: 31.
The Applicants do not describe any other CBM having at least 75% sequence identity to SEQ ID NO: 31, except for SEQ ID NO: 31 itself. Neither the specification nor the prior art teaches conserved structures responsible for CBM.
The Federal Circuit has recently clarified the application of the written description requirement to inventions in the field of biotechnology. See University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568, 43 USPQ2d 1398, 1406 (Fed. Cir. 1997). In summary, the court stated that a written description of an invention requires a precise definition, one that defines the structural features of the chemical genus that distinguishes it from other chemical structures. A definition by function does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. The court goes on to say, “A description of a genus of cDNAs may be achieved by means of a recitation of a representative number of cDNAs, defined by nucleotide sequence, falling within the scope of the genus or of a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus.” See University of California v. Eli Lilly and Co., 119 F.3d 1559; 43 USPQ2d 1398, 1406 (Fed. Cir. 1997).
Applicants fail to describe a representative number of variants of SEQ ID NO:31. Applicants only describe a single species which is SEQ ID NO:31 itself. Furthermore, Applicants fail to describe structural features common to members of the claimed genus of CBM. Hence, Applicants fail to meet either prong of the two-prong test set forth by Eli Lilly. Furthermore, given the lack of description of the necessary elements essential for the CBM of SEQ ID NO: 31, it remains unclear what features identify a CBM of SEQ ID NO: 31. Since said genus has not been described by specific structural features, the specification fails to provide an adequate written description to support the breath of the claims.
Scope of Enablement
7. Claims 1, 3, 6-9, 11-12, 17 and 44 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for the modified Vip3A polypeptide comprising SEQ ID NO: 23 and being pesticidal against lepidopteran insect, does not reasonably provide enablement for any modified Vip3A polypeptide comprising any variants of SEQ ID NO: 23. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to practice the invention commensurate in scope with these claims.
Instant claims are broadly directed to any modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase, and comprising a sequence that is at least 75% identical to SEQ ID NO:23.
The specification teaches several modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase comprising SEQ ID NO:23.
However, given that the modified Vip3 is obtained by combination of any Vip3 comprising with any heterologous CBM from β-1,4-mannanase while keeping only a portion of Domain I and II, there are unmanageable number of possible combinations for such modified Vip3, however, without a functional language associated with those modified Vip3 protein, undue experimentation would have been required to develop assay for each of the variants and to test the unknown functionality for each of the variants.
To overcome the rejection, it is suggested to specifying that the modified Vip3 is pesticidal against lepidopteran insect.
As for variants of SEQ ID NO:23, although the consensus sequence can be obtained through the alignment of Vip3 proteins, they are obtained only by the sequence alignment without any experimental verification. Falcon-Perez JM et al. (1999, J Biol Chem. 274:23584-90) teach that when twenty-two single amino acid substitutions or deletions by site-directed mutagenesis in the nucleotide binding domains, the proposed regulatory domain, and the fourth cytoplasmic loop of the yeast cadmium factor (Ycf1p) vacuolar protein were made, two conserved amino acid residues, Glu (709) and Asp (821), were found to be unnecessary for Ycf1p biogenesis and function (abstract).
Making “conservative” substitutions (e.g., substituting one polar amino acid for another, or one acidic one for another) does not produce predictable results. Lazar et al. (1988, Mol. Cell. Biol. 8:1247-1252) teach that the “conservative” substitution of glutamic acid for aspartic acid at position 47 reduced biological function of transforming growth factor alpha while “nonconservative” substitutions with alanine or asparagine had no effect (abstract). Similarly, Hill et al (1998, Biochem. Biophys. Res. Comm. 244:573-577) teach that when three histidines that are maintained in ADP-glucose pyrophosphorylase across several species are substituted with the “nonconservative” amino acid glutamine, there is little effect on enzyme activity, while the substitution of one of those histidines with the “conservative” amino acid arginine drastically reduced enzyme activity (see Table 1). All these mutated proteins would have at least 95% identity to the original protein.
Given the claim breath, unpredictability, and lack of guidance as discussed above, undue experimentation would have been required by one skilled in the art to develop assay for each of variants and test for its functionality.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
8. Claims 1, 3, 6, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 10,421,791.
Instant claims are drawn to modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase, wherein the CBM is substituted for all or a portion if domain III; wherein the Vip3A comprises all or a portion of domain I/II of Vip3; or wherein the modified Vip3A polypeptide comprises all or a portion if domain I of Vip3, all or a portion if domain II of Vip3 and the heterologous CBM; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises an agriculturally acceptable carrier; or wherein CBM comprises a metal binding site; or a method for controlling pests comprising contacting the pests with a pesticidally effective amount of the modified Vip3 with an agriculturally acceptable carrier.
Claims 1-9 of U.S. Patent No. 10,421,791 teach modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase, wherein the CBM is substituted for all or a portion if domain III and wherein the modified Vip3A polypeptide is pesticidal against an insect; or wherein the Vip3A comprises all or a portion of SEQ ID NO:1 or wherein all or a portion of domain III comprises amino acids 542 to 667 of SEQ ID NO:1; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises am agriculturally acceptable carrier; or wherein CBM comprises a metal binding site. Therefore Claims 1-9 of U.S. Patent No. 10,421,791 teach teaches all the limitation set forth by instant claims.
9. Claims 1, 3, 6, 9, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 10,421,791, as applied for claims 1, 3, 6, 12, 15-17 and 44, further in view of Estruch et al. (Proc. Natl. Acad. Sci. USA Vol. 93, pp. 5389-5394, May 1996).
.
Instant claims 1, 3, 6, 12, 15-17 and 44, are discussed above.
Claim 9 further teaches that the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
The teaching of claims 1-9 of U.S. Patent No. 10,421,791 is discussed above.
Claims 1-9 of U.S. Patent No. 10,421,791 do not teach the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
Estruch et al. teach a Vip3 protein that is about 85% identical to instant SEQ ID NO: 23 (see alignment below).
It would have been obvious to modified Vip3 protein from Bacillus thuringiensis of Estruch et al. by replacing domain III of Vip3 of Estruch et al. with modified CBM from bacteria β-1,4-mannanase comprising SEQ ID NO: 24 of U.S. Patent No. 10,421,791, resulting instant invention with reasonable expectation of success. One would have been motivated for such modification given that Vip3 protein from Bacillus thuringiensis of Estruch et al. is an obvious design choice for making a modified Vip3 protein. Such modified Vip3 protein would obviously comprise sequence that has at least 75% amino acid sequence similarity with instant SEQ ID NO: 23.
RESULT 1
Q45792_BACTU
ID Q45792_BACTU Unreviewed; 789 AA.
AC Q45792;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 08-OCT-2025, entry version 76.
DE SubName: Full=Vegetative insecticidal protein VIP3 {ECO:0000313|EMBL:AFK76350.1};
DE SubName: Full=Vip3A(A) protein {ECO:0000313|EMBL:AAC37036.1};
GN Name=vip3A(a) {ECO:0000313|EMBL:AAC37036.1};
GN Synonyms=vip3A1-4 {ECO:0000313|EMBL:AFK76350.1};
OS Bacillus thuringiensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428 {ECO:0000313|EMBL:AAC37036.1};
RN [1] {ECO:0000313|EMBL:AAC37036.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AB88 {ECO:0000313|EMBL:AAC37036.1};
RX PubMed=8643585; DOI=10.1073/pnas.93.11.5389;
RA Estruch J.J., Warren G.W., Mullins M.A., Nye G.J., Craig J.A., Koziel M.G.;
RT "Vip3A, a novel Bacillus thuringiensis vegetative insecticidal protein with
RT a wide spectrum of activities against lepidopteran insects.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5389-5394(1996).
RN [2] {ECO:0000313|EMBL:AFK76350.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S1/4 {ECO:0000313|EMBL:AFK76350.1};
RX PubMed=22915162; DOI=10.1002/jobm.201100653;
RA Sellami S., Zghal T., Cherif M., Zalila-Kolsi I., Jaoua S., Jamoussi K.;
RT "Screening and identification of a Bacillus thuringiensis strain S1/4 with
RT large and efficient insecticidal activities.";
RL J. Basic Microbiol. 53:539-548(2013).
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DR EMBL; L48811; AAC37036.1; -; Genomic_DNA.
DR EMBL; JQ768411; AFK76350.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45792; -.
DR SMR; Q45792; -.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR022180; Vip3.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF12495; Vip3A_N; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 536..652
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
SQ SEQUENCE 789 AA; 88672 MW; 9DD3DD926823C7AE CRC64;
Query Match 84.5%; Score 3412.5; Length 789;
Best Local Similarity 86.8%;
Matches 697; Conservative 17; Mismatches 68; Indels 21; Gaps 7;
Qy 1 MNKNNTKLSTRALPSFIDYFNGIYGFATGIKDIMNMIFKTDTGGDLTLDEILKNQQLLND 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MNKNNTKLSTRALPSFIDYFNGIYGFATGIKDIMNMIFKTDTGGDLTLDEILKNQQLLND 60
Qy 61 ISGKLDGVNGSLNDLIAQGNLNTELSKEILKIANEQNQVLNDVNNKLDAINTMLRVYLPK 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ISGKLDGVNGSLNDLIAQGNLNTELSKEILKIANEQNQVLNDVNNKLDAINTMLRVYLPK 120
Qy 121 ITSMLSDVMKQNYALSLQIEYLSKQLQEISDKLDIINVNVLINSTLTEITPAYQRIKYVN 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 ITSMLSDVMKQNYALSLQIEYLSKQLQEISDKLDIINVNVLINSTLTEITPAYQRIKYVN 180
Qy 181 EKFEELTFATETSSKVKKDGSPADILDELTELTELAKSVTKNDVDGFEFYLNTFHDVMVG 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 EKFEELTFATETSSKVKKDGSPADILDELTELTELAKSVTKNDVDGFEFYLNTFHDVMVG 240
Qy 241 NNLFGRSALKTASELITKENVKTSGSEVGNVYNFLIVLTALQAQAFLTLTTCRKLLGLAD 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 NNLFGRSALKTASELITKENVKTSGSEVGNVYNFLIVLTALQAQAFLTLTTCRKLLGLAD 300
Qy 301 IDYTSIMNEHLNKEKEEFRVNILPTLSNTFSNPNYAKVKGSDEDAKMIVEAKPGHALIGF 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 IDYTSIMNEHLNKEKEEFRVNILPTLSNTFSNPNYAKVKGSDEDAKMIVEAKPGHALIGF 360
Qy 361 EISNDSITVLKVYEAKLKQNYQVDKDSLSEVIYGDMDKLLCPDQSEQIYYTNNIVFPNEY 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 EISNDSITVLKVYEAKLKQNYQVDKDSLSEVIYGDMDKLLCPDQSEQIYYTNNIVFPNEY 420
Qy 421 VITKIDFTKKMKTLRYEVTANFYDSSTGEIDLNKKKVESSEAEYRTLSANDDGVYMPLGV 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 VITKIDFTKKMKTLRYEVTANFYDSSTGEIDLNKKKVESSEAEYRTLSANDDGVYMPLGV 480
Qy 481 ISETFLTPINGFGLQADENSRLITLTCKSYLRELLLATDLSNKETKLIVPPSGFISNIVE 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 ISETFLTPINGFGLQADENSRLITLTCKSYLRELLLATDLSNKETKLIVPPSGFISNIVE 540
Qy 541 NPGF-EDNLASWTNWGNTSSVTSPAFAGAKAARIASGEGGAGQII-----PGIPSGTTYV 594
| |||| | : | | :|| | | | |
Db 541 NGSIEEDNLEPWKANNKNAYVDHTGGVNGTKALYVHKDGGISQFIGDKLKPKTEYVIQYT 600
Qy 595 LSGHGSVS-AGTDTAIVGVDCLDANNNVLAKNTLRFNQTLYEFKSTAFTTVPGTAKLQVY 653
: | |: :| : : | ||| | ||: : ||| || ||
Db 601 VKGKPSIHLKDENTGYIHYE--DTNNN------LEDYQTI----NKRFTT--GTDLKGVY 646
Qy 654 IYKNADSGANAFLDDLSLVEVSPSEKLLSPELINTNNWTSTGSTNISGNTLTLYQGGRGI 713
: : :| |: |: ::|:|||||||||||||||||||||||||||||||||||||||
Db 647 LILKSQNGDEAWGDNFIILEISPSEKLLSPELINTNNWTSTGSTNISGNTLTLYQGGRGI 706
Qy 714 LKQNLQLDSFSTYRVYFSVSGDANVRIRNSREVLFEKRYMSGAKDVSEMFTTKFEKDNFY 773
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 707 LKQNLQLDSFSTYRVYFSVSGDANVRIRNSREVLFEKRYMSGAKDVSEMFTTKFEKDNFY 766
Qy 774 IELSQGNNLYGGPIVHFYDVSIK 796
|||||||||||||||||||||||
Db 767 IELSQGNNLYGGPIVHFYDVSIK 789
Db 781 SFENVSIK 788
10. Claims 1, 3, 6, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 11,028,134.
Instant claims are drawn to modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase, wherein the CBM is substituted for all or a portion if domain III; wherein the Vip3A comprises all or a portion of domain I/II of Vip3; or wherein the modified Vip3A polypeptide comprises all or a portion if domain I of Vip3, all or a portion if domain II of Vip3 and the heterologous CBM; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises an agriculturally acceptable carrier; or wherein CBM comprises a metal binding site; or a method for controlling pests comprising contacting the pests with a pesticidally effective amount of the modified Vip3 with an agriculturally acceptable carrier.
Claims 1-9 of U.S. Patent No. 11,028,134 teach modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase, wherein the CBM is substituted for all or a portion if domain III and wherein the modified Vip3A polypeptide is pesticidal against an insect; or wherein the Vip3A comprises all or a portion of SEQ ID NO:2 or wherein all or a portion of domain III comprises amino acids 542 to 667 of SEQ ID NO:2; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises am agriculturally acceptable carrier; or wherein CBM comprises a metal binding site;
Therefore Claims 1-9 of U.S. Patent No. 11,028,134 teach teaches all the limitation set forth by instant claims.
11. Claims 1, 3, 6, 9, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 11,028,134 as applied for claims 1, 3, 6, 12, 15-17 and 44, further in view of Estruch et al. (Proc. Natl. Acad. Sci. USA Vol. 93, pp. 5389-5394, May 1996).
.
Instant claims 1, 3, 6, 12, 15-17 and 44, are discussed above.
Claim 9 further teaches that the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
The teaching of claims 1-9 of U.S. Patent No. 11,028,134 is discussed above.
Claims 1-9 of U.S. Patent No. 10,421,791 do not teach the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
Estruch et al. teach a Vip3 protein that is about 85% identical to instant SEQ ID NO: 23 (see alignment below).
It would have been obvious to modified Vip3 protein from Bacillus thuringiensis of Estruch et al. by replacing domain III of Vip3 of Estruch et al. with CBM from bacteria β-1,4-mannanase comprising SEQ ID NO: 29 of U.S. Patent No. 11,028,134, resulting instant invention with reasonable expectation of success. One would have been motivated for such modification given that Vip3 protein from Bacillus thuringiensis of Estruch et al. is an obvious design choice for making a modified Vip3 protein. Such modified Vip3 protein would obviously comprise sequence that has at least 75% amino acid sequence similarity with instant SEQ ID NO: 23.
12. Claims 1, 3, 6, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 11,771,092.
.
Instant claims are drawn to modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase, wherein the CBM is substituted for all or a portion if domain III; wherein the Vip3A comprises all or a portion of domain I/II of Vip3; or wherein the modified Vip3A polypeptide comprises all or a portion if domain I of Vip3, all or a portion if domain II of Vip3 and the heterologous CBM; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises an agriculturally acceptable carrier; or wherein CBM comprises a metal binding site; or a method for controlling pests comprising contacting the pests with a pesticidally effective amount of the modified Vip3 with an agriculturally acceptable carrier.
Claims 1-15 of U.S. Patent No. 11,771,092 teach modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase comprising SEQ ID NO:25, wherein the CBM is substituted for all or a portion if domain III and wherein the modified Vip3A polypeptide is pesticidal against an insect; or wherein the Vip3A comprises all or a portion of SEQ ID NO:2 or wherein all or a portion of domain III comprises amino acids 542 to 667 of SEQ ID NO:2; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises am agriculturally acceptable carrier; or wherein CBM comprises a metal binding site. Therefore claims 1-15 of U.S. Patent No. 11,771,092 teach all the limitation set forth by instant claims.
13. Claims 1, 3, 6, 9, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 11,771,092 as applied for claims 1, 3, 6, 12, 15-17 and 44, further in view of Estruch et al. (Proc. Natl. Acad. Sci. USA Vol. 93, pp. 5389-5394, May 1996).
.
Instant claims 1, 3, 6, 12, 15-17 and 44, are discussed above.
Claim 9 further teaches that the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
The teaching of claims 1-15 of U.S. Patent No. 11,771,092 is discussed above.
Claims 1-9 of U.S. Patent No. 10,421,791 do not teach the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
Estruch et al. teach a Vip3 protein that is about 85% identical to instant SEQ ID NO: 23 (see alignment below).
It would have been obvious to modified Vip3 protein from Bacillus thuringiensis of Estruch et al. by replacing domain III of Vip3 of Estruch et al. with CBM from bacteria β-1,4-mannanase comprising SEQ ID NO: 25 of U.S. Patent No. 11,771,092, resulting instant invention with reasonable expectation of success. One would have been motivated for such modification given that Vip3 protein from Bacillus thuringiensis of Estruch et al. is an obvious design choice for making a modified Vip3 protein. Such modified Vip3 protein would obviously comprise sequence that has at least 75% amino acid sequence similarity with instant SEQ ID NO: 23.
14. Claims 1, 3, 6, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 12,207,658.
Instant claims are drawn to modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase, wherein the CBM is substituted for all or a portion if domain III; wherein the Vip3A comprises all or a portion of domain I/II of Vip3; or wherein the modified Vip3A polypeptide comprises all or a portion if domain I of Vip3, all or a portion if domain II of Vip3 and the heterologous CBM; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises an agriculturally acceptable carrier; or wherein CBM comprises a metal binding site; or a method for controlling pests comprising contacting the pests with a pesticidally effective amount of the modified Vip3 with an agriculturally acceptable carrier.
Claims 1-15 of US Patent No. 12,207,658 are drawn to modified Vip3 comprising a heterologous CBM from bacteria β-1,4-mannanase comprising SEQ ID NO:28, wherein the CBM is substituted for all or a portion if domain III and wherein the modified Vip3A polypeptide is pesticidal against an insect, wherein the Vip3A comprises all or a portion of SEQ ID NO:1 or wherein all or a portion of domain III comprises amino acids 542 to 667 of SEQ ID NO:1; or wherein the modified Vip3A polypeptide is pesticidal against corn earworm; or wherein the composition further comprises am agriculturally acceptable carrier; or wherein CBM comprises a metal binding site; or wherein the modified Vip3 polypeptide comprises SEQ ID NO: 11 or 20. Therefore claims 1-15 of U.S. Patent No. 12,207,658 teach all the limitation set forth by instant claims.
15. Claims 1, 3, 6, 9, 12, 15-17 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 12,207,658 as applied for claims 1, 3, 6, 12, 15-17 and 44, further in view of Estruch et al. (Proc. Natl. Acad. Sci. USA Vol. 93, pp. 5389-5394, May 1996).
.
Instant claims 1, 3, 6, 12, 15-17 and 44, are discussed above.
Claim 9 further teaches that the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
The teaching of claims 1-15 of U.S. Patent No. 12,207,658 is discussed above.
Claims 1-9 of U.S. Patent No. 12,207,658 do not teach the modified Vip3A polypeptide has at least 75% amino acid sequence similarity with SEQ ID NO: 23.
Estruch et al. teach a Vip3 protein that is about 85% identical to instant SEQ ID NO: 23 (see alignment below).
It would have been obvious to modified Vip3 protein from Bacillus thuringiensis of Estruch et al. by replacing domain III of Vip3 of Estruch et al. with CBM from bacteria β-1,4-mannanase comprising SEQ ID NO: 28 of U.S. Patent No. 12,207,658, resulting instant invention with reasonable expectation of success. One would have been motivated for such modification given that Vip3 protein from Bacillus thuringiensis of Estruch et al. is an obvious design choice for making a modified Vip3 protein. Such modified Vip3 protein would obviously comprise sequence that has at least 75% amino acid sequence similarity with instant SEQ ID NO: 23.
Conclusion
No claim is allowed.
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/LI ZHENG/Primary Examiner, Art Unit 1662