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 25 and 37 are amended.
Claims 10-23, 28-34, 36, 38, 40-50, 52, 54, and 59-60 are canceled.
Claims 1-9, 24-27, 35, 37, 39, 51, 53, and 55-58 are pending.
Information Disclosure Statement
The Applicants have not submitted an information disclosure statement (IDS) for consideration. The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Election/Restrictions
Applicant’s election without traverse of Group 1 (claims 1-9, 24, 26, 39, and 51 in the reply filed on 08/24/2026 is acknowledged. In the interest of compact prosecution and in light of Applicant’s amended amendment of claim 25 to be dependent on Claim 1, the Examiner has rejoined claim 25 to Group 1.
Applicant’s election without traverse of position 26 (Species Group 1) in the reply filed on 08/24/206 is acknowledged. Examiner notes that Applicant did not elect a specific species from Species Group 5, Species Group 6, Species Group 7, Species Group 8, Species Group 9, Species Group 10, or Species Group 58 as requested in the Requirement for Restriction/Election (02/24/2026).
Claims 3-6, 8, 27, 35, 37, 53, and 55-58 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected subject matter, there being no allowable generic or linking claim.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 08/24/2026.
Claim Objections
Claim 9 is objected to because of the following informalities:
Claim 9 is objected to as being dependent upon a rejected base claim. Appropriate correction is required.
Drawings
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the drawings are not identified by sequence identifiers in accordance with 37 CFR 1.821(d). Sequence identifiers for nucleotide and/or amino acid sequences must appear either in the drawings or in the Brief Description of the Drawings. Figure 1 lacks an associated SEQ ID NO.
Required response – Applicant must provide:
Replacement and annotated drawings in accordance with 37 CFR 1.121(d) inserting the required sequence identifiers;
AND/OR
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers into the Brief Description of the Drawings, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Specification
The disclosure is objected to because of the following informalities: Description for Figure 1 lacks a SEQ ID NO. for the sequence.
Appropriate correction is required.
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. (see References). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
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.
Claim 25 is 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.
With regards to claim 25, the claim recites “where the amino acid is SEQ ID NO: 11”. It is unclear how an amino acid can be SEQ ID NO: 11 and thus the claim is rendered indefinite. In the interest of compact prosecution, the Examiner is interpreting the claim as the peptide having the amino acid of SEQ ID NO: 11.
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 1-2, 7, 9, 24-26, 39, and 51 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.
With regards to claim 1 (and claims 2, 7, 9, 24-26, 39, and 51 dependent on), the claim is directed to all possible “peptides comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid. The specification, however, only provides representative species of a peptide comprising a sequence of SEQ ID NO: 1 with substitutions at position 26 (variants 8a-8i, specification pg. 6-7), substitution at position 33 (variants 9a-9s, see specification pg. 8-9), and substitution at position 120 (variants 10a-10s, see specification pg. 9-10). There is no disclosure of any particular structure to function/activity relationship in the disclosed species. Vasina et al. (Journal of Biomedical Science, Vol. 31;75; published 2024) teaches that the active site of the enzyme contains three amino acids coordinating a zinc ion, and two charged acids bound to a water molecule for zinc coordination and forming a charged groove important for peptidoglycan binding. For endolysins acting against Gram-negative bacteria, the presence of an additional membrane-translocating domain is predicted, allowing the enzymes to cross the outer membrane of bacteria and reach the peptidoglycan substrate, that there is no obvious characteristic sequence on either the C-terminal or N-terminal of LysECD7 but a region enriched in charged and polar amino acids detected in the a2 helix, predicted to be an intrinsically disordered region containing a possible antimicrobial peptide. Vasin teaches that it forms a protusion covering the substrate binding pocket of the enzyme and is enriched with lysine residues along the inner surface. Vasina teaches that such elements lack a compact ordered structure under conditions of normal pH in vitro while under certain conditions the structure is stabilized and the domain acquires functionality, either the intrinsically disordered region can fold upon binding to the interaction partner (see pg. 9). The specification also fails to describe any identifying structural characteristics or properties for which predictability of structure is apparent.
Regarding the level of skill and knowledge of the art of amino acid mutation, the reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017, cited on the attached Form 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 column 1, top, pg. 7). 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-892) 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 (column 1, pg. 1475).
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.
Claims 1-2, 7, 9, 24-26, 39, and 51 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for peptides comprising a sequence of SEQ ID NO: 1 with substitutions at position 26 (variants 8a-8i, specification pg. 6-7), substitution at position 33 (variants 9a-9s, see specification pg. 8-9), or substitution at position 120 (variants 10a-10s, see specification pg. 9-10), does not reasonably provide enablement for all possible “peptides comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid. 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/or 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 1 (and claims 2, 7, 9, 24-26, 39, and 51 dependent on) are so broad as to encompass all possible peptides comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid. The scope of the claims is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of peptides comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid and variants broadly encompassed by the claim. The claims rejected under this section of U.S.C. 112, first paragraph, place minimal structural limits on the required variant polypeptides comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid 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 peptides comprising a sequence of SEQ ID NO: 1 with substitutions at position 26 (variants 8a-8i, specification pg. 6-7), substitution at position 33 (variants 9a-9s, see specification pg. 8-9), or substitution at position 120 (variants 10a-10s, see specification pg. 9-10).
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/peptide/polypeptide 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 or polypeptide 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 peptides comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid because the specification does not establish (A) regions of the polypeptide which may be modified effecting the antimicrobial activity of the LysECD7 peptide; (B) the general tolerance of LysECD7 peptide to modification and extent of such tolerance; (C) a rational and predictable scheme for modifying any amino acid residue of the LysECD7 peptide 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 antimicrobial activity of the LysECD7 peptide 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 antimicrobial activity 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 possible peptide comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid. 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 peptides comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence wherein the wild type sequence has a sequence as follows, SEQ ID NO: 1, wherein the LysECD7 variant comprises a SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid and retaining function 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 § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claim 1 is rejected under 35 U.S.C. 101 because the claimed invention is directed to a product of nature without significantly more. The claim(s) recite(s): (claim 1) a peptide comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence (SEQ ID NO: 1) wherein the LysECD7 variant comprises SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid; This judicial exception is not integrated into a practical application because the additional elements do not contribute any meaningful limitation to the natural product .The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because claim 1 recites a peptide comprising a sequence that is a LysECD7 variant of a LysECD7 wild-type sequence (SEQ ID NO: 1) wherein the LysECD7 variant comprises SEQ ID NO: 1 with at least one amino acid residue selected from positions 25-40, 68-73, 97-110, 119-131, and 138-143 of SEQ ID NO: 1 substituted with a different amino acid. The claim encompasses a composition of a polypeptide that is structurally identical to a natural occurring polypeptide as evidenced by UniProt Database entry: (A0A6B9SWD3_9CAUD; first entry June 17, 2020). UniProt A0A6B9SWD3_9CAUD discloses a L-Ala-D-Glu peptidase like protein (endolysin) that is a variant of LysECD7 that has a substitution at position 127 (substituted with a T residue) (see sequence alignment below). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 86.3%; Score 651; Length 129;
Best Local Similarity 97.6%;
Matches 122; Conservative 0; Mismatches 3; Indels 0; Gaps 0;
Qy 19 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 78
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 61
Qy 79 HLHGLAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVSVEWGGDWVSFKDGVHFQLP 138
|||| ||||||||||||||||||||||||||||||||||| ||||||| |||||||||||
Db 62 HLHGFAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVPVEWGGDWTSFKDGVHFQLP 121
Qy 139 HSKYP 143
|||||
Db 122 HSKYP 126
UniProt A0A6B9SWD3_9CAUD teaches that the polypeptide is from Escherichia phage Ec_Makalu_001.
Because there is no difference in characteristics (structural, functional, or otherwise) between the claimed and naturally occurring composition and function of the composition, the claimed composition does not have markedly different characteristics and thus is a product of nature exception. Accordingly, the product is directed to an exception (Step 2A: Yes). Because the claim does not include any additional features that could add significantly more to the exception (Step 2: No), the claim does not qualify as eligible subject matter and is rejected.
Claim 2 is rejected under 35 U.S.C. 101 because the claimed invention is directed to a product of nature without significantly more. The claim(s) recite(s): (claim 2) the peptide according to claim 1 comprising a sequence of SEQ ID NO: 2 wherein X is independently selected from the following amino acids: A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V and where at least one X is not the same amino acid as that in the same position in SEQ ID NO: 1. This judicial exception is not integrated into a practical application because the additional elements do not contribute any meaningful limitation to the natural product. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because claim 2 recites the peptide according to claim 1 comprising a sequence of SEQ ID NO: 2 wherein X is independently selected from the following amino acids: A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V and where at least one X is not the same amino acid as that in the same position in SEQ ID NO: 1. The claim encompasses a composition of a polypeptide that is structurally identical to a natural occurring polypeptide as evidenced UniProt Database entry: (C4MYS4_9CAUD; first entry July 7, 2009). C4MYS4_9CAUD discloses a L-Ala-D-Glu peptidase like protein that is a variant of LysECD7 that has a substitution at position 123 (substituted with a V residue; different from residue G in the same position in SEQ ID NO. 1) (see sequence alignment below). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 72.3%; Score 467.5; Length 129;
Best Local Similarity 76.0%;
Matches 95; Conservative 2; Mismatches 27; Indels 1; Gaps 1;
Qy 19 FKLSQRXXDRXXXVHPDXVKVXHRALELTPVDFGITEGVRSLETQKKYVAEGKXKTMKSR 78
|||||| || |||| ||| ||||||||||||||||||||||||||||||| ||||||
Db 2 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 61
Qy 79 HLHGLAVDVVAYPKDKDTWNMKXYRMXADXFKQAGRELGVSVE-XXXXVSXXXGVHFQLP 137
|||| ||||||||||||||||| ||| || |||||||||| | |: | | :|
Db 62 HLHGFAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVPVICGVDWVTFKDGPHMELD 121
Qy 138 HSKYP 142
||
Db 122 KKVYP 126
UniProt C4MYS4_9CAUD teaches that the polypeptide is from Escherichia phage JSE.
Because there is no difference in characteristics (structural, functional, or otherwise) between the claimed an naturally occurring composition and function of the composition, the claimed composition does not have markedly different characteristics and thus is a product of nature exception. Accordingly, the product is directed to an exception (Step 2A: Yes). Because the claim does not include any additional features that could add significantly more to the exception (Step 2: No), the claim does not qualify as eligible subject matter and is rejected.
Claim 7 is rejected under 35 U.S.C. 101 because the claimed invention is directed to a product of nature without significantly more. The claim(s) recite(s): (claim 7) the peptide according to claim 1 comprising a sequence according to the following: (SEQ ID NO: 7) wherein X is independently selected from the following amino acids: A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V and wherein at least one X is not the same amino acid as that in the same position in SEQ ID NO: 1. This judicial exception is not integrated into a practical application because the additional elements do not contribute any meaningful limitation to the natural product. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because claim 7 recites he peptide according to claim 1 comprising a sequence according to the following: (SEQ ID NO: 7) wherein X is independently selected from the following amino acids: A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V and wherein at least one X is not the same amino acid as that in the same position in SEQ ID NO: 1. The claim encompasses a composition of a polypeptide that is structurally identical to a natural occurring polypeptide as evidenced UniProt Database entry: (H2IY48_RAHAC; first entry March 21, 2012). H2IY48_RAHAC discloses a L-ala-D-Glu peptidase like protein (endolysin) that is a variant of LysECD7 that has an E substitution at position 26 (equivalent amino acid in position 26 of SEQ ID NO: 1 is a K residue). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 57.6%; Score 423; Length 129;
Best Local Similarity 61.6%;
Matches 77; Conservative 21; Mismatches 27; Indels 0; Gaps 0;
Qy 19 FKLSQRSXDRLXXVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 78
|| |||| : | |: |||||| ||::|: :|||:|||:||:| ||: ||||||:|| ||
Db 4 FKFSQRSENNLKGVNADLVKVVRRAIQLSAIDFGVTEGLRSVERQKQLVAEGKSQTMNSR 63
Qy 79 HLHGLAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVSVEWGGDWVSFXDGVHFQLP 138
|: | |||| ||| :|: |||: |::||||||:|| | ||||||| : || |||||
Db 64 HISGHAVDVFAYPTPAGSWDWKYYQQISEAFKQAGKELNVPVEWGGDWTTLKDGPHFQLP 123
Qy 139 HSKYP 143
:: ||
Db 124 YAAYP 128
UniProt H2IY48_RAHAC teaches that the polypeptide is from Rahnella aquatillis (strain ATCC 33071/DSM 4594/JCM1683/NBCR 105701/ NCIMB 13365 /CIP 78.65).
Because there is no difference in characteristics (structural, functional, or otherwise) between the claimed an naturally occurring composition and function of the composition, the claimed composition does not have markedly different characteristics and thus is a product of nature exception. Accordingly, the product is directed to an exception (Step 2A: Yes). Because the claim does not include any additional features that could add significantly more to the exception (Step 2: No), the claim does not qualify as eligible subject matter and is rejected.
Claim 25 is rejected under 35 U.S.C. 101 because the claimed invention is directed to a product of nature without significantly more. The claim(s) recite(s): (claim 25) the peptide according to claim 1 wherein the amino acid sequence is SEQ ID NO: 11. This judicial exception is not integrated into a practical application because the additional elements do not contribute any meaningful limitation to the natural product. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because claim 25 recites the peptide according to claim 1 wherein the amino acid sequence is SEQ ID NO: 11. The claim encompasses a composition of a polypeptide that is structurally identical to a natural occurring polypeptide as evidenced UniProt Database entry: (A0A0B7MRT1_9CAUD; first entry April 1, 2015). A0A0B7MRT1_9CAUD discloses a L-Ala-D-Glu-peptidase like protein (a variant of LysECD7 with substitutions at positions 25, 119, and 127 of SEQ ID NO. 1 (see sequence alignment below and underlined bold residues). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 83.8%; Score 631; Length 129;
Best Local Similarity 95.2%;
Matches 119; Conservative 0; Mismatches 6; Indels 0; Gaps 0;
Qy 19 FKLSQRSIDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 78
||||||| ||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 61
Qy 79 HLHGLAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVSVEWGGDWVSFKDGVHFQLP 138
|||| ||||||||||||||||||||||||||||||||||| ||||||| ||||| | |||
Db 62 HLHGFAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVPVEWGGDWTSFKDGPHLQLP 121
Qy 139 HSKYP 143
|||||
Db 122 HSKYP 126
UniProt A0A0B7MRT1_9CAUD teaches that the polypeptide is from Enterobacteria phage GEC-3S.
Because there is no difference in characteristics (structural, functional, or otherwise) between the claimed an naturally occurring composition and function of the composition, the claimed composition does not have markedly different characteristics and thus is a product of nature exception. Accordingly, the product is directed to an exception (Step 2A: Yes). Because the claim does not include any additional features that could add significantly more to the exception (Step 2: No), the claim does not qualify as eligible subject matter and is rejected.
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 and 51 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (A0A6B9SWD3_9CAUD; first entry June 17, 2020), hereinafter referred to as A0A6B9SWD3_9CAUD .
With regards to claim 1 and 51, A0A6B9SWD3_9CAUD discloses a L-Ala-D-Glu peptidase like protein (endolysin) that is a variant of LysECD7 that has a substitution at position 127 (substituted with a T residue) (see sequence alignment below). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 86.3%; Score 651; Length 129;
Best Local Similarity 97.6%;
Matches 122; Conservative 0; Mismatches 3; Indels 0; Gaps 0;
Qy 19 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 78
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 61
Qy 79 HLHGLAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVSVEWGGDWVSFKDGVHFQLP 138
|||| ||||||||||||||||||||||||||||||||||| ||||||| |||||||||||
Db 62 HLHGFAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVPVEWGGDWTSFKDGVHFQLP 121
Qy 139 HSKYP 143
|||||
Db 122 HSKYP 126
Therefore, claims 1 and 51 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (A0A6B9SWD3_9CAUD; first entry June 17, 2020).
Claim 2 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (C4MYS4_9CAUD; first entry July 7, 2009), hereinafter referred to as C4MYS4_9CAUD.
With regards to claim 2, C4MYS4_9CAUD discloses a L-Ala-D-Glu peptidase like protein (endolysin) that is a variant of LysECD7 that has a substitution at position 123 (substituted with a V residue; different from residue G in the same position in SEQ ID NO. 1) (see sequence alignment below). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 72.3%; Score 467.5; Length 129;
Best Local Similarity 76.0%;
Matches 95; Conservative 2; Mismatches 27; Indels 1; Gaps 1;
Qy 19 FKLSQRXXDRXXXVHPDXVKVXHRALELTPVDFGITEGVRSLETQKKYVAEGKXKTMKSR 78
|||||| || |||| ||| ||||||||||||||||||||||||||||||| ||||||
Db 2 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 61
Qy 79 HLHGLAVDVVAYPKDKDTWNMKXYRMXADXFKQAGRELGVSVE-XXXXVSXXXGVHFQLP 137
|||| ||||||||||||||||| ||| || |||||||||| | |: | | :|
Db 62 HLHGFAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVPVICGVDWVTFKDGPHMELD 121
Qy 138 HSKYP 142
||
Db 122 KKVYP 126
Therefore, claim 2 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (C4MYS4_9CAUD; first entry July 7, 2009), hereinafter referred to as C4MYS4_9CAUD.
Claim 7 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (H2IY48_RAHAC; first entry March 21, 2012), hereinafter referred to as H2IY48_RAHAC.
With regards to claim 7, H2IY48_RAHAC discloses a L-ala-D-Glu peptidase like protein (endolysin) that is a variant of LysECD7 that has an E substitution at position 26 (equivalent amino acid in position 26 of SEQ ID NO: 1 is a K residue) (see sequence alignment below). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 57.6%; Score 423; Length 129;
Best Local Similarity 61.6%;
Matches 77; Conservative 21; Mismatches 27; Indels 0; Gaps 0;
Qy 19 FKLSQRSXDRLXXVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 78
|| |||| : | |: |||||| ||::|: :|||:|||:||:| ||: ||||||:|| ||
Db 4 FKFSQRSENNLKGVNADLVKVVRRAIQLSAIDFGVTEGLRSVERQKQLVAEGKSQTMNSR 63
Qy 79 HLHGLAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVSVEWGGDWVSFXDGVHFQLP 138
|: | |||| ||| :|: |||: |::||||||:|| | ||||||| : || |||||
Db 64 HISGHAVDVFAYPTPAGSWDWKYYQQISEAFKQAGKELNVPVEWGGDWTTLKDGPHFQLP 123
Qy 139 HSKYP 143
:: ||
Db 124 YAAYP 128
Therefore, claim 7 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (H2IY48_RAHAC; first entry March 21, 2012), hereinafter referred to as H2IY48_RAHAC.
Claim 25 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (A0A0B7MRT1_9CAUD; first entry April 1, 2015), hereinafter referred to as A0A0B7MRT1_9CAUD.
A0A0B7MRT1_9CAUD discloses a L-Ala-D-Glu-peptidase like protein ( a variant of LysECD7 with substitutions at positions 25, 119, and 127 of SEQ ID NO. 1 (see sequence alignment below and underlined bold residues). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 83.8%; Score 631; Length 129;
Best Local Similarity 95.2%;
Matches 119; Conservative 0; Mismatches 6; Indels 0; Gaps 0;
Qy 19 FKLSQRSIDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 78
||||||| ||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 61
Qy 79 HLHGLAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVSVEWGGDWVSFKDGVHFQLP 138
|||| ||||||||||||||||||||||||||||||||||| ||||||| ||||| | |||
Db 62 HLHGFAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVPVEWGGDWTSFKDGPHLQLP 121
Qy 139 HSKYP 143
|||||
Db 122 HSKYP 126
Therefore, claim 25 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Database entry: (A0A0B7MRT1_9CAUD; first entry April 1, 2015).
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.
Claim 24 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt Database entry: (A0A6B9SWD3_9CAUD; first entry July 7, 2009), hereinafter referred to as A0A6B9SWD3_9CAUD, in view of Skerlavaj et al. (FEBS Letters, Vol. 463, pg. 58-62; published 1999), hereinafter referred to as Skerjavaj and further in view of Briers et al. (Antimicrobial Agents and Chemotherapy, Vol. 58, pg. 3774-3784; published July 2014), hereinafter referred to as Briers.
With regards to claim 24, A0A6B9SWD3_9CAUD discloses a L-Ala-D-Glu peptidase like protein (endolysin) that is a LysECD7 variant that has a substitution at position 127 (substituted with a V residue) (see sequence alignment below). Under broadest reasonable interpretation (BRI) of a peptide comprising a sequence that is a LysECD7 variant, a variant of LysECD7 may contain additional substitutions and/or deletions or insertions.
Query Match 86.3%; Score 651; Length 129;
Best Local Similarity 97.6%;
Matches 122; Conservative 0; Mismatches 3; Indels 0; Gaps 0;
Qy 19 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 78
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 FKLSQRSKDRLVGVHPDLVKVVHRALELTPVDFGITEGVRSLETQKKYVAEGKSKTMKSR 61
Qy 79 HLHGLAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVSVEWGGDWVSFKDGVHFQLP 138
|||| ||||||||||||||||||||||||||||||||||| ||||||| |||||||||||
Db 62 HLHGFAVDVVAYPKDKDTWNMKYYRMIADAFKQAGRELGVPVEWGGDWTSFKDGVHFQLP 121
Qy 139 HSKYP 143
|||||
Db 122 HSKYP 126
A0A6B9SWD3_9CAUD does not teach that RGLRRLGRKIAHGVKKYGPTVLRIIRIAG (SEQ ID NO: 9) is attached at the N-terminal or C-terminal end of the peptide through an amine bond.
However, Skerlavaj teaches a peptide RGLRRLGRKIAHGVKKYGPTVLRIIRIAG, termed SMAP-29, that has highly potent antimicrobial activity in vitro against a broad spectrum of microorganisms including antibiotic resistant clinical strains and fungi that cause serious infections. Skerlavaj teaches that SMAP-29 acts by rapidly permeabilizing bacterial membranes (see pg. 58). Skerlavaj does not teach that it is fused to the L-ala-D-Glu peptidase taught by A0A6B9SWD3_9CAUD.
However, Briers teaches that endolysins are enzymes produced by bacterial viruses at the end of their lytic cycle. They enzymatically degrade the peptidoglycan layer within the infected host cell and they induce a sudden lysis of the infected bacterial cell. Exogenous application of purified endolysins to Gram-positive pathogens quickly kills them by lysis due to turgor pressure. Briers teaches that a major hurdle in the development of endolysins as antibacterials is the expansion to Gram-negative pathogens since the outer membrane shields access to the peptidoglycan layer from outside (see pg. 3775). Briers teaches the combination of the self-promoted uptake mechanism of a cationic antimicrobial peptide and the PG-degrading activity of an endolysin by the fusion of the sheep myeloid fusion antimicrobial peptide of 29 amino acids (SMAP-29) to the N-terminus of the endolysin, KZ144 (see pg. 3775). Briers teaches the fusion of SMAP-29 to KZ144 results in a highly potent antibacterial that kills virtually all P. aeruginosa strains and acts quickly (see pg. 3775).
It would have been obvious to one of ordinary skill in the art of protein engineering before the effective filing date of the current instant application to combine the self-promoted uptake mechanism of the cationic microbial peptide, SMAP-29 taught by Skerlavaj and Briers, with the PG-degrading activity of the endolysin of SEQ ID NO. 1 taught by A0A6B9SWD3_9CAUD by fusing the SMAP-29 peptide taught by Skerlavaj and Briers to the N-terminus of the endolysin taught by A0A6B9SWD3_9CAUD. The motivation to do so would come from the teachings of Skerlavaj and Briers who teach that fusing the SMAP-29 to an endolysin resulted in a fusion which combines the uptake mechanism of the cationic microbial peptide with the PG-degrading activity of the endolysin to form a fusion with improved anti-microbial activity. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of A0A6B9SWD3_9CAUD, Skerlavaj and Briers who provide all the teachings, reagents, and methods to do so.
Therefore, claim 24 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt Database entry: (A0A6B9SWD3_9CAUD; first entry July 7, 2009) in view of Skerlavaj et al. (FEBS Letters, Vol. 463, pg. 58-62; published 1999) and further in view of Briers et al. (Antimicrobial Agents and Chemotherapy, Vol. 58, pg. 3774-3784; published July 2014).
Claim 26 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt A0A6B9SWD3_9CAUD; first entry June 17, 2020), hereinafter referred to as A0A6B9SWD3_9CAUD as applied to claim 1 above, and further in view of Henriques et al. (WIPO International Publication Number WO 2008/017483 A2; published February 14, 2008), hereinafter referred to as Henrique, and further in view of Antonova et al. (Biomolecules Vol. 10: 440, published 2020), hereinafter referred to as Antonova et al.
The teachings of A0A6B9SWD3_9CAUD as applied to claim 1 are summarized above.
A0A6B9SWD3_9CAUD does not teach a fusion protein comprising one or more peptides and a spore crust protein selected from CotV, CotW, CotX, CotY, CotZ, and CgeA, wherein the one or more peptides are N-terminally attached, C-terminally attached, or both N-terminally attached to the spore crust protein.
However, Henriques teaches that microbial surface display has increasingly become a tool of choice to display peptides or proteins of biotechnological interest on natural nanostructures (see pg. 1, lines 4-10). Henriques teaches that surface display requires only the synthesis of the hybrid protein that consists of a passenger protein of commercial interest fused to a carrier protein which anchors it onto the biological surface (see lines 8-10, pg. 1). Henriques teaches the construction of a system aimed at the display of an enzymatic activity on the spore surface (see lines-13-14, pg. 10). Goldman teaches a spore which is genetically modified by a genetic DNA construct wherein the DNA construct comprises a first DNA portion encoding a target protein which is a bioactive polypeptide and a second DNA portion encoding a carrier when transcribed and translated, expresses a fusion protein between the carrier and the target peptide. Henriques teaches that the second DNA portion of the construct encoding the carrier may be selected from the spore proteins CotW, CotZ, CotX, CotV and CotY (see claims 1 and 5). It is inherent that the fusion protein taught by Henrique is N-terminally attached to the spore crust protein in the DNA construct described above.
Furthermore, Antonova teaches that the use of recombinant endolysins is a promising approach for microbial therapy and that LysECD7 has bactericidal activity (see Abstract, pg. 1).
It would have been obvious to one of ordinary skill in the art of protein engineering before the effective filing date of the current instant application to modify the fusion protein taught by Henrique (passenger protein of interest fused to carrier protein) by substituting the passenger protein with a LysECD7 variant polypeptide taught by A0A6B9SWD3_9CAUD and Antonova and selecting either spore protein CotW, CotZ, CotX, CotV, or CotY as the carrier protein in the fusion protein. The motivation to do so would come from the teachings of Henrique who teaches that fusion of a passenger polypeptide of interest that has bioactivity to a spore protein would allow for surface display of the fusion protein for biotechnological interest such as antimicrobial activity. One of ordinary skill in the art would find further motivation to do so from the teachings of Antonova who teaches that LysECD7 is an endolysin with lytic activity that could be a promising therapeutic agent for antimicrobial drug development (see pg. 3). One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of A0A6B9SWD3_9CAUD, Henrique, and Antonova who provide all the teachings, compositions, and methods needed to do so.
Therefore, claim 26 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt A0A6B9SWD3_9CAUD; first entry June 17, 2020) as applied to claim 1 above, and further in view of Henriques et al. (WIPO International Publication Number WO 2008/017483 A2; published February 14, 2008) and further in view of Antonova et al. (Biomolecules Vol. 10: 440, published 2020).
Claim 39 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt A0A6B9SWD3_9CAUD; first entry June 17, 2020), hereinafter referred to as A0A6B9SWD3_9CAUD as applied to claim 1 above, and further in view of Bhuyan et al. (WIPO International Publication Number WO 2020/24730 A1; published December 3, 2020), hereinafter referred to as Bhuyan, and further in view of Antonova et al. (Biomolecules Vol. 10: 440, published 2020), hereinafter referred to as Antonova et al.
The teachings of A0A6B9SWD3_9CAUD as applied to claim 1 are summarized above.
A0A6B9SWD3_9CAUD does not teach a spore having a peptide selected from a wt LysECED7 peptide, a wt LysECD7_SMAP29 peptide, or a peptide (LysEDC7 variant), attached to the surface or wherein the spore is modified to express the peptide on the surface of the spore, wherein the spore comprises one or more recombinant biological barcodes and wherein the spore has a genome modified to render inoperable one or more genes that are needed for spore germination and/or production of an essential metabolite or wherein the isolated spores are non-germinating and/or auxotrophic.
However, Bhuyan teaches that a nucleic acid biological barcode can be contained in a microorganism such as a bacterial spore. Bhuyan teaches that bacterial spores are genetically modified to carry the nucleic acid barcode in its genome or display it on its surface (see paragraph 0009). Bhuyan also teaches microorganisms such as spores comprising one or more recombinant biological barcodes and a genome modified to render inoperable one or more genes that are needed for spore germination or for production of an essential metabolite. Bhuyan teaches that as such, the microorganism can be non-germinating and/or auxotrophic.(see paragraph 0010). Bhuyan further teaches that a fluorescent indicator such as red fluorescent protein is affixed to a surface (see paragraphs 0014 and 0069).
Furthermore, Antonova teaches that the use of recombinant endolysins is a promising approach for microbial therapy and that LysECD7 has bactericidal activity (see Abstract, pg. 1).
It would have been obvious to one of ordinary skill in the art of protein engineering before the effective filing date of the current instant application to modify the spore taught by Bhuyan by modifying the spore to express a LysECD7 variant taught by A0A6B9SWD3_9CAUD instead of red fluorescent protein. The motivation to do so would also come from the teachings of Antonova who teaches that endolysins such as LysECD7 have bactericidal activity and by Bhuyan who teaches a biotechnological solution for tracking a spore by incorporating the use of biological barcodes. One of ordinary skill in the art would find this further motivating as a way of tracking the spore containing the antimicrobial peptide during therapeutic applications. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of A0A6B9SWD3_9CAUD, Bhuyan, and Antonova who provide all the teachings, compositions, and methods needed to so.
Therefore, claim 39 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt A0A6B9SWD3_9CAUD; first entry June 17, 2020) as applied to claim 1 above, and further in view of Bhuyan et al. (WIPO International Publication Number WO 2020/24730 A1; published December 3, 2020) and further in view of Antonova et al. (Biomolecules Vol. 10: 440, published 2020).
Conclusion
No claims are allowed.
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/GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652
/ROBERT B MONDESI/ Supervisory Patent Examiner, Art Unit 1652
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