DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims Status
Claims 1-20 are pending.
Information Disclosure Statement
Currently there are no information disclosure statements in this application.
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-12 in the reply filed on 12/29/2025 is acknowledged.
Applicant’s election without traverse of the following species:
First or second linker peptide SEQ ID NO species: SEQ ID NO: 153
Signal domain SEQ ID NO species : SEQ ID NO: 155
ED domain SEQ ID NO species : SEQ ID NO: 16
Membrane-associated ED protein or vesicle targeting protein SEQ ID NO species: SEQ ID NO: 111
Signal domain species: myristoylation signal domain and BIP secretion domain
Species of protein family comprising myristoylation signal domain: MARCKS in the reply filed on 12/29/2025 is acknowledged.
Claims 13-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected subject matter, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 12/29/2025.
Specification
The disclosure is objected to because of the following informalities:
Figure 5 does not contain SEQ ID NOs. for the listed sequences. SEQ ID NOs. for the sequences should be listed either in the figure itself or in its description.
Appropriate correction is required.
Claim Objections
Claim 1 objected to because of the following informalities:
Claim 1 recites “a membrane associated-ED protein. The abbreviation for ED should be defined after the abbreviation is first recited. Currently, it is defined after the recitation of “an effector domain (ED) but would be more appropriate if “ED” is defined after recitation of “membrane associated-ED”. Additionally, it is recommended that in the recitation of “an effector domain (ED) domain”, the underlined domain term should be removed as it is repetitive. Appropriate correction is required.
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 1-12 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 1 ( and claims 2-12 dependent on) recites (a) and (b) but it in the current written form, it is unclear what the relationship of (a) or (b) is to the preamble of the claim. The recitation of (a) does not further limit the preamble of the claim. For the purpose of advancing prosecution, the Examiner is interpreting the claim as a membrane associated-ED protein that comprises a signal domain that is linked to an effector domain.
Claim 1 (and claims 2-4, 8-12 dependent on) recites “an effector domain” but it is unclear as to what defines or encompasses an effector domain as the specification states that the vesicle targeting protein comprises a signal domain and an effector domain (ED) (see paragraph 0027, pg. 8) and does not define any further functional features that an effector domain contains. Therefore, claim 1 and claims 2-4, 8-12 dependent on are rendered indefinite. For the purpose of advancing prosecution, the Examiner is defining an effector domain as encompassing any or all portions of a functional part of the protein.
Claim 11 recites “a curvature sensing domain”. It is unclear what falls within the scope of a curvature sensing domain or what defines a curvature sensing domain as the specification states that the membrane associated-ED protein further comprises a curvature sensing domain on the C-terminus or N-terminus of the membrane associated-ED protein or is a linker peptide between the signal domain and the ED domain or comprises a SNX-1 curvature sensing domain. There is no definition beyond this description that describes structural or function properties that are attributed to the domain and therefore, the claim is rendered indefinite.
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 2, 5 and 8 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 2 is directed to all possible “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38. The specification however, only provides a representative species of a membrane associated-ED protein of claim 1 wherein the signal domain has an amino acid sequence comprising SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38. There is no disclosure of any particular structure to function/activity relationship in the disclosed species.
Claim 5 is directed to all “membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38. The specification however, only provides a representative species of a membrane-associated-ED protein of claim 1, wherein the ED domain has an amino acid sequence comprising SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38. There is no disclosure of any particular structure to function/activity relationship in the disclosed species.
Claim 8 is directed to all “membrane associated-ED proteins of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising 70% sequence similarity to SEQ ID NO: 111. The specification however, only provides a representative species of a membrane associated-ED protein that has an amino acid sequence comprising SEQ ID NO: 111. There is no disclosure of any particular structure to function/activity relationship in the disclosed species.
Signal transduction originates at the membrane, and the clustering of signaling proteins is a key step in transmitting messages. The molecular mechanism of signaling proteins and membranes is difficult to study and their influence on signaling is only understood at the most rudimentary level (see Groves et. al. (Nature Structural Biology, Vol. 17, pg. 659-665, published May 23, 2010, cited on the attached PTO-892). The specification also fails to describe additional representative species of these proteins by identifying structural characteristics or properties for which no predictability of structure is apparent.
Regarding the level of skill and knowledge in the art of amino acid mutation, the reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached PTO-892) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see pg. 7, column 1, top). Also, the unpredictability associated with amino acid mutations is exemplified by the reference of Zhang et al. (Structure 26: 1474-1485, 2018; cited on the attached Form PTO-82) which discloses that even a mutation of a surface residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1).
Given this lack of additional representative species as encompassed by the claims, Applicants have failed to sufficiently describe the claimed invention, in such full, clear, concise, and exact terms that a skilled artisan would recognize Applicants were in possession of the claimed invention.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Claims 2, 5 , and 8 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Claim 2 is 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 a membrane-associated-ED protein of claim 1 wherein the signal domain has an amino acid sequence comprising SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38, does not reasonably provide enablement for all possible “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38.. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Claim 5 is 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 a “membrane-associated-ED protein of claim 1, wherein the ED domain has an amino acid sequence comprising SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38, does not reasonably provide enablement for all “membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Claim 8 is 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 a “membrane associated-ED protein of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising SEQ ID NO: 111, does not reasonably provide enablement for all “membrane associated-ED proteins of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising 70% sequence similarity to SEQ ID NO: 111. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required, are summarized in In re Wands (858 F.2d 731, 8 USPQ 2nd 1400 (Fed. Cir. 1988)) as follows: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claim(s).
Claim 2 is so broad as to encompass all possible “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38. The scope of the claims is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38 comprising the required recombinant proteins of the membrane associated-ED protein group and variants broadly encompassed by the claims.
Claim 5 is so broad as to encompass all “membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38. The specification however, only provides a representative species of a membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38. The scope of the claims is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38 group and variants broadly encompassed by the claims.
Claim 8 is so broad as to encompass all “membrane associated-ED proteins of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising 70% sequence similarity to SEQ ID NO: 111. The specification however, only provides a representative species of a membrane associated-ED protein that has an amino acid sequence comprising SEQ ID NO: 111. The scope of the claims is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of “membrane associated-ED proteins encompassed by the claims.
The claims rejected under this section of U.S.C. 112, first paragraph, place minimal structural limits on the required variant polypeptides encompassed by the claims. Since the amino acid sequence of a protein determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. However, in this case the disclosure is limited to:
(claim 2) “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38”.
(claim 5) “membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38”.
(claim 8) “membrane associated-ED proteins of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising SEQ ID NO: 111. The specification however, only provides a representative species of a membrane associated-ED protein has an amino acid sequence comprising SEQ ID NO: 111”.
.
While recombinant and mutagenesis techniques are known, it is not routine in the art to screen for multiple substitutions or multiple modifications, as encompassed by the instant claims, and the positions within a protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
The specification does not support the broad scope of the claims which encompass any possible:
(claim 2) “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38”;
(claim 5) “membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38”;
(claim 8) “membrane associated-ED proteins of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising 70% sequence similarity to SEQ ID NO: 111”
because the specification does not establish: (A) regions of the polypeptide which may be modified effecting membrane associated-ED protein; (B) the general tolerance of enzymes of the membrane associated-ED protein group to modification and extent of such tolerance; (C) a rational and predictable scheme for modifying any amino acid residue of a protein of the membrane associated-ED protein group with an expectation of obtaining the desired biological function; and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. Because of this lack of guidance, the extended experimentation that would be required to determine which substitutions would be acceptable to retain the required functions of the membrane associated protein of claim 1 and the fact that the relationship between the sequence of a peptide and its tertiary structure (i.e. its activity) are not well understood and are not predictable (e.g., see Sheng et al, FEBS J., Vol. 24, pg. 4703-13, 2015, Ngo et al. in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495; Franceus et al., J. Ind. Microbiol. Biotechnol. Vol 44, pp 687-695, 2017), it would require undue experimentation for one skilled in the art to arrive at the majority of polypeptides having the function of the membrane associated-ED proteins of the claimed genus.
Thus, applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims broadly including any:
(claim 2) “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38”;
(claim 5) “membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38”;
(claim 8) “membrane associated-ED proteins of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising 70% sequence similarity to SEQ ID NO: 111”.
The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of:
(claim 2) “membrane associated-ED proteins of claim 1 wherein the signal domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 155 with the proviso that the resulting amino acid sequence of the membrane associated-ED protein is not SEQ ID NO: 38”.
(claim 5) “membrane-associated-ED proteins of claim 1, wherein the ED domain has an amino acid sequence comprising at least 70% sequence similarity to SEQ ID NO: 16 with the proviso that the resulting amino acid sequence of the membrane associated -ED protein is not SEQ ID NO: 38”.
(claim 8) “membrane associated-ED proteins of claim 1, wherein the membrane associated-ED protein has an amino acid sequence comprising 70% sequence similarity to SEQ ID NO: 111. The specification however, only provides a representative species of a membrane associated-ED protein has an amino acid sequence comprising at least 70%, 90% and 100% sequence similarity to SEQ ID NO: 111” is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Claim Rejections - 35 USC § 102
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 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 1, 5 and 12 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2)as being anticipated by Codiak Biosciences (WIPO International Publication Number WO 2020/101740 A1; published May 22, 2020), hereinafter referred to as Codiak.
With regards to claim 1, Codiak discloses a membrane associated-ED protein comprising an N-terminus domain (ND) and an effector domain (ED) wherein the ND is associated with the luminal surface of an isolated extracellular vesicle (EV) (see claim 1, pg. 122). Codiak further discloses that in some aspects, the ND is associated with the luminal surface of the EV via myristoylation (signal domain) (see Paragraph 00245, pg. 53). Codiak discloses that the ND and ED are joined by a linker (see claim 17, pg. 124). Codiak further discloses that the linker is a peptide and the peptide linker can comprise at least four amino acids (see Paragraph 00256, pg. 55) and that the linker is a glycine/serine linker where the glycine linker can comprise the sequence (GGS)n where n is an integer between 1 and 100. Note that the linker sequence in the current instant application claim 1 is GGSG (SEQ ID NO: 153). See alignment below:
RESULT 1
AASEQ2_04072026_150854
Query Match 72.7%; Score 16; DB 1; Length 3;
Best Local Similarity 100.0%;
Matches 3; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy GGS
|||
Db GGSG
With regards to claim 5, Codiak further discloses a biologically active molecule linked to a scaffold protein wherein the scaffold protein comprises an N-terminal domain and an effector domain that are joined by a linker wherein the N-terminal domain and effector domain are associated with the luminal surface of an extracellular vesicle in which the N-terminal domain is associated with the luminal surface via myristoylation (signal domain) (see paragraph 0036, pg. 8). Codiak further discloses that scaffold protein comprises the sequence of MARCKSL1 (SEQ ID NO: 2) or a fragment or variant thereof (see paragraph 0061, pg. 13). SEQ ID NO: 2 of Codiak comprises the residues KKKKFSFKKPF (see pg. 102) which shares 79.3% sequence identity with SEQ ID NO: 16 of the current instant application (see sequence alignment below).
RESULT 1
AASEQ2_04152026_070059
Query Match 79.3%; Score 46; DB 1; Length 11;
Best Local Similarity 100.0%;
Matches 9; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy KKKKFSFKK
|||||||||
Db KKKKFSFKK
With regards to claim 12, in addition to the teachings of Codiak as applied to claim 1 above, Codiak further discloses that in some embodiments, the ND does not comprise Met at the N-terminus (see Paragraph 00245, pg. 53).
Therefore, claims 1, 5 and 12 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Codiak Biosciences (WIPO International Publication Number WO 2020/101740 A1; published May 22, 2020).
Claims 1-4 are rejected under pre-AIA 35 U.S.C. 102(a)(1) as being anticipated by Uniprot_202601 (Database entry: A0A2K6N575_RHIBE; entry date March 28, 2018), hereinafter referred to as UnitProt_RHIBE.
With regards to claims 1-4, UnitProt_RHIBE discloses the Endoplasmic reticulum chaperone BIP protein which comprises a signal domain (residues 1-18) that shares 100% sequence identity to SEQ ID NO: 155 of the current instant application (see sequence alignment below) that is linked to an effector domain (residues 19-467). UnitProt_RHIBE discloses that the subcellular location of BIP is the endoplasmic reticulum lumen (membrane-associated).
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..467
FT /note="Endoplasmic reticulum chaperone BIP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014462761"
FT COILED 278..305
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 467 AA; 51286 MW; B6B7735C95DF53DA CRC64;
Query Match 100.0%; Score 76; Length 467;
Best Local Similarity 100.0%;
Matches 18; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MKLSLVAAMLLLLSAARA 18
||||||||||||||||||
Db 1 MKLSLVAAMLLLLSAARA 18
Therefore, claims 1-4 are rejected under pre-AIA 35 U.S.C. 102(a)(1) as being anticipated by Uniprot_202601 (Database entry: A0A2K6N575_RHIBE; entry date March 28, 2018).
Claims 1 and 5 are rejected under pre-AIA 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Esser et al. (US Patent Application Publication No: US 2011/0086808; published April 14, 2011), hereinafter referred to as Esser.
With regards to claims 1 and 5, Esser discloses a modified therapeutic agent (protein) (see paragraph 0015, pg. 1) that comprises two or more lipophilic membrane binding domains (see paragraph 0033, pg. 2) that are linked (see paragraph 0042, pg. 3) in which the therapeutic protein has a lipophilic tail that promotes localization of the therapeutic protein to the cellular membrane (signal domain) (see paragraph 0029, pg. 2) and additional membrane binding elements (effector domain) selected from basic amino acid sequences such as SEQ ID NO: 3 (SPSNETPKKKKKRFSFKKSG) (see paragraph 0034, pg. 2) which shares 81% sequence identity with SEQ ID NO: 16 of the current instant application (see sequence alignment below).
SUMMARIES
%
Result Query
No. Score Match Length DB ID Description
----------------------------------------------------------------------------
1 47 81.0 20 1 AASEQ2_04142026_205205
ALIGNMENTS
RESULT 1
AASEQ2_04142026_205205
Query Match 81.0%; Score 47; DB 1; Length 20;
Best Local Similarity 81.8%;
Matches 9; Conservative 1; Mismatches 1; Indels 0; Gaps 0;
Qy KKKKFSFKKFG
|||:||||| |
Db KKKRFSFKKSG
Therefore, claims 1 and 5 are rejected under pre-AIA 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Esser et al. (US Patent Application Publication No: US 2011/0086808; published April 14, 2011).
The prior art made of record and not relied upon is considered pertinent to applicant’s disclosure:
Morton et al. “MARCKS-ED Peptide as a curvature and Lipid Sensor”, ACS Chemical Biology, Vol. 8, pg. 218-225, published January 18, 2013, PMID: 23075500. (teaches a MARCKS-ED peptide that senses membrane curvature).
McConnell et al. US Patent Application Publication No: US 2019/0151456 A1; published May 23, 2019.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to GEORGE T LOUNTOS whose telephone number is (571)272-0502. The examiner can normally be reached Monday-Friday 8:00 am - 5:00 pm.
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/GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652
/RICHARD G HUTSON/Primary Examiner, Art Unit 1652
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