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 .
Copending Applications
Applicants must bring to the attention of the Examiner, or other Office official involved with the examination of a particular application, information within their knowledge as to other copending United States applications, which are "material to patentability" of the application in question. MPEP 2001.06(b). See Dayco Products Inc. v. Total Containment Inc., 66 USPQ2d 1801 (CA FC 2003).
Claims 1-5, 7-10 and 31-42, pending in this application, are examined.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 4-5, 9-10, 34-36 and 38-42 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 4, drawn to a fused protein with two or more Av3 variant polypeptide separated by a linker, does not further limit parent claim 1, drawn to an Av3 variant polypeptide having at least one of the mutations (a) R1K relative to SEQ ID NO: 1 and (b) a deletion of the C-terminal valine relative to SEQ ID NO: 1. The Av3 variant polypeptide of claim 1 cannot be a fused protein because it has only SEQ ID NO: 1 with mutations and does not have other Av3 variants. If Applicant intends claim 4 to depend from claim 3, the claim should be amended to replace “claim 1” with ----claim 3---. Claim 5 does not obviate the rejection.
Claim 5 is confusing in the recitation of “.., wherein the linker is cleavable inside at least one of …………..; and (ii) cleavable inside the gut of a mammal”. Clarification is required to more clearly define the metes and bounds of the claim.
Claim 9 is indefinite in the recitation of “operable to encode” as it is not defined in the specification and is open to an individual interpretation. If Applicant intends “a polynucleotide that encodes an Av3 variant polypeptide, it is suggested that “operable to encode” in line 1 be replaced with ---that encodes---. Dependent claim 10 is included in the rejection because it does not obviate the rejection.
Claim 34 is indefinite in the recitation of “operable to express” as it is not defined in the specification and is open to an individual interpretation. If Applicant intends “a polynucleotide that encodes an Av3 variant polypeptide, it is suggested that “operable to express” in line 3 be replaced with ---that encodes--- (as in claim 37). Dependent claims 35-36 and 38-42 are included in the rejection.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1 and 31-32 are rejected under 35 U.S.C. 102(b) as being anticipated by Martinez et al (Accession no. TZAZ3; July 2004; Martinez et al (FEBS Lett (1977) 84::247-252).
The claims are drawn to an Av3 variant polypeptide having an insecticidal activity against one or insects having one or more of mutations R1K relative to SEQ ID NO: 1 and a deletion of the C-terminal valine relative to SEQ ID NO: 1; an Av3 variant consisting of SEQ ID NO: 2, 3 or 4; or comprising an amino acid sequence that is at least 90% identical to SEQ ID NO: 2, 3 or 4 (that does not consist of the amino acid sequence of SEQ ID NO: 1).
SEQ ID NO: 2-4 are Av3 variants derived from SEQ ID NO: 1.
SEQ ID NO: 1 consists of 27 amino acid residues (native)
SEQ ID NO: 2: is an Av3 variant with the N-terminal amino acid substitution R1K relative to SEQ ID NO: 1.
SEQ ID NO: 3: is an Av3 variant with a deletion of the C-terminal valine relative to SEQ ID NO: 1. SEQ ID NO: 3 consists of 26 amino acids.
SEQ ID NO: 4: is an Av3 variant with both the N-terminal amino acid substitution of R1K and a deletion of a C-terminal valine relative to SEQ ID NO: 1.
Martinez et al teach peptide sequence having at least 98% identity to Applicant’s SEQ ID NO: 2 and 4 (that does not consist of SEQ ID NO: 1); and a peptide sequence that is 100% identical to Applicant’s SEQ ID NO: 3. See the alignment of sequences shown below.
Regarding the limitation “the variant polypeptide does not consist of the amino acid sequence of SEQ ID NO: 1”, it is noted that: “consisting SEQ ID NO: 1” requires the full length sequence with 100% identity to SEQ ID NO: 1 and same length of SEQ ID NO: 1”. Therefore, Martinez et al teach all claim limitations.
Search Results of Instant SEQ ID NO: 2:
RESULT 1
TZAZ3
toxin III - snake-locks sea anemone
C;Species: Anemonia sulcata (snake-locks sea anemone)
C;Date: 30-Apr-1979 #sequence_revision 24-Sep-1981 #text_change 09-Jul-2004
C;Accession: A91446; A91674; A01798
R;Martinez, G.; Kopeyan, C.; Schweitz, H.; Lazdunski, M.
FEBS Lett. 84, 247-252, 1977
A;Title: Toxin III from Anemonia sulcata: primary structure.
A;Reference number: A91446; MUID:78084776; PMID:23311
A;Accession: A91446
A;Molecule type: protein
A;Residues: 1-27 <MAR>
A;Cross-references: UNIPROT:P01535; UNIPARC:UPI00001105B0
R;Beress, L.; Wunderer, G.; Wachter, E.
Hoppe-Seyler's Z. Physiol. Chem. 358, 985-988, 1977
A;Title: Amino acid sequence of toxin III from Anemonia sulcata.
A;Reference number: A91674; MUID:78044787; PMID:21843
A;Accession: A91674
A;Molecule type: protein
A;Residues: 1-21,'SC',24-27 <BER>
A;Cross-references: UNIPARC:UPI0000173620
C;Comment: Three disulfide bonds are present.
C;Superfamily: toxin III
C;Keywords: venom
Query Match 98.4%; Score 183; Length 27;
Best Local Similarity 96.3%;
Matches 26; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KSCCPCYWGGCPWGQNCYPEGCSGPKV 27
:||||||||||||||||||||||||||
Db 1 RSCCPCYWGGCPWGQNCYPEGCSGPKV 27
Search Results of Instant SEQ ID NO: 3
RESULT 1
TZAZ3
toxin III - snake-locks sea anemone
C;Species: Anemonia sulcata (snake-locks sea anemone)
C;Date: 30-Apr-1979 #sequence_revision 24-Sep-1981 #text_change 09-Jul-2004
C;Accession: A91446; A91674; A01798
R;Martinez, G.; Kopeyan, C.; Schweitz, H.; Lazdunski, M.
FEBS Lett. 84, 247-252, 1977
A;Title: Toxin III from Anemonia sulcata: primary structure.
A;Reference number: A91446; MUID:78084776; PMID:23311
A;Accession: A91446
A;Molecule type: protein
A;Residues: 1-27 <MAR>
A;Cross-references: UNIPROT:P01535; UNIPARC:UPI00001105B0
R;Beress, L.; Wunderer, G.; Wachter, E.
Hoppe-Seyler's Z. Physiol. Chem. 358, 985-988, 1977
A;Title: Amino acid sequence of toxin III from Anemonia sulcata.
A;Reference number: A91674; MUID:78044787; PMID:21843
A;Accession: A91674
A;Molecule type: protein
A;Residues: 1-21,'SC',24-27 <BER>
A;Cross-references: UNIPARC:UPI0000173620
C;Comment: Three disulfide bonds are present.
C;Superfamily: toxin III
C;Keywords: venom
Query Match 100.0%; Score 182; Length 27;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RSCCPCYWGGCPWGQNCYPEGCSGPK 26
||||||||||||||||||||||||||
Db 1 RSCCPCYWGGCPWGQNCYPEGCSGPK 26
Search Results of Instant SEQ ID NO: 4
RESULT 1
TZAZ3
toxin III - snake-locks sea anemone
C;Species: Anemonia sulcata (snake-locks sea anemone)
C;Date: 30-Apr-1979 #sequence_revision 24-Sep-1981 #text_change 09-Jul-2004
C;Accession: A91446; A91674; A01798
R;Martinez, G.; Kopeyan, C.; Schweitz, H.; Lazdunski, M.
FEBS Lett. 84, 247-252, 1977
A;Title: Toxin III from Anemonia sulcata: primary structure.
A;Reference number: A91446; MUID:78084776; PMID:23311
A;Accession: A91446
A;Molecule type: protein
A;Residues: 1-27 <MAR>
A;Cross-references: UNIPROT:P01535; UNIPARC:UPI00001105B0
R;Beress, L.; Wunderer, G.; Wachter, E.
Hoppe-Seyler's Z. Physiol. Chem. 358, 985-988, 1977
A;Title: Amino acid sequence of toxin III from Anemonia sulcata.
A;Reference number: A91674; MUID:78044787; PMID:21843
A;Accession: A91674
A;Molecule type: protein
A;Residues: 1-21,'SC',24-27 <BER>
A;Cross-references: UNIPARC:UPI0000173620
C;Comment: Three disulfide bonds are present.
C;Superfamily: toxin III
C;Keywords: venom
Query Match 98.4%; Score 179; Length 27;
Best Local Similarity 96.2%;
Matches 25; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KSCCPCYWGGCPWGQNCYPEGCSGPK 26
:|||||||||||||||||||||||||
Db 1 RSCCPCYWGGCPWGQNCYPEGCSGPK 26
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 1-5, 7-10 and 31-42 are rejected under 35 U.S.C. 103 as being obvious over Kennedy et al Kennedy et al (US 20170174731 A1; same as Kennedy et al (WO 2013/134734 A3; Applicant’s IDS) in view of Moran et al (Biochem. J. (2007) 406, pp.41-48; Applicant’s IDS) and Martinez et al (FEBS Lett (1977) 84:247-252).
The claims are drawn to an Av3 variant polypeptide having at least one or both of the mutations (a) R1K relative to SEQ ID NO: 1 and (b) a deletion of the C-terminal valine relative to SEQ ID NO: 1; wherein said Av3 variant polypeptide further comprises a homopolymer or heteropolymer of two or more Av3 variant polypeptides having the same or different amino acid sequences or separated by a cleavable or non-cleavable linker; a plant, plant tissue/seed/cell comprising said Av3 variant polypeptide or a polynucleotide encoding the same; and a composition comprising said Av3 variant polypeptide; and a method of producing an AVP comprising preparing a vector comprising a first expression cassette comprising a polynucleotide encoding an Av3 variant having at least one of the mutations (a) R1K relative to SEQ ID NO: 1 and (b) a deletion of the C-terminal valine relative to SEQ ID NO: 1, introducing the vector into a yeast strain; growing the yeast strain in a growth medium under conditions suitable for expression of the AVP and secretion into the growth medium, and isolating the expressed AVP from the growth medium; wherein the vector is a plasmid comprising an alpha-MF signal, a Kex 2 cleavage site; wherein the yeast strain is Kluyveromyces lactis. The claims are also drawn to an Av3 variants sequences having at least 90% identity to SEQ ID NO: 2, 3 or 4 that does not consist of SEQ ID NO: 1.
SEQ ID NO: 2: is an Av3 variant with the N-terminal amino acid substitution R1K relative to SEQ ID NO: 1.
SEQ ID NO: 3: is an Av3 variant with a deletion of the C-terminal valine relative to SEQ ID NO: 1.
SEQ ID NO: 4: is an Av3 variant with both the N-terminal amino acid substitution R1K and a deletion of a C-terminal valine relative to SEQ ID NO: 1.
Kennedy et al teach the unmodified (native) AV3 (or AVP) from Anemonia viridis and Av3 variant sequence Av3 + 2 having insecticidal activity, a polynucleotide encoding said AV3 variant, and a plant, plant cell or seed expressing said AV3 peptide ([00359]). At Table 3, Kennedy et al show that the addition of glycine-serine dipeptide to the N-terminus of the AV3 peptide contributes to significant improvement of the peptide yield. See the alignment of sequences shown below. At columns [0379]-[0385] and Example 3 teach a method of expressing a vector comprising Av3 and Av3+2 peptide ORF which encode alpha-MF-Kex 2 cleavage site:Av3 (or Av3+2) in the yeast strain Kluyveromyces lactis ; growing the yeast strain in a growth medium under conditions suitable for expression of the AVP and secretion into the growth medium, and isolating the expressed AVP from the growth medium [00386-0388]. At Example 3, SEQ ID NO:29 (Av3 variant or Av3+2); SEQ ID NO: 30 (native Av3); SEQ ID NO: 31 (optimized Av3+2 expression ORF sequence); and SEQ ID NO: 32 (optimized native Av3 expression ORF) are the insecticidal polypeptides to express in in the yeast Kluyveromyces lactis strains. At Figs 17-18, Kennedy et al show the Av3+2 variant polypeptide yield produced from yeast transformants were more than three times higher than the yield of native Av3 polypeptide [0388]. Other yeast strains that can be used for production of the Av3 and variant polypeptides include Pichia pastoris, Yarrowia and Hansenula sp., Schizosaccharomyces and Saccharomyces ([0308] and [0432-0433]). At paragraphs [0445]-[0447], Kennedy et al suggest producing fusion cysteine rich polypeptides including the Av3 polypeptides and variants thereof for synergistic effects by combining different (heteropolymer) or same (homopolymer) polypeptide sequences that can act on the lining of the insect gut or hemolymph for effective control; and compositions comprising said polypeptides and excipients [0450].
While Kennedy et al teach mutations to the AV3 (instant SEQ ID NO: 1) to produce AVP variants that retain the insecticidal activity; Av3 variant (Av3+2) and the polynucleotide encoding said variant, Kennedy et al do not explicitly teach Av3 variant with one or both of the mutations (a) R1K relative to SEQ ID NO: 1 and (b) a deletion of the C-terminal valine relative to SEQ ID NO: 1. However, SEQ ID NO: 1 consists of only 27 amino acid residues and mutations including substitutions and/or deletions of any one or more amino acids thereof to obtain variants that retain or with enhanced insecticidal activity are taught in the prior art as evidenced by each of Moran et al and Martinez et al.
Moran et al teach that the Av3 (or AVP) is a short peptide toxin isolated from Anemonia viridis having insecticidal activity. Table 1 and page 45 show substitution of 16 residues native Av3, not including glycine and cysteine, with alanine, and toxicity and binding assays. Table 1 of Moran et al teach effects of amino acid substitutions in positions R1, S2, P5, Y7, W8, P12, W13, Q15, N16, Y18, P19, E20, S23, P25, K26, and V27 of the AV3, on the toxicity to blowfly larvae. Moran et al suggest that the changes of the AV3 activity as result of these amino acid substitutions may be related to the functional role of the residues in the interaction with the channel. Moran et al describe the Av3 as a unique model for design of selective anti-insect compounds. At the paragraph bridging pages 46 and 47, Moran et al reasoned why study on Av3 is important by stating “…their ability to interact in various ways with Na illuminates a heterogenous receptor. In addition, the smaller bioactive surface of Av3 and its selectivity to insect Nav s compared with other site-3 toxin offers a convenient model for studying how to design selective anti-insect compounds”. Moran et al teach a method of adding the amino acids GS to the N-terminal of Av3 polypeptide by creating a fusion protein which includes a protease cleavage site and expressing said fusion protein in a recombinant host cell, cultivating said host cell and obtaining the fusion protein.
Martinez et al is cited in Moran et al. the teachings of martineza et al is discussed above.
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to apply one or amino acid substitutions in the AV3 and identify mutants that retain insecticidal activity as taught by each of Kennedy et al (US 20170174731) and Moran et al, with a reasonable expectation of success. One would have been motivated to alter the highly flexible R1, given that its substitution affected the binding affinity and activity of the toxin as taught by Moran et al. Applicant shows no unexpected results with the amino acid substitutions in the 27 amino acids sequence. Therefore, that given SEQ ID NO: 2-4 of the instant claims are taught in the prior art, and given that the AV3 (SEQ ID NO: 1) is structurally and functionally well characterized in the prior art as discussed above, one would have been motivated to conduct further amino acid substitutions, deletions and/or additions in the AV3 to identify and obtain variants that retain insecticidal activity with good yield and express the variant peptides in transgenic plants or plant parts, with a reasonable expectation of success, as suggested by each of Kennedy et al and Moran et al.
MPEP 2141 (III) teaches that the prior art is not limited just to the references being applied, but includes the understanding of one of ordinary skill in the art. The prior art reference (or references when combined) need not teach or suggest all the claim limitations, and the "mere existence of differences between the prior art and an invention does not establish the invention's nonobviousness." Dann v. Johnston, 425 U.S. 219, 230, 189 USPQ 257, 261 (1976). The gap between the prior art and the claimed invention may not be "so great as to render the [claim] nonobvious to one reasonably skilled in the art."ld. In determining obviousness, neither the particular motivation to make the claimed invention nor the problem the inventor is solving controls. The proper analysis is whether the claimed invention would have been obvious to one of ordinary skill in the art after consideration of all the facts.
MPEP 2145 teaches that a showing of unexpected results must be based on evidence, not argument or speculation. In re Mayne, 104 F.3d 1339, 1343-44, 41 USPQ2d 1451, 1455-56 (Fed. Ciro 1997) (conclusory statements that claimed compound possesses unusually low immune response or unexpected biological activity that is unsupported by comparative data held insufficient to overcome prima fade case of obviousness). In the instant case, Applicant has not provided any evidence to support unexpected results.
Therefore, for all the reasons discussed above, the claimed invention is a prima facie obvious.
RESULT 1
BAT11272
ID BAT11272 standard; DNA; 360 BP.
XX
AC BAT11272;
XX
DT 07-NOV-2013 (first entry)
XX
DE Anemore Viridis optimized native Av3 expression ORF, SEQ 32.
XX
KW codon usgae; crop improvement; ds; insect infection; insect resistance;
KW protein production; recombinant protein; transgenic plant.
XX
OS Anemonia viridis.
OS Synthetic.
XX
CC PN WO2013134734-A2.
XX
CC PD 12-SEP-2013.
XX
CC PF 08-MAR-2013; 2013WO-US030042.
XX
PR 09-MAR-2012; 2012US-0608921P.
PR 08-MAY-2012; 2012US-0644212P.
PR 07-SEP-2012; 2012US-0698261P.
PR 26-NOV-2012; 2012US-0729905P.
XX
CC PA (VEST-) VESTARON CORP.
XX
CC PI Kennedy RM, Tedford W, Hendrickson C, Venable R, Foune C;
CC PI Mcintyre J, Carlson A, Bao L;
XX
DR WPI; 2013-N24132/64.
XX
CC PT New protein comprising an endoplasmic reticulum signal peptide operably
CC PT linked to a cysteine rich insecticidal protein such as an inhibitor
CC PT cysteine knot motif protein.
XX
CC PS Disclosure; SEQ ID NO 32; 186pp; English.
XX
CC The present invention relates to a novel insecticidal protein useful for
CC controlling Bacillus thuringiensis resistant insects in a plant. The
CC protein comprises an endoplasmic reticulum signal peptide (ERSP) at its N
CC -terminal, operably linked to a cysteine rich insecticidal protein (CRIP)
CC such as an inhibitor cysteine knot (ICK) motif protein. The invention
CC further relates to: (1) a peptide comprising an N-terminal dipeptide with
CC a nonpolar and a polar amino acid to its N and C terminals respectively,
CC operable linked to the CRIP, ICK or a non-ICK peptide; (2) a composition
CC comprising a pore forming insecticidal protein (PFIP) and the CRIP; and
CC (3) a method for controlling Bacillus thuringiensis resistant insects
CC such as Plutella xylostella Acanthoscelides obtectus, Forficula
CC auricularia, Leucophaea maderae, Blaniulus guttulatus, Aonidiella
CC auraniii and Armadillidium vulgare by creating a plant expressing a
CC combination of the PFIP and CRIP. The proteins and composition of the
CC invention are economically used for controlling the insects at the larval
CC stage thus improving yield of the plant and has good insecticidal
CC activity leading to high productivity. The present sequence represents a
CC Anemore Viridis optimized native Av3 expression ORF, which is useful for
CC preparing the plant expressing the insecticidal proteins of the present
CC invention.
XX
SQ Sequence 360 BP; 100 A; 67 C; 84 G; 109 T; 0 U; 0 Other;
Alignment Scores:
Length: 360
Score: 139.00 Matches: 18
Percent Similarity: 80.8% Conservative: 3
Best Local Similarity: 69.2% Mismatches: 5
Query Match: 80.3% Indels: 0
DB: 46 Gaps: 0
US-17-276-050-30 (1-26) x BAT11272 (1-360)
Qy 1 LysAlaCysCysProCysTyrTrpGlyGlyCysProTrpGlyAlaAlaCysTyrProAla 20
::::::|||||||||||||||||||||||||||||||||||| |||||||||
Db 269 AGATCATGCTGCCCTTGTTACTGGGGTGGTTGTCCATGGGGTCAAAATTGTTATCCAGAG 328
Qy 21 GlyCysAlaAlaAlaLys 26
||||||::: |||
Db 329 GGTTGTTCTGGACCTAAG 346
RESULT 2
EU919733
LOCUS EU919733 354 bp mRNA linear INV 21-AUG-2009
DEFINITION Anemonia viridis clone 3 neurotoxin 7 precursor, mRNA, complete
cds.
ACCESSION EU919733
VERSION EU919733.1
KEYWORDS .
SOURCE Anemonia viridis
ORGANISM Anemonia viridis
Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
Actiniidae; Anemonia.
REFERENCE 1 (bases 1 to 354)
AUTHORS Moran,Y., Weinberger,H., Lazarus,N., Gur,M., Kahn,R., Gordon,D. and
Gurevitz,M.
TITLE Fusion and retrotransposition events in the evolution of the sea
anemone Anemonia viridis neurotoxin genes
JOURNAL J. Mol. Evol. 69 (2), 115-124 (2009)
PUBMED 19609479
REFERENCE 2 (bases 1 to 354)
AUTHORS Moran,Y., Weinberger,H. and Gurevitz,M.
TITLE Direct Submission
JOURNAL Submitted (23-JUL-2008) Department of Plant Sciences, Tel Aviv
University, Ramat Aviv, Tel Aviv 69978, Israel
FEATURES Location/Qualifiers
source 1..354
/organism="Anemonia viridis"
/mol_type="mRNA"
/db_xref="taxon:51769"
/clone="3"
/country="Israel"
5'UTR 1..70
CDS 71..289
/note="Av7; inhibits inactivation of invertebrate sodium
channels"
/codon_start=1
/product="neurotoxin 7 precursor"
/protein_id="ACL12308.1"
/translation="MMSRLLVFLMLGAAFMLVVSANDAYGDEPAFKDLNQGDESLGKR
KSCCPCWLRGNCFWGQNCYPEGCSGPKV"
sig_peptide 71..202
mat_peptide 203..286
/product="neurotoxin 7"
/note="Av7"
3'UTR 290..354
Alignment Scores:
Length: 354
Score: 137.50 Matches: 22
Percent Similarity: 85.7% Conservative: 2
Best Local Similarity: 78.6% Mismatches: 3
Query Match: 73.9% Indels: 1
DB: 279 Gaps: 1
US-17-276-050-1 (1-27) x EU919733 (1-354)
Qy 1 ArgSerCysCysProCysTyrTrp---GlyGlyCysProTrpGlyGlnAsnCysTyrPro 19
:::|||||||||||||||::: ||| ||| |||||||||||||||||||||
Db 203 AAATCCTGCTGTCCTTGCTGGTTGCGCGGTAATTGCTTCTGGGGACAGAACTGCTATCCG 262
Qy 20 GluGlyCysSerGlyProLysVal 27
||||||||||||||||||||||||
Db 263 GAAGGCTGCTCAGGCCCTAAAGTA 286
RESULT 10
US-15-390-153-31
; Sequence 31, Application US/15390153
; Publication No. US20170174731A1
; GENERAL INFORMATION
; APPLICANT: Vestaron Corporation
; TITLE OF INVENTION: Toxic Peptide Production, Peptide Expression in Plants and
; TITLE OF INVENTION:Combinations of Cysteine Rich Peptides
; FILE REFERENCE: 225312/FAM X US/361200
; CURRENT APPLICATION NUMBER: US/15/390,153
; CURRENT FILING DATE: 2016-12-23
; PRIOR APPLICATION NUMBER: 14/383,841
; PRIOR FILING DATE: 2014-09-08
; PRIOR APPLICATION NUMBER: PCT/US2013/030042
; PRIOR FILING DATE: 2013-03-08
; NUMBER OF SEQ ID NOS: 1593
; SOFTWARE: PatentIn version 3.5
; SEQ ID NO 31
; LENGTH: 366
; TYPE: DNA
; ORGANISM: Hordeum Vulgare
US-15-390-153-31
Alignment Scores:
Length: 366
Score: 186.00 Matches: 27
Percent Similarity: 100.0% Conservative: 0
Best Local Similarity: 100.0% Mismatches: 0
Query Match: 100.0% Indels: 0
DB: 68 Gaps: 0
US-17-276-050-1 (1-27) x US-15-390-153-31 (1-366)
Qy 1 ArgSerCysCysProCysTyrTrpGlyGlyCysProTrpGlyGlnAsnCysTyrProGlu 20
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 275 AGATCATGCTGCCCTTGTTACTGGGGTGGTTGTCCATGGGGACAAAACTGTTATCCTGAA 334
Qy 21 GlyCysSerGlyProLysVal 27
|||||||||||||||||||||
Db 335 GGATGTTCTGGTCCAAAGGTA 355
Remarks
No claim is allowed.
Contact Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MEDINA AHMED IBRAHIM whose telephone number is (571)272-0797. The examiner can normally be reached Monday-Friday, 9:00 - 6:00.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, BRATISLAV STANCOVIC can be reached at 571-270-0305. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
MEDINA AHMED. IBRAHIM
Primary Examiner
Art Unit 1662
/MEDINA A IBRAHIM/Primary Examiner, Art Unit 1662