DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Amendment after Non-final office action filed on 11/3/2025 is acknowledged.
3. Claim filed on 11/3/2025 is acknowledged.
4. Claims 3, 4, 7, 9-11, 13, 16-20, 23, 25, 27-40, 42, 45, 47, 48, 50-53, 55-62, 64-73 and 75-83 have been cancelled.
5. Claims 1, 2, 5, 6, 8, 12, 14, 15, 21, 22, 24, 26, 41, 43, 44, 46, 49, 54, 63 and 74 are pending in this application.
6. Claims 1, 2, 5, 6, 8, 12, 21, 22, 24, 26, 43, 44, 46, 49, 54, 63 and 74 remain withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to non-elected inventions, there being no allowable generic or linking claim.
7. Applicant elected without traverse of Group 3 (claims 14, 15 and 21) and elected SEQ ID NO: 34 as species of polypeptide in the reply filed on 6/20/2025.
Restriction requirement was deemed proper and made FINAL in the previous office action. Group 3 is drawn to a polypeptide comprising a stable antimicrobial peptide (SAMP) that has an α-helical structure, wherein the SAMP comprises a sequence of (V/S/A)H(V/L)E(F/Y)(A/T/S)(N/A/T)(L/E/I/S/T)(F/L/M)(L/S)(A/S/P/G/T) (N/A/Q/S)(L/V/I)(E/D)K(V/I/T/F)(L/I/V)(V/L/I)(I/L/V/F)DYK (SEQ ID NO: 53), and wherein the SAMP is less than 67 amino acids in length; and an agricultural composition comprising such polypeptide. A search was conducted on the elected species; and this appears to be free of prior art. A search was extended to the genus in claim 14; and prior art was found. Claims 14, 15 and 41 are examined on the merits in this office action.
Claim Interpretations
8. With regards to the limitation “comprises a sequence” recited in instant claim 14, as stated in the previous office action, the term “a sequence” broadly includes both fragments and full length of instant SEQ ID NO: 53 recited in instant claim 14. As an example, a SAMP that has an α-helical structure and comprises the amino acid sequence YK is a SAMP recited in instant claim 14. Such interpretation applies to all the rejections set forth below.
With regards to the polypeptide recited in instant claim 15, the Examiner is interpretating the polypeptide recited in instant claim 15 is one comprising the amino acid sequence of any of the recited SEQ ID NOs. Such interpretation applies to all the rejections set forth below.
Withdrawn Objections and Rejections
9. Objection to the drawings is hereby withdrawn in view of Applicant’s amendments to the drawings and the description of the drawings in the specification.
10. Objection to claim 14 is hereby withdrawn in view of Applicant’s amendments to the claim.
11. Rejection to claims 14, 15 and 41 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph (new matter rejection) is hereby withdrawn in view of Applicant’s amendment to the claim.
Maintained/Revised Objections
12. The use of trademarks has been noted in this application, for example, Onetime® and many others on page 34, paragraph [0107] and throughout the specification. Each letter of the trademarks should be capitalized wherever it appears and be accompanied by the generic terminology. Although the use of trademarks is 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 trademarks.
Please note: The specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification (see MPEP § 608.01).
Response to Applicant's Arguments
13. Applicant fails to address all the minor issues in instant specification. Therefore, the objection is deemed proper and is hereby maintained.
14. (Revised due to Applicant’s amendment to the claim) Claim 15 remains objected to for the following minor informality: Applicant is suggested to amend claim 15 as “The polypeptide of claim 14, wherein the polypeptide comprises the sequence:…”.
Response to Applicant's Arguments
15. Applicant’s amendment to the claim introduces additional minor issues into instant claim 15. Therefore, the objection is deemed proper and is hereby maintained.
Maintained/Revised Rejections
Claim Rejections - 35 U.S.C. § 101
16. 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.
17. (Revised due to Applicant’s amendment to the claim) Claims 14, 15 and 41 remain rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Claims 14, 15 and 41 are directed to a polypeptide comprising a stable antimicrobial peptide (SAMP) that has an α-helical structure, wherein the SAMP comprises a sequence of (V/S/A)H(V/L)E(F/Y)(A/T/S)(N/A/T) (L/E/I/S/T)(F/L/M)(L/S)(A/S/P/G/T)(N/A/Q/S)(L/V/I)(E/D)K(V/I/T/F)(L/I/V)(V/L/I)(I/L/V/F)DYK (SEQ ID NO: 53), and wherein the SAMP is less than 67 amino acids in length; and an agricultural composition comprising such polypeptide.
Pak et al (Biochemical and Biophysical Research Communications, 2007, 362, pages 562-567, filed with IDS) teach a heat-stable protein with antimicrobial activity isolated from Arabidopsis thaliana (a plant that is Liberibacter disease-resistant/tolerant as disclosed in instant specification), wherein the heat-stable protein is 109 amino acids in length and consists of the amino acid sequence MEEAKGPVKHVLLASFKDGVSPEKI EELIKGYANLVNLIEPMKAFHWGKDVSIENLHQGYTHIFESTFESKEAVAEYIAHPAHVEFATIFLGSLDKVLVIDYKPTSVSL (comprising the amino acid sequence of instant SEQ ID NO: 45 or 53, underlined), for example, Title; Abstract; and page 564, Figure 2A. The heat-stable protein isolated from Arabidopsis thaliana in Pak et al meets all the limitations of the instant claimed polypeptide recited in claims 14, 15 and 41. And the heat-stable protein isolated from Arabidopsis thaliana is a naturally occurring polypeptide. Furthermore, with regards to the agricultural composition recited in instant claim 41, the instant specification discloses that “As used herein, the term “agricultural composition" refers to a composition formulated for application to a plant or plant part (e.g.. seed, cutting, shoots, etc.)” (see page 17, paragraph [0064] of instant specification). Therefore, the agricultural composition recited in instant claim 41 can be the polypeptide recited in instant claim 14 only.
The claims 14, 15 and 41 do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claimed polypeptide and an agricultural composition comprising such polypeptide in instant claims 14, 15 and 41 do not recite features or steps demonstrating a marked difference from what exists in nature; and the claimed polypeptide and an agricultural composition comprising such polypeptide in instant claims 14, 15 and 41 do not recite meaningful limitations that add something of significance to the judicial exception. Therefore, the claimed polypeptide and an agricultural composition comprising such polypeptide in instant claims 14, 15 and 41 are not significantly different than a judicial exception (natural product).
Response to Applicant's Arguments
18. Applicant argues that “The Examiner provides no evidence that the particular polypeptides or SAMPs recited by the SEQ ID NOs: 34, 36-47, and 50-56. are found in nature, and claim 14 requires the polypeptide sequence comprise of the particular recited amino acids, not the entire protein sequence of Pak et al.”; and “the polypeptides in the claims are "markedly different" from what is found in nature and thus is not natural phenomena and not a judicial exception.”
19. Applicant's arguments have been fully considered but have not been found persuasive.
In response to Applicant's arguments about instant rejection, first, the Examiner would like to point out that due to Applicant’s amendment to the claim, the polypeptide recited in instant claims 14, 15 and 41 is not limited to any particular length. Furthermore, as stated in Section 17 above, the heat-stable protein isolated from Arabidopsis thaliana meets all the limitations of the instant claimed polypeptide recited in claims 14, 15 and 41. And the heat-stable protein isolated from Arabidopsis thaliana is a naturally occurring polypeptide. Therefore, the claimed polypeptide and an agricultural composition comprising such polypeptide in instant claims 14, 15 and 41 are not significantly different than a judicial exception (natural product).
Thus, the rejection is deemed proper and is hereby maintained.
Claim Rejections - 35 U.S.C. § 112 paragraph (a)
Written Description
20. The following is a quotation 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 35 U.S.C. 112 (pre-AIA ), first paragraph:
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.
21. (Revised due to Applicant’s amendment to the claim) Claims 14, 15 and 41 remain 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.
The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient” (MPEP § 2163).
A claimed genus may be satisfied through sufficient description of a representative number of species or disclosure of relevant, identifying characteristics such as functional characteristics coupled with a known or disclosed correlation between function and structure (MPEP § 2163(3)a(II)). The number of species that describe the genus must be adequate to describe the entire genus; if there is substantial variability, a large number of species must be described.
The analysis for adequate written description considers (a) actual reduction to practice, (b) disclosure of drawings or structural chemical formulas, (c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure, and (d) representative number of samples.
In the instant case, claims 14, 15 and 41 are drawn to a polypeptide comprising a stable antimicrobial peptide (SAMP) that has an α-helical structure, wherein the SAMP comprises a sequence of (V/S/A)H(V/L)E(F/Y)(A/T/S)(N/A/T)(L/E/I/S/T)(F/L/M)(L/S) (A/S/P/G/T)(N/A/Q/S)(L/V/I)(E/D)K(V/I/T/F)(L/I/V)(V/L/I)(I/L/V/F)DYK (SEQ ID NO: 53), and wherein the SAMP is less than 67 amino acids in length; and an agricultural composition comprising such polypeptide.
The genus of instant claimed polypeptide comprising a SAMP is extremely broad, including any polypeptide that comprises at least a dipeptide of instant SEQ ID NO: 53; and any polypeptide comprising any one of the SEQ ID NOs recited in instant claim 15.
The instant specification discloses that peptides of instant SEQ ID NOs: 34, 35, 38-44 and 50-52 as functional SAMP helix fragments.
The issue at question is whether a person of ordinary skilled in the art would be able to determine what structural feature/amino acid sequence is required for the instant claimed polypeptide to have the functional characteristics of comprising a SAMP or not.
(a) actual reduction to practice and (b) disclosure of drawings or structural chemical formulas:
In the instant case, the instant specification discloses that peptides of instant SEQ ID NOs: 34, 35, 38-44 and 50-52 as functional SAMP helix fragments.
Furthermore, the polypeptide of instant SEQ ID NO: 34 is tested in the working examples in instant specification.
Taken all these together, other than the limited examples, the instant specification fails to describe a general correlation between structure and function for claimed polypeptide to have the functional characteristics of comprising a SAMP.
(c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure:
As discussed above, in the instant case, based on the disclosure of instant specification, other than the limited examples, a person of ordinary skilled in the art would not be able to determine what structural feature/amino acid sequence is required for the instant claimed polypeptide to have the functional characteristics of comprising a SAMP.
With regards to a polypeptide having the functional characteristics of comprising a SAMP, Wang et al (US 2005/0074763 A1, cited and enclosed in the previous office action) teach peptide of SEQ ID NO: 14, which is 47 amino acids in length and consists of the amino acid sequence LHQGYTHILESTFESKEAVAEYIAHPAHVEFATIFLGSL DKVLVIDY, wherein the peptide is isolated from Arabidopsis thaliana (a plant that is Liberibacter disease-resistant/tolerant as disclosed in instant specification) and can treat parasite infection of plant, for example, Figure 12, SEQ ID NO: 14; and page 10, paragraph [0110]. The peptide of SEQ ID NO: 14 in Wang et al comprises a sequence of instant SEQ ID NO: 53 (underlined). And as evidenced by the SEQ ID NO 14 in US 2005/0074763 A1 secondary structure document (accessed 6/25/2025, pages 1-2, from https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q9LUV2/structures, cited and enclosed in the previous office action), the peptide of SEQ ID NO: 14 in Wang et al has an α-helical structure (see the structure on page 2). However, other than the very limited example, a polypeptide having the functional characteristics of comprising a SAMP is unknown in the art.
Furthermore, it is well known in the peptide/protein art that even single amino acid changes or differences in the amino acid sequence of a protein can have dramatic effects on the protein’s function. As an example of the unpredictable effects of mutations on protein function, Drumm et al (Annu. Rev. Pathol. Mech. Dis., 2012, 7, pages 267-282, cited and enclosed in the previous office action) teach cystic fibrosis is an autosomal recessive disorder caused by mutations in the CFTR (cystic fibrosis transmembrane conductance regulator) gene, for example, page 268, Section “CYSTIC FIBROSIS”. Drumm et al further teach several mutations can cause cystic fibrosis, including two mutations G551D and G551S; and clinical consequences are quite different for these two changes, as the G551D variant has virtually no detectable activity, and consequently a classic, severe phenotype is associated; G551S, however, has reduced but clearly detectable function and is associated with a much milder presentation of CF, for example page 269, left column, the last paragraph. Drumm et al also teach that in the most common cystic fibrosis mutation ΔF508 (the absence of amino acid 508 of the normally 1,480-amino acid protein) gives rise to the cystic fibrosis phenotype, for example, page 268, right column, the 2nd paragraph. Thus, even the substitution or deletion of a single amino acid can have dramatic and unpredictable effects on the function of the protein. The unpredictability of the effect of amino acid substitution on the function and/or property of peptide/protein is further confirmed and discussed in Yampolsky et al (Genetics, 2005, 170, pages 1459-1472, cited and enclosed in the previous office action). Yampolsky et al teach even conservative substitution can significantly affect the function of the protein/peptide, for example, page 1465, Table 3. Although the disclosures of Drumm et al and Yampolsky et al are directed to proteins/peptides other than a polypeptide having the functional characteristics of comprising a SAMP, they illustrate the inherent unpredictability with respect to the biological activity of a given protein/peptide after even minor changes to the primary amino acid sequence.
Therefore, based on the state of art, a person of ordinary skilled in the art would not be able to determine what structural feature/amino acid sequence is required for the instant claimed polypeptide having the functional characteristics of comprising a SAMP.
(d) representative number of samples:
In the instant case, the genus of instant claimed polypeptide comprising a SAMP is extremely broad, including any polypeptide that comprises at least a dipeptide of instant SEQ ID NO: 53; and any polypeptide comprising any one of the SEQ ID NOs recited in instant claim 15.
And, as discussed in (a) and (b) above the instant specification discloses that peptides of instant SEQ ID NOs: 34, 35, 38-44 and 50-52 as functional SAMP helix fragments.
Furthermore, the polypeptide of SEQ ID NO: 34 is tested in the working examples in instant specification.
Considering the broadness of the genus of instant claimed polypeptide, the instant specification fails to provide sufficient examples to describe the entire genus of polypeptide having the functional characteristics of comprising a SAMP claimed.
Taken all these together, considering the state of the art and the disclosure in instant specification, it is deemed that the instant specification fails to provide adequate written description for the claimed genus of polypeptide having the functional characteristics of comprising a SAMP; and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
Response to Applicant's Arguments
22. Applicant fails to address this rejection. Therefore, the rejection is deemed proper and is hereby maintained.
Claim Rejections - 35 U.S.C. § 102(a)(1)
23. 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.
24. (Revised due to Applicant’s amendment to the claim) Claims 14 and 41 remain rejected under 35 U.S.C. 102(a)(1) as being anticipated by Wang et al (US 2005/0074763 A1, cited and enclosed in the previous office action), and as evidenced by the SEQ ID NO 14 in US 2005/0074763 A1 secondary structure document (accessed 6/25/2025, cited and enclosed in the previous office action, from https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q9LUV2/structures, pages 1-2).
The instant claims 14 and 41 are drawn to a polypeptide comprising a stable antimicrobial peptide (SAMP) that has an α-helical structure, wherein the SAMP comprises a sequence of (V/S/A)H(V/L)E(F/Y)(A/T/S)(N/A/T)(L/E/I/S/T)(F/L/M)(L/S) (A/S/P/G/T)(N/A/Q/S)(L/V/I)(E/D)K(V/I/T/F)(L/I/V)(V/L/I)(I/L/V/F)DYK (SEQ ID NO: 53), and wherein the SAMP is less than 67 amino acids in length; and an agricultural composition comprising such polypeptide.
Wang et al teach peptide of SEQ ID NO: 14, which is 47 amino acids in length and consists of the amino acid sequence LHQGYTHILESTFESKEAVAEYIAHPAHVEF ATIFLGSLDKVLVIDY, wherein the peptide is isolated from Arabidopsis thaliana (a plant that is Liberibacter disease-resistant/tolerant as disclosed in instant specification) and can treat parasite infection of plant, for example, Figure 12, SEQ ID NO: 14; and page 10, paragraph [0110]. The peptide of SEQ ID NO: 14 in Wang et al comprises a sequence of instant SEQ ID NO: 53 (underlined). And as evidenced by the SEQ ID NO 14 in US 2005/0074763 A1 secondary structure document, the peptide of SEQ ID NO: 14 in Wang et al has an α-helical structure (see the structure on page 2). Therefore, the peptide of SEQ ID NO: 14 in Wang et al meets the limitations of instant claim 14. Furthermore, with regards to the agricultural composition recited in instant claim 41, the instant specification discloses that “As used herein, the term “agricultural composition" refers to a composition formulated for application to a plant or plant part (e.g.. seed, cutting, shoots, etc.)” (see page 17, paragraph [0064] of instant specification). Therefore, the peptide of SEQ ID NO: 14 in Wang et al meets the limitation of instant claim 41.
Since the reference teaches all the limitations of instant claims 14 and 41; the reference anticipates instant claims 14 and 41.
Response to Applicant's Arguments
25. Applicant argues that “Wang et al. fails to teach every element of claim 14 in its currently amended form and therefore fails to anticipate claim 14”.
26. Applicant's arguments have been fully considered but have not been found persuasive.
In response to Applicant's arguments about instant rejection, the Examiner would like to point out that based on the claim interpretation set forth in Section 8 above, the peptide of SEQ ID NO: 14 in Wang et al comprises a sequence of instant SEQ ID NO: 53 (KVLVIDY). Furthermore, as stated in Section 24 above, as evidenced by the SEQ ID NO 14 in US 2005/0074763 A1 secondary structure document, the peptide of SEQ ID NO: 14 in Wang et al has an α-helical structure. Therefore, the peptide of SEQ ID NO: 14 in Wang et al meets the limitation of instant claim 14.
Taken all these together, the rejection is deemed proper and is hereby maintained.
New Rejections
Claim Rejections - 35 U.S.C. § 102(a)(1)
27. 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.
28. Claims 14, 15 and 41 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Pak et al (Biochemical and Biophysical Research Communications, 2007, 362, pages 562-567, filed with IDS).
The instant claims 14, 15 and 41 are drawn to a polypeptide comprising a stable antimicrobial peptide (SAMP) that has an α-helical structure, wherein the SAMP comprises a sequence of (V/S/A)H(V/L)E(F/Y)(A/T/S)(N/A/T)(L/E/I/S/T)(F/L/M)(L/S) (A/S/P/G/T)(N/A/Q/S)(L/V/I)(E/D)K(V/I/T/F)(L/I/V)(V/L/I)(I/L/V/F)DYK (SEQ ID NO: 53), and wherein the SAMP is less than 67 amino acids in length; and an agricultural composition comprising such polypeptide.
Pak et al teach a heat-stable protein with antimicrobial activity isolated from Arabidopsis thaliana (a plant that is Liberibacter disease-resistant/tolerant as disclosed in instant specification), wherein the heat-stable protein is 109 amino acids in length and consists of the amino acid sequence MEEAKGPVKHVLLASFKDGVSPEKIEELIKGY ANLVNLIEPMKAFHWGKDVSIENLHQGYTHIFESTFESKEAVAEYIAHPAHVEFATIFLGSLDKVLVIDYKPTSVSL (comprising the amino acid sequence of instant SEQ ID NO: 45 or 53, underlined), for example, Title; Abstract; and page 564, Figure 2A. It meets the limitations of the polypeptide recited in instant claims 14 and 15. Furthermore, with regards to the agricultural composition recited in instant claim 41, the instant specification discloses that “As used herein, the term “agricultural composition" refers to a composition formulated for application to a plant or plant part (e.g.. seed, cutting, shoots, etc.)” (see page 17, paragraph [0064] of instant specification). Therefore, the heat-stable protein with antimicrobial activity isolated from Arabidopsis thaliana in Pak et al meets the limitation of instant claim 41.
Since the reference teaches all the limitations of instant claims 14, 15 and 41; the reference anticipates instant claims 14, 15 and 41.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
No claim is allowed.
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/LI N KOMATSU/Primary Examiner, Art Unit 1658