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
Status of Application/Election/Restrictions
Applicant’s election of Tryptophan as an amino acid having a hydrophobic side, 9 loops, one CPP having 6 amino acids including SEQ ID NO:124 and a fluorescent protein as looped protein in the reply filed on September 15, 2025 is acknowledged. 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 § 818.01(a)).
Claims 1-35 are canceled. Claims 36-59 are pending in this Application. Upon reconsideration, the species election among different amino acids having a hydrophobic side chain recited in claim 36, the species election among different loops, different numbers of amino acids in CPP recited in claims 37 and 41, and the species election among different SEQ ID NOs: recited in claim 52 and different looped proteins recited in claim 59 are withdrawn because the subject matter can be found in the same prior art reference. Thus, the subject matter to the extent of the above species is included and under examination in this office action. Election was treated as without traverse in the reply filed on September 15, 2025.
Claims 36-59 are under examination in this office action.
Specification
The disclosure is objected to because of the following informalities: The use of the term “nanobody” (p.34, [0094]-p. 35, [0095]), which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 36-59 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
To provide adequate written description and evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof.
Claims 36-59 are drawn to a looped protein comprising at least one loop and at least one cell penetrating peptide (CPP), wherein at least one CPP comprises at least three arginines (3R) or analogs thereof and at least one CPP comprises at least three amino acids having a hydrophobic side chain selected from naphthylalaine (Nal), 3-(3-benzothienyl)-alanine (Bta), phenylglycine (Phg), homophenylalanine (HPhe), phenylalanine (Phe/F), tryptophan (Trp/W), or tyrosine (Tyr/Y).
The claims encompass a genus of looped protein comprising at least one loop and at least one CPP, wherein at least one CPP comprises at least 3R or analogs thereof, and at least one CPP comprises at least 3 amino acids having a hydrophobic side chain selected from naphthylalaine (Nal), 3-(3-benzothienyl)-alanine (Bta), phenylglycine (Phg), homophenylalanine (HPhe), phenylalanine (Phe/F), tryptophan (Trp/W), or tyrosine (Tyr/Y).
Applicant has not disclosed sufficient species for the broad genus of looped protein comprising at least one loop and at least one CPP wherein at least one CPP comprises at least 3R or analogs thereof and at least one CPP comprises at least three amino acids having a hydrophobic side chain selected from Nal, Bta, Phg, HPhe, Phe/F, Trp/W, or Tyr/Y.
The specification only describes loop insertion mutants with a CPP (SEQ ID NO:117 or 118) in a specific loop region of PTP1B, GFP-binding Nanobody (GBN), EGFP and Purine Nucleoside Phosphorylase (PNP).
Based on Applicant’s own admission, only the following specific loop insertion mutants with a CPP (SEQ ID NO:117 or 118) in a specific loop region of PTP1B, GFP-binding Nanobody (GBN), EGFP and Purine Nucleoside Phosphorylase (PNP) can still maintain activities:
i. Loop insertion mutants of PTP1B with the CPP(SEQ ID NO:117 or 118) in 5 solvent exposed loop regions of PTP1B (Examples 1-2, Figures 4A-B):
i) only PTP1B-1W (SEQ ID NO:136), PTP1B-2R (SEQ ID NO:139) and PTP1B-4R (SEQ ID NO:143) among the 10 loop insertion mutants of PTP1B in Table 1 showed catalytic activities as wild type PTP1B based on p-nitrophenyl phosphate (pNPP, 0.5mM) as substrate; and
ii) only PTP1B-2R (SEQ ID NO:139) and PTP1B-4R (SEQ ID NO:143) mutants exhibited lower pY level in NIH 3T3 cells.
ii. Loop insertion mutants of GFP-binding Nanobody (GBN) with the CPP(SEQ ID NO:117 or 118) in Non-CDR loops and CDR1-3 of GBN (Examples 3-4, Tables 3-5, Figures 7-8, 11-12):
i) only GBN-1W (SEQ ID NO:161), GBN-3W (SEQ ID NO:165) and GBN-3R (SEQ ID NO:164) produced soluble proteins;
ii) only GBN-3W (SEQ ID NO:165) and GBN-3R (SEQ ID NO:164) can form a complex with GFP at 1:1;
iii) GBN-3R failed to co-localize with intracellularly expressed GFP in HeLa cells;
iv) only GBN-3W showed partially colocalize with GFP; and
v) GBN-3W-NLS (c-Myc nuclear localization signal) failed to cause nuclear accumulation of GFP or colocalize with GFP.
iii. Loop insertion mutants of EGFP with the CPP (SEQ ID NO:117 or 118) in Loop 9 of EGFP (Example 5, Table 5A):
i) EGFP- W3R3(SEQ ID NO:168) showed no improvement in cellular uptake compared to WT EGFP; and
ii) only EGFP-R3W3 (SEQ ID NO:169) and EGFP-R4W4 (SEQ ID NO:170) entered the cell with 8 and 13-fold higher efficiency than EGFP.
iv. Loop insertion mutants of Purine Nucleoside Phosphorylase (PNP) with the CPP (SEQ ID NO:117 or 118) in loop regions of His20-Pro25 (loop 1), Asn74-Gly75 (loop 2) and Gly182-Leu187 (loop 3) of PNP (Example 6, Table 6, Figure 14B):
i) Only PNP-3R (SEQ ID NO:175) resulted in 1.35-fold higher PNP activity than normal S49 cells based on a commercial PNP enzymatic assay kit.
However, the claims are not limited to mutants of PTP1B, GBN, EGFP or PNP modified with insertion of the CPP of SEQ ID NO:117 or 118 into a specific loop in the PTP1B, GBN, EGFP or PNP set forth above but also encompass a genus of structurally and functionally undefined looped proteins comprising at least one loop from a genus of structurally and functionally undefined loop and at least one CPP recited in instant claims.
In making a determination of whether the application complies with the written description requirement of 35 U.S.C. 112, first paragraph, it is necessary to understand what Applicant is in possession of and what Applicant is claiming.
M.P.E.P. § 2163 instructs:
An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. . . .
An applicant may show possession of an invention by disclosure of drawings or structural chemical formulas that are sufficiently detailed to show that applicant was in possession of the claimed invention as a whole. . . .
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics.”
This standard has not been met in this case. From the specification, it is clear that Applicant is in possession of loop insertion mutants of PTP1B-1W (SEQ ID NO:136), PTP1B-2R (SEQ ID NO:139) and PTP1B-4R (SEQ ID NO:143); GBN-3W (SEQ ID NO:165); EGFP-R3W3 (SEQ ID NO:169) and EGFP-R4W4 (SEQ ID NO:170); and PNP-3R (SEQ ID NO:175). However, Applicant is not in possession of other structurally and functionally undefined looped protein comprising at least one structurally and functionally undefined loop and at least one structurally and functionally undefined CPP.
Based on Applicant’s own admission in the specification (para. [0151]), the stability of mutant proteins with insertion of amphipathic CPP sequences into protein loops depends on the specific CPP sequences, the site of insertion and the nature of the host protein. Based on Applicant’s own admission in the specification (Examples 1-7), only PTP1B-1W (SEQ ID NO:136), PTP1B-2R (SEQ ID NO:139) and PTP1B-4R (SEQ ID NO:143); GBN-3W (SEQ ID NO:165); EGFP-R3W3 (SEQ ID NO:169) and EGFP-R4W4 (SEQ ID NO:170); and PNP-3R (SEQ ID NO:175) can still maintain the activities of the proteins.
The specification provides no structural and functional relationship and correlation between the claimed genus of looped protein and PTP1B-1W (SEQ ID NO:136), PTP1B-2R (SEQ ID NO:139) and PTP1B-4R (SEQ ID NO:143); GBN-3W (SEQ ID NO:165); EGFP-R3W3 (SEQ ID NO:169) and EGFP-R4W4 (SEQ ID NO:170); and PNP-3R (SEQ ID NO:175) that sill maintain activities of their counterparts shown in Examples 1-6.
It is known that a single amino acid change on a molecule or protein can abolish the activity or the binding ability of the molecule or protein. For example, a substitution of lysine residue by glutamic acid at position 118 of acidic fibroblast growth factor results in a substantial loss of its biological activity including the binding ability to heparin and its receptor (Burgess et al. J of Cell Bio. 1990, 111:2129-2138). Even if an active or binding site were identified in the specification, they may not be sufficient, as the ordinary artisan would not immediately recognize that an active or binding site must assume the proper three-dimensional configuration to be active because conformation is dependent upon surrounding residues; i.e. substitution of non-essential residues can often destroy activity. In addition to a core determinant sequence, the protein-protein interaction also relies on the flanking or noncontiguous residues (see p. 445 the second column, first paragraph, Pawson et al. 2003, Science 300:445-452). The optimal binding motif for a domain is not necessarily suitable for physiological or in vivo interaction. The predictive data always need to be validated by actual analyses in cells (see p. 445, the third column, second paragraph, Pawson et al. 2003, Science 300:445-452). Alaoui-lsmaili teaches that designing a mutein having predictable activities is difficult because of the complexity of the interactions between ligands and receptors (Alaoui-lsmaili et al., Cytokine Growth Factor Rev. 2009; 20:501-507). For example, given the complexity of BMP-BMP receptor interactions, it is difficult to design BMPs with improved affinity and/or specificity for one specific receptor. More importantly, predicting the in vivo biological activity of such altered BMPs remains a challenging undertaking (see p. 502, right col., 2th paragraph). Further, when multiple mutations are introduced, there is even less predictability because Guo et al. teaches that the effects of mutations on protein function are largely additive (see p. 9207, left col., 2th paragraph, Guo et al., PNAS 2004; 101:9205-9210).
The specification fails to teach what structures/amino acid sequences can or cannot be included/changed in looped protein in order to preserve the activity of the claimed genus of looped proteins. There is no identification of any particular portion of the structure that must be conserved. The instant specification fails to provide sufficient descriptive information, such as definitive structural or functional features of the claimed genus of looped proteins comprising at least one loop and at least one CPP. There is no description of the conserved regions which are critical to the function of the claimed genus. There is no description of the sites at which variability may be tolerated and there is no information regarding the relation of structure of other looped protein to the function of PTP1B-1W (SEQ ID NO:136), PTP1B-2R (SEQ ID NO:139) and PTP1B-4R (SEQ ID NO:143); GBN-3W (SEQ ID NO:165); EGFP-R3W3 (SEQ ID NO:169) and EGFP-R4W4 (SEQ ID NO:170); and PNP-3R (SEQ ID NO:175) shown in Examples 1-6. Furthermore, the prior art does not provide compensatory structural or correlative teachings sufficient to enable one of skill to identify what other looped proteins comprising at least one loop and at least one CPP might be.
Since the common characteristics/features of other looped proteins comprising at least one loop and at least one CPP are unknown, a skilled artisan cannot envision the functional correlations of the genus with the claimed invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the genus of looped proteins comprising at least one loop and at least one CPP.
Based on MPEP § 2161.01 and §2163, “to satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116”.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116).
As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of looped proteins comprising at least one loop and at least one CPP, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483.
Therefore, the claimed looped protein comprising at least one loop and at least one CPP has not met the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115). Applicant is directed to the Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, ¶ 1 "Written Description" Requirement. See MPEP § 2161.01 and 2163.
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 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.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 36-59 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Claims 36-59 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Pei’648 (WO2018089648, published May 17, 2018, priority Nov 9, 2016).
Claims 36-59 are drawn to a looped protein comprising at least one loop and at least one cell penetrating peptide (CPP), wherein at least one CPP comprises at least three arginines (3R) or analogs thereof, and at least one CPP comprises at least three amino acids having a hydrophobic side chain selected from naphthylalaine (Nal), 3-(3-benzothienyl)-alanine (Bta), phenylglycine (Phg), homophenylalanine (HPhe), phenylalanine (Phe/F), tryptophan (Trp/W), or tyrosine (Tyr/Y).
Pei’648 (WO2018089648) teaches compounds comprising bicyclic peptides having the formula of 1-12 (see p. 50-51), wherein a first cyclic peptide comprises a CPP (Xm) and a second cyclic peptide comprises a cargo peptide sequence (Xn), wherein the Xm comprises 4 or more amino acids, and includes WWWRRRR (SEQ ID NO:143) or WWWRRR (SEQ ID NO:146), FFFRRR (SEQ ID NO:109), FFFRRR (SEQ ID NO:120), FfFRrR (SEQ ID NO:132), fFfRrR (SEQ ID NO:134), FfFrRr (SEQ ID NO:135), fFFФrRr (SEQ ID NO:136), fФfrRr (SEQ ID NO:137), ФFfrRr (SEQ ID NO:138) (i.e. W=tryptophan; R=L-arginine; r=D-arginine Ф=naphthylalanine; F=L-phenylalanine; f=D-phenylalanine) (See the sequence alignment below; p. 60-62, Table 2; p. 64-68), which comprises at least 3R and at least 3 amino acids having a hydrophobic side chain including naphthylalanine, phenylalanine, tryptophan or comprising WWWRRR (instant SEQ ID NO:123) or WWWRRRR (instant SEQ ID NO:117) as recited in claims 36-50 and 52 or a sequence shown in Table D recited in claim 51 (e.g. instant SEQ ID NO:16 or 17); and wherein the compounds also comprise a detectable moiety including a fluorescent protein as in claim 53-59 (see p.79) or a therapeutic moiety including an enzyme, or an antibody or GFP, PTP1B as in claims 53-59 (see p. 82, p. 84; p. 87 ).Thus, the compounds disclosed by Pei’648 meet the limitations recited in claims 36-59. Accordingly, claims 36-59 are anticipated by Pei’648 (WO2018089648).
The sequence search results disclose as follows:
SEQ ID NO:136/SEQ ID NO:117/SEQ ID NO:123
BFH28580
(NOTE: this sequence has 4 duplicates in the database searched.
See complete list at the end of this report)
ID BFH28580 standard; peptide; 7 AA.
XX
AC BFH28580;
XX
DT 12-JUL-2018 (first entry)
XX
DE Bicyclic peptide constructing cell penetrating peptide, SEQ ID 143.
XX
KW antiinflammatory; autoimmune disease; cytostatic; drug delivery;
KW immunosuppressive; inflammatory disease; neoplasm;
KW prophylactic to disease; protein production; protein therapy;
KW therapeutic.
XX
OS Unidentified.
XX
CC PN WO2018089648-A2.
XX
CC PD 17-MAY-2018.
XX
CC PF 09-NOV-2017; 2017WO-US060881.
XX
PR 09-NOV-2016; 2016US-0419781P.
PR 22-NOV-2016; 2016US-0425550P.
PR 22-DEC-2016; 2016US-0438141P.
XX
CC PA (OHIO-) OHIO STATE INNOVATION FOUND.
XX
CC PI Pei D, Qian Z;
XX
DR WPI; 2018-38796M/42.
XX
CC PT New bicyclic peptide, for preparing pharmaceutical composition for
CC PT treating inflammatory disorder, autoimmune disorder, or disorder of
CC PT uncontrolled cellular proliferation; and for delivering therapeutic agent
CC PT to cytoplasm of cell.
XX
CC PS Claim 7; SEQ ID NO 143; 166pp; English.
XX
CC The present invention relates to a novel bicyclic peptide, useful in
CC preparing a pharmaceutical composition for treating inflammatory
CC disorder, autoimmune disorder or disorder of uncontrolled cellular
CC proliferation. The invention also provides: a pharmaceutical composition
CC comprising the bicyclic peptide and a pharmaceutical carrier; a method
CC for treating the inflammatory disorder, autoimmune disorder or disorder
CC of uncontrolled cellular proliferation by administering the bicyclic
CC peptide to a subject identified as having a need for treatment of the
CC disorder; a method for making the bicyclic peptide; and a method for
CC delivering a therapeutic agent to cytoplasm of a cell. The present
CC sequence represents a cell penetrating peptide sequence, which is used in
CC constructing the bicyclic peptide involved in preparing the
CC pharmaceutical composition for treating the above mentioned diseases.
XX
SQ Sequence 7 AA;
Query Match 67.9%; Score 53; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 3 WWWRRRR 9
|||||||
Db 1 WWWRRRR 7
Claims 36-44, 46, 48-51 and 53-59 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Pei’691(WO2015/179691, published Nov 26, 2015, priority May 21, 2014).
Pei’691 (WO2015/179691) teaches a compound comprising a CPP moiety and a cargo moiety and having the formula of II, IIa-IIc, wherein the cargo moiety is cyclic (i.e. a loop protein) and the CPP is cyclic to form a fused bicyclic system (abstract; p. 15-16; p. 23; p. 28; p. 30; p. 33-40), wherein the CPP comprises AA1-AA9 and includes 6-8,.. 6-12 amino acids; and wherein the CPP includes CPP comprising at least 3 arginines (3R) or analogs thereof and at least one amino acid comprising napthylalanine, tryptophan, phenylalanine, phenylglycine or analogues or derivatives thereof, and includes FfФRrRrQ, FFФRRRRQ, RFRFRФRQ (see p. 18, Table 2), which comprises a sequence shown in Table D as in claims 48-51 (e.g. instant SEQ ID NO:16 or 17); and wherein the cargo moiety includes a detectable moiety such as a fluorescent protein (which comprises different loop regions) as in claim 53-59 (p. 21; p. 23; p. 28) or a therapeutic moiety such as an enzyme, or an antibody or GFP, PTP1B (which comprises different loop regions) as in claims 53-59 (see abstract; p. 23; p. 28; p. 30; p. 33-40).Thus, the compound disclosed by Pei’691 meets the limitations recited in claims 36-38, 40-44, 46, 48-51 and 53-59. Accordingly, claims 36-38, 40-44, 46, 48-51 and 53-59 are anticipated by Pei’691 (WO2015/179691).
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Claim Rejections - 35 USC § 103
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 of this title, 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 set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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 45, 47 and 51-52 are rejected under 35 U.S.C. 103 as being unpatentable over Pei’648 (WO2018089648) in view of Gait et al. (WO2015022504, published Feb 19, 2015, priority Aug 8, 2014).
Pei’648 is set forth above but does not explicitly teach that the CCP comprises RRRWWW (SEQ ID NO:124) or RRRRWWW (instant SEQ ID NO:118) as in claims 45, 47, 51 or 52.
Gait et al. (WO2015022504) teaches a peptide-cargo conjugate comprising a cell penetrating peptide (CPP) and a cargo molecule including a cyclic peptide, an antibody or an antibody mimic, wherein the CPP comprises the sequence of -RRRRWWW- (i.e. instant SEQ ID NO:118) which comprises -RRRWWW-(instant SEQ ID NO:124) (see the sequence alignment below; abstract; p. 9; p. 11; p. 15; p. 23-26; figure 13, LB2_58).
A person of ordinary skill in the art would have recognized that selecting and applying the known CPP sequence comprising RRRRWWW (instant SEQ ID NO:118) or RRRWWW (instant SEQ ID NO:124) and the known technique disclosed by Gait to the compound of Pei’648 would have yielded the predictable result of generation of a compound or looped protein comprising a loop of an enzyme, or an antibody or GFP, PTP1B (which comprises different loop regions) and a CPP comprising the sequence of instant SEQ ID NO:118 or 124, and resulted in an improved product because the CPP sequence comprising RRRRWWW (instant SEQ ID NO:118) or RRRWWW (instant SEQ ID NO:124) has been used for generation of a CPP-a cargo molecule conjugate to deliver the cargo molecule including therapeutic agents.
Using the known CPP sequence comprising RRRRWWW (instant SEQ ID NO:118) or RRRWWW (instant SEQ ID NO:124) in the compound of Pei’648 would generate the claimed looped protein comprising a loop and a CPP comprising the sequence of instant SEQ ID NO:118 or 124, and expand application of the compound of Pei’648 in pharmaceutical purposes for drug screening, diagnosis and for better cell penetration and delivery of therapeutic treatment.
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to select and apply the known CPP sequence comprising RRRRWWW (instant SEQ ID NO:118) or RRRWWW (instant SEQ ID NO:124) and the known technique disclosed by Gait to the compound of Pei’648 to provide better cell penetration and delivery of therapeutic treatment or diagnosis, and yield the predictable result of a compound or looped protein comprising a loop of an enzyme, or an antibody or GFP, PTP1B (which comprises different loop regions) and a CPP comprising the sequence of instant SEQ ID NO:118 or 124.
The sequence search results disclose as follows:
SEQ ID NO:170/SEQ ID NO:118/SEQ ID NO:124
BBU95134
(NOTE: this sequence has 5 duplicates in the database searched)
ID BBU95134 standard; peptide; 12 AA.
XX
AC BBU95134;
XX
DT 09-APR-2015 (first entry)
XX
DE Cell penetrating peptide (CPP)-library peptide LB2_58, SEQ ID:118.
XX
KW peptide library; peptide-cargo conjugate; screening.
XX
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Modified-site 1
FT /note= "Coupled to 4-pentynoic acid"
FT Modified-site 12
FT /note= "C-terminal amide"
XX
CC PN WO2015022504-A2.
XX
CC PD 19-FEB-2015.
XX
CC PF 08-AUG-2014; 2014WO-GB052439.
XX
PR 12-AUG-2013; 2013GB-00014411.
XX
CC PA (MRCX ) MEDICAL RES COUNCIL.
XX
CC PI Gait MJ, Deuss PJ, Odonovan E, O'donovan E;
XX
DR WPI; 2015-13548L/17.
XX
CC PT Forming peptide-cargo conjugate, by contacting peptide with cargo
CC PT construct comprising cargo molecule, partitioning peptide-cargo construct
CC PT conjugate from unreacted peptide, and releasing peptide-cargo conjugate
CC PT from tag.
XX
CC PS Example 1; SEQ ID NO 118; 104pp; English.
XX
CC The present invention relates to a method for forming a peptide-cargo
CC conjugate, the conjugate comprises a peptide bonded to a cargo molecule.
CC The method involves: (i) preparing a plurality of peptides each attached
CC to a first functional group at the N- or C- terminus, (ii) preparing a
CC plurality of cargo constructs each comprising a cargo molecule attached
CC to a second functional group, where the cargo molecule comprises a tag,
CC (iii) contacting a peptide attached to a first or second functional
CC groups at the N- or C-terminus with a cargo construct comprising a cargo
CC molecule attached to a second functional group, where the cargo molecule
CC comprises a tag, under conditions that allow reaction between the
CC functional groups to form a bond between the respective peptide and cargo
CC molecule, thereby forming a plurality of peptide-cargo construct
CC conjugates in which the cargo molecule is bonded to the N-or C-terminus
CC of the peptide, (iv) partitioning the peptide-cargo construct conjugate
CC from unreacted peptide by binding the tag to a capture element, (iv)
CC exposing the peptide-cargo construct conjugates to several capture
CC elements allowing the tag to associate with the capture element, and (v)
CC releasing the peptide-cargo conjugates from their respective tags. The
CC peptide is a cell penetrating peptide (CPP; sometimes called membrane
CC translocating peptides or cell delivery peptides), or a candidate cell
CC penetrating peptide, and the cargo molecule is a peptide nucleic acid
CC (PNA), phosphorodiamidate morpholino oligonucleotide (PMO), locked
CC nucleic acid (LNA), or small interfering RNA (siRNA). The invention
CC further discloses: (1) a method for generating library of peptide-cargo
CC conjugates; (2) a method for screening several peptide-cargo conjugates
CC for functional property of the peptide-cargo conjugate, which involves
CC simultaneously assaying several different peptide-cargo conjugates for
CC the functional property; (3) a library of peptide-cargo conjugates
CC comprising several containers each containing a quantity of an isolated
CC or substantially purified peptide-cargo conjugate; (4) a peptide-cargo
CC construct conjugate; and (5) several peptide-cargo construct conjugates
CC immobilized on solid support through association of a tag with a capture
CC element. The methods of the invention are simple, rapid and suitable for
CC high-throughput synthesis of conjugates for screening purpose. The
CC present sequence represents a cell penetrating peptide (CPP)-library
CC peptide LB2_58 comprising a N-terminal alkyne linker and conjugation to
CC N3-PNA705-S-S-biotin, which is analyzed by MALDI-TOF mass-spectrometry.
XX
SQ Sequence 12 AA;
Query Match 74.6%; Score 53; Length 12;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 2 RRRRWWW 8
|||||||
Db 1 RRRRWWW 7
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 filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual 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/apply/applying-online/eterminal-disclaimer.
Claims 36-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 6-7, 10-12, 17-22 of U.S. Patent No. 10626147 (the ‘147 Patent), claims 16-27, 36-40 of U.S. Patent No. 10815276 (the ‘276 patent), claims 8-20, 23-34 and 41 of U.S. Patent No. 11225506 (the ‘506 patent), or claims 1-4, 12-18 of U.S. Patent No. 11878046 (the ‘046 patent). Although the claims at issue are not identical, they are not patentably distinct from each other because the bispecific peptide of the ‘147, the 276, the ‘506 and the ‘046 patents anticipate instant claims.
Claims 6-7, 10-12, 17-22 of US10626147 (the ‘147 Patent) claim a cyclic peptide comprising formula IIa, IIb or IIc comprising a CPP fused to a cargo moiety, wherein the CPP comprises AA1-AA9 including AA1 is L-phenylalanine, AA2 is D-phenylalanine, AA3 is L-naphthylalanine, AA4 is L-arginine, AA5 is D-arginine, AA6 is L-arginine, and wherein the cargo moiety comprises a detectable moiety, a therapeutic moiety, a targeting moiety or a combination thereof, which meet the limitations recited in instant claims because the claims of the ‘147 patent are a species of instant claims and thus anticipate instant claims.
Claims 16-27 and 36-40 of US10815276 (the ‘276 patent) claim a cyclic peptide comprising formula IIa, IIb or IIc comprising a CPP fused to a cargo moiety, wherein the CPP comprises AA1-AA9 including AA1 is L-phenylalanine, AA2 is D-phenylalanine, AA3 is L-naphthylalanine, AA4 is L-arginine, AA5 is D-arginine, AA6 is L-arginine, and wherein the cargo moiety comprises a detectable moiety, a therapeutic moiety, a targeting moiety or a combination thereof, which meet the limitations recited in instant claims because the claims of the ‘276 patent are a species of instant claims and thus anticipate instant claims.
Claims 8-20, 23-34 and 41 of US11225506 (the ‘506 patent) claim a peptide comprising the formula I (AA1-AA9) and a cargo moiety, including AA1 is L-phenylalanine, AA2 is D-phenylalanine, AA3 is L-naphthylalanine, AA4 is L-arginine, AA5 is D-arginine, AA6 is L-arginine, and wherein the cargo moiety comprises a detectable moiety, a therapeutic moiety, a targeting moiety or a combination thereof, which meet the limitations recited in instant claims because the claims of the ‘506 patent are a species of instant claims and thus anticipate instant claims.
Claims 1-4, 12-18 of US11878046 (the ‘046 patent) claim a bispecific peptide comprising a first cyclic peptide and a second cyclic peptide, wherein the first cyclic peptide comprises AA1-AA9, including AA1 is L-phenylalanine, AA2 is D-phenylalanine, AA3 is L-naphthylalanine, AA4 is L-arginine, AA5 is D-arginine, AA6 is L-arginine, and wherein the second cyclic peptide includes a peptide inhibits at least one protein-protein interaction including PTP1B, which meet the limitations recited in instant claims because the claims of the ‘046 patent are a species of instant claims and thus anticipate instant claims.
Therefore, claims 36-59 of instant Application are not patentably distinct from claims 6-7, 10-12, 17-22 of the ‘147 patent, claims 16-27, 36-40 of the ‘276 patent, claims 8-20, 23-34 and 41 of the ‘506 patent, or claims 1-4, 12-18 of the ‘046 patent, because instant claims 36-59 are anticipated by claims 6-7, 10-12, 17-22 of the ‘147 patent, claims 16-27, 36-40 of the ‘276 patent, claims 8-20, 23-34 and 41 of the ‘506 patent, or claims 1-4, 12-18 of the ‘046 patent.
Claims 36-59 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 2, 6 and 50-52 of copending Application No. 18/278259 (the ‘259 Application), claims 1 and 5-20 of copending Application No. 18/734759 (the ‘759 Application), claims 1-22 of copending Application No.18/847105 (the ‘105 Application), or claims 1-5, 9-15, 17-19 and 22-26 of copending Application No.18/862643 (the ‘643 Application). Although the claims at issue are not identical, they are not patentably distinct from each other because the compound or the cyclic peptide coupled to a cargo moiety recited in claims of the ‘259 Application and the ‘759 Application meets the limitations recited in instant claims and thus anticipate instant claims.
Claims 1, 2, 6 and 50-52 of Application No. 18/278259 (the ‘259 Application) claim a cyclic peptide coupled to a cargo moiety selected from a detectable moiety, a therapeutic moiety, a targeting moiety or a combination thereof, and wherein the CPP comprises at least three or four arginines and at least three amino acids having a hydrophobic side chain selected from L-3-benzaothienylalanine, L-1-naphthylalanine, L/D-Phenylalanine, including the amino acids recited in claim 46, which meet the claimed CPP recited in instant claims. The claims of the ’259 Application are a species of instant claims and thus anticipate instant claims.
Claims 1 and 5-20 of Application No. 18/734759 (the ‘759 Application) claim a compound comprising Formula II comprising a CPP of formula I-linked to a cargo, wherein the CPP comprises three or more amino acids that are arginine, at least one amino acid is napthylalanine, tryptophan, or phenylalanine or derivative or analogue thereof and wherein the cargo moiety comprises a detectable moiety, a therapeutic moiety, a targeting moiety or a combination thereof; and wherein the CPP includes FFФRrRrQ (SEQ ID NO:16), FFФRRRRQ (SEQ ID NO:17), which meets the CPP recited in instant claims. The claims of the ‘759 Application are a species of instant claims and thus anticipate instant claims.
Claims 1-22 of Application No.18/847105 (the ‘105 Application) claim a peptide comprising a membrane translocation domain having at least one or more CPP motifs, wherein the at least one or more CPP motif is 3-10 or 2-8 amino acid residue in length and has at least two hydrophobic residues and wherein the transmembrane domain includes human fibronectin type III having BC, DE, CD and FG loops and one or more of the BC, DE, CD and FG loops have CPP motifs, and wherein the CPP motifs include RRRWWW or WWWRRR, which meets the claimed looped protein recited in instant claims. The claims of the ‘105 Application are a species of instant claims and thus anticipate instant claims.
Claims 1-5, 9-15, 17-19 and 22-26 of Application No.18/862643 (the ‘643 Application claim a peptide comprising a membrane translocation domain having at least one or more CPP motifs, and a cargo moiety linked to the membrane translocation domain, wherein the cargo moiety comprises a plant bioactive moiety, wherein the at least one or more CPP motif is 3-10 or 2-8 amino acid residue in length and has at least two hydrophobic residues and wherein the transmembrane domain includes human fibronectin type III having BC, DE, CD and FG loops and one or more of the BC, DE, CD and FG loops have CPP motifs, and wherein the CPP motifs include RRRWWW or WWWRRR, which meets the claimed looped protein recited in instant claims. The claims of the ‘643 Application are a species of instant claims and thus anticipate instant claims.
Therefore, claims 36-59 of instant Application are not patentably distinct from claims 1, 2, 6 and 50-52 of the ‘259 Application, claims 1 and 5-20 of the ‘759 Application, claims 1-22 of the ‘105 Application, or claims 1-5, 9-15, 17-19 and 22-26 of the ‘643 Application because instant claims 36-59 are anticipated by claims 1, 2, 6 and 50-52 of the ‘259 Application, claims 1 and 5-20 of the ‘759 Application, claims 1-22 of the ‘105 Application or claims 1-5, 9-15, 17-19 and 22-26 of the ‘643 Application.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
NO CLAIM IS ALLOWED.
Sequence alignment
SEQ ID NO:170 1 IRRRRWWWGSV 11
SEQ ID NO:143 1 PRRRRWWWHGP 11
SEQ ID NO:139 1 KRRRRWWWKE- 10
SEQ ID NO:118 1 -RRRRWWW--- 7
SEQ ID NO:124 1 –RRRWWW---- 6
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Chen(PhD Dissertation: Intracellular Protein Delivery by Genetically Encoded And Structurally constrained Cell-Penetrating peptides, 2019, Graduate Program in Chemistry, The Ohio State University) teaches looped proteins comprising a loop and a CPP (p. 23, table 2), wherein the looped proteins include EGFP mutants, Purine nucleoside phosphorylase (PNP) mutants or GFP-binding nanobody (GBN) mutants (p. 11, Table 1, cyclo-FΦRRRQ as CPP and GFP and PTP1B as cargo); wherein the EGFP mutants comprise insertion of CPP into a solved exposed loop of EGFP (p. 25-27; p. 28-31) and include EGFP-W3R3, EGFP-R3W3, EGFP-R4W3 (p. 28, table 3; p. 42-43); the PNP mutants comprise insertion of CPP into His20-Pro25, Asn74-Gly75, and Gly182-Leu187 of the PNP (p. 32-38, table 4; p. 44-46); the GBN mutants comprise insertion of a CPP into non-CDR loops, CDR1 and CDR3 loops of GBN (see p.p. 68-88, Table 9).
JP2005185101 teaches a transcription factor comprising -RRRRWWW (instant SEQ ID NO:118)- or -RRRWWW- (instant SEQ ID NO:124) (see the sequence alignment below).
SEQ ID NO:118: -RRRRWWW-
SEQ ID NO:124: -RRRWWW-
AQD45100
ID AQD45100 standard; protein; 98 AA.
XX
AC AQD45100;
XX
DT 12-JUN-2008 (first entry)
XX
DE Rice cDNA-encoded protein SEQ ID No 38959.
XX
KW plant; transgenic plant; crop improvement.
XX
OS Oryza sativa.
XX
CC PN JP2005185101-A.
XX
CC PD 14-JUL-2005.
XX
CC PF 11-DEC-2002; 2002JP-00383870.
XX
PR 30-MAY-2002; 2002JP-00203269.
XX
CC PA (DOKU-) DOKURITSU GYOSEI HOJIN NOGYO SEIBUTSU SH.
CC PA (SEIB-) SEIBUTSUKEI TOKUTEI SANGYO GIJUTSU.
CC PA (DOKU-) DOKURITSU GYOSEI HOJIN RIKAGAKU KENKYUSH.
CC PA (KOKU-) ZH KOKUSAI KAGAKU SHINKO ZAIDAN.
XX
CC PI Kikuchi H, Hayashizaki Y, Otomo Y, Matsubara K, Murakami K;
CC PI Kishimoto N, Sato K, Nagata T, Kawakami N, Yazaki J, Ishikawa M;
CC PI Doi K, Kawai J;
XX
DR WPI; 2005-566181/58.
XX
CC PT Novel DNA encoding transcription factor, derived from rice plant, useful
CC PT for obtaining transcriptional-regulatory regions in plant and for
CC PT producing modified plant.
XX
CC PS Claim 1; SEQ ID NO 38959; 2928pp; Japanese.
XX
CC The present invention relates to Rice cDNA clones and to: DNA encoding an
CC antisense RNA that is complementary to the transcription product of the
CC cDNA; a DNA encoding an RNA having ribozyme activity that cleaves
CC specifically the transcription product of the cDNA; DNA encoding an RNA
CC that suppresses the expression of cDNA through RNA interference effect at
CC the time of the expression in a plant cell; or a DNA encoding RNA that
CC suppresses the expression of the cDNA through co-suppression effect at
CC the time of expression in a plant cell; a vector containing the cDNA or
CC DNA encoding a interference RNA; a transformed plant cell the vector; a
CC transformed plant the plant cell; an offspring, a clone or a reproductive
CC fragment of the plant; a protein encoded by the cDNA; an antibody binding
CC to the protein encoded by the cDNA; a rice-genome database containing a
CC cDNA or protein sequence of the invention; and a method for determining
CC transcriptional-regulatory regions by mapping a base sequence chosen from
CC the cDNA sequences of the invention and determining the transcriptional-
CC regulatory region in the mapped region and in the 5'-terminal. The DNA
CC sequences, proteins, vectors, plants, antibodies, databases and methods
CC of the invention are useful for: producing the protein of the invention,
CC for producing transgenic plants, for controlling the expression of a gene
CC in a plant ,and for producing a modified plant with desired and different
CC characteristics. The present sequence is a protein encoded by a cDNA
CC clone of the invention.
XX
SQ Sequence 98 AA;
Query Match 83.8%; Score 57; Length 98;
Best Local Similarity 77.8%;
Matches 7; Conservative 2; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KRRRRWWWK 9
:|||||||:
Db 80 RRRRRWWWR 88
WO2016187508 teaches a tumor-specific mutation containing human derived polypeptide comprising -WWWRRRR (instant SEQ ID NO:117)- or -WWWRRR- (instant SEQ ID NO:123) (see the sequence alignment below).
SEQ ID NO:117: -WWWRRRR-
SEQ ID NO:123: -WWWRRR-
BDJ76923
ID BDJ76923 standard; protein; 38 AA.
XX
AC BDJ76923;
XX
DT 12-JAN-2017 (first entry)
XX
DE Tumor-specific mutation containing human derived polypeptide, SEQ: 3102.
XX
KW cancer; chemotherapy; cytostatic; immune stimulation; immunotherapy;
KW mutein; prophylactic to disease; surgery; therapeutic;
KW vaccine, anticancer.
XX
OS Homo sapiens.
OS Synthetic.
XX
CC PN WO2016187508-A2.
XX
CC PD 24-NOV-2016.
XX
CC PF 20-MAY-2016; 2016WO-US033452.
XX
PR 20-MAY-2015; 2015US-0179877P.
PR 23-FEB-2016; 2016US-0389377P.
XX
CC PA (BROA-) BROAD INST INC.
CC PA (DAND ) DANA FARBER CANCER INST INC.
CC PA (GEHO ) GEN HOSPITAL CORP.
XX
CC PI Fritsch EF, Hacohen N, Rooney MS, Shukla SA;
XX
DR WPI; 2016-72379L/83.
XX
CC PT Pharmaceutical composition useful as immunogenic composition for
CC PT preventing or treating tumor, comprises neoantigenic peptide comprising
CC PT tumor-specific neoepitope capable of binding to human leukocyte antigen
CC PT (HLA) protein, and carrier.
XX
CC PS Example 4; SEQ ID NO 3102; 473pp; English.
XX
CC The invention relates to a novel pharmaceutical composition useful for
CC preventing or treating a tumor in a subject. The composition comprises at
CC least one neoantigenic peptide: (a) containing a tumor-specific mutation;
CC (b) containing a tumor-specific neoepitope capable of binding to a human
CC leukocyte antigen (HLA) protein in the subject; and (c) capable of
CC eliciting an immune response against a tumor. The pharmaceutical
CC composition herein is an immunogenic or a vaccine composition, used in
CC combination with an additional therapy for prophylactic cancer treatment.
CC The additional therapy is surgery, chemotherapy, or a targeted therapy.
CC The present sequence represents a human derived polypeptide comprising a
CC tumor-specific mutation, useful for preparing the pharmaceutical
CC composition.
XX
SQ Sequence 38 AA;
Query Match 69.2%; Score 54; Length 38;
Best Local Similarity 87.5%;
Matches 7; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 2 QWWWRRRR 9
:|||||||
Db 23 RWWWRRRR 30
US2007214517 teaches a polypeptide from Arabidopsis, soybean, maize, wheat or rice comprising -WWWRRRR (instant SEQ ID NO:117)- or -WWWRRR- (instant SEQ ID NO:123) (see the sequence alignment below).
SEQ ID NO:117: -WWWRRRR-
SEQ ID NO:123: -WWWRRR-
ARN11445
(NOTE: this sequence has 1 duplicate in the database searched)
ID ARN11445 standard; protein; 150 AA.
XX
AC ARN11445;
XX
DT 07-AUG-2008 (first entry)
XX
DE Zea mays subsp. mays amino acid sequence SEQ ID 110816.
XX
KW plant; plant breeding; gene regulation; DNA detection; mapping.
XX
OS Zea mays subsp. mays.
XX
CC PN US2007214517-A1.
XX
CC PD 13-SEP-2007.
XX
CC PF 02-MAR-2007; 2007US-00713768.
XX
PR 13-FEB-2004; 2004US-0544190P.
PR 14-FEB-2005; 2005US-00056355.
XX
CC PA (CERE-) CERES INC.
XX
CC PI Alexandrov N, Brover V;
XX
DR WPI; 2008-B58774/11.
XX
CC PT New isolated nucleic acids and polypeptides from Arabidopsis, soybean,
CC PT maize, wheat, and rice, useful for controlling the behavior of a gene in
CC PT the chromosome, controlling the expression of a gene, or as tools for
CC PT genetic mapping.
XX
CC PS Claim 11; SEQ ID NO 110816; 122pp; English.
XX
CC The invention relates to an isolated nucleic acid molecule which
CC comprises (a) a full-length cDNA nucleic acid, or (b) a nucleic acid,
CC which is the reverse of the nucleotide sequence of (a), where the
CC sequences are described in the Sequence Listing which is available in
CC electronic form from the USPTO website. Also described: (1) a vector
CC construct comprising: (a) a first nucleic acid having a regulatory
CC sequence capable of causing transcription and/or translation; and (b) a
CC second nucleic acid having the sequence of the isolated nucleic acid
CC molecule above, where the first and second nucleic acids are operably
CC linked and where the second nucleic acid is heterologous to any element
CC in the vector construct; (2) a host cell comprising the isolated nucleic
CC acid molecule or the vector construct, where the nucleic acid molecule is
CC flanked by exogenous sequence; (3) an isolated polypeptide comprising an
CC amino acid sequence: (a) exhibiting at least 40-90% sequence identity of
CC an amino acid sequence encoded by a sequence in the Sequence Listing or
CC the Sequence Listing-Miscellaneous Feature documents, or a fragment; and
CC (b) capable of exhibiting at least one of the biological activities of
CC the polypeptide encoded by the nucleotide sequence in the Sequence
CC Listing or the Sequence Listing-Miscellaneous Feature documents, or a
CC fragment; (4) an antibody capable of binding the isolated polypeptide;
CC (5) a method of introducing an isolated nucleic acid into a host cell;
CC (6) a method for detecting a nucleic acid in a sample; (7) a plant or
CC cell of a plant comprising a nucleic acid molecule, which is exogenous or
CC heterologous to the plant or plant cell; (8) a plant or cell of a plant
CC comprising the vector construct; and (9) a plant, which has been
CC regenerated from a plant cell above. Specifically claimed are over 100000
CC isolated polynucleotides and their encoded polypeptides from Arabidopsis,
CC soybean, maize, wheat, and rice. The nucleic acids are useful for
CC specifying a gene product in cells, either as a promoter or as a protein
CC coding sequence or as an UTR or as a 3' termination sequence, and are
CC also useful in controlling the behavior of a gene in the chromosome, in
CC controlling the expression of a gene, or as tools for genetic mapping,
CC recognizing or isolating identical or related DNA fragments, or
CC identification of a particular individual organism, or for clustering of
CC a group of organisms with a common trait. The present sequence represents
CC a specifically claimed sequence-determined DNA fragment encoded amino
CC acid sequence from the present invention.
XX
SQ Sequence 150 AA;
Query Match 70.5%; Score 55; Length 150;
Best Local Similarity 88.9%;
Matches 8; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 3 WWWRRRRND 11
||||||| |
Db 42 WWWRRRRWD 50
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHANG-YU WANG whose telephone number is (571)272-4521. The examiner can normally be reached on Monday-Thursday, 7:00am-5:00pm EST.
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, Jeffrey Stucker can be reached on 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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Chang-Yu Wang
December 30, 2025
/CHANG-YU WANG/Primary Examiner, Art Unit 1675