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. In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the cited rejections 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.
3. Response to Election/Restriction filed on 8/28/2025 is acknowledged.
4. Claim filed on 1/4/2023 is acknowledged.
5. Claim 13-18 and 21 have been cancelled.
6. New claims 23-26 have been added.
7. Claims 1-12, 19, 20 and 22-26 are pending in this application.
8. Claims 9-11, 19, 20 and 23-26 are withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to non-elected inventions, there being no allowable generic or linking claim. Claims 5, 6 and 8 are withdrawn from consideration as being drawn to non-elected species.
9. Claims 1-4, 7, 12 and 22 are under examination.
Election/Restrictions
10. Applicant’s election without traverse of Group 1 (claims 1-8 and part of claims 12 and 22) and election without traverse of SEQ ID NO: 1 as species of peptide in the reply filed on 8/28/2025 is acknowledged. Since the elected species of peptide is a subgenus, not a species, the Examiner telephoned Applicant’s representative, Susan M. Michaud, for further species election. Applicant’s representative elected on the phone that SEQ ID NO: 6 as the species of peptide on 9/8/2025. The requirement is made FINAL in this office action.
Group 1 is drawn to a peptide that blocks the function of human Guanine Nucleotide Exchange Factor-H1 (GEF-H1), wherein the peptide comprises an amino acid sequence that has at least 80% sequence identity to SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2; a pharmaceutical composition comprising such peptide and a pharmaceutically acceptable carrier; and a kit comprising such peptide or a pharmaceutical composition comprising (a) the peptide and (b) a pharmaceutically acceptable carrier, and instructions for use. A search was conducted on the elected species; this appears to be free of prior art. A search was extended to the genus in claim 1; and prior art was found. Claims 5, 6 and 8 are withdrawn from consideration as being drawn to non-elected species. Claims 1-4, 7, 12 and 22 are examined on the merits in this office action.
Sequence Non-Compliance
11. This application contains sequence disclosures that are encompassed by the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR 1.821(a)(1) and (a)(2). However, this application fails to comply with the requirements of 37 CFR 1.821 through 1.825 for the reason(s) set forth below. All sequences disclosed in the application must comply with the requirements of 37 C.F.R. 1.821-1.825, not only those recited in the claims.
In the instant case, the instant specification discloses the peptides R8 and R9 on page 14, line 29 of instant specification. However, these peptides are not in the sequence listing filed on 1/4/2023.
All such sequences are relevant for the purposes of building a comprehensive database and properly assessing prior art. It is therefore essential that all sequences, whether only disclosed or also claimed, be included in the database.
Objections
12. The specification is objected to for failing to comply with 37 CFR 1.821(c) and 37 CFR 1.821(d). The instant specification discloses the peptides R8 and R9 on page 14, line 29 of instant specification. However, these peptides are not in the sequence listing filed on 1/4/2023; and they are missing their respective sequence identifiers. Applicant is therefore required to amend the specification to comply with 37 CFR 1.821(c) and 37 CFR 1.821(d).
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).
13. The drawings are objected to for the following minor informality:
Figure 3B recites various peptides. However, they are missing their respective sequence identifiers. Applicant is therefore required to amend figure 3B to comply with 37 CFR 1.821(d).
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
14. Claim 1 is objected to for the following minor informality: Applicant is suggested to amend claim 1 as “A peptide that blocks the function of human Guanine Nucleotide Exchange Factor-H1 (GEF-H1), wherein the peptide comprises the amino acid sequence that is at least 80% identical to the amino acid sequence of SEQ ID NO: 1…”. In the instant case, the Examiner would like to point out that the term “an amino acid sequence” broadly includes both fragments and full-length of the sequence that is at least 80% identical to any of the recited SEQ ID NOs.
15. Claim 2 is objected to for the following minor informality: Applicant is suggested to amend claim 2 as “…wherein the peptide comprises the amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO: 1…or SEQ ID NO: 2, and wherein the peptide blocks the function of human GEF-H1”.
16. Claim 3 is objected to for the following minor informality: Applicant is suggested to amend claim 3 as “…wherein the peptide comprises the amino acid sequence that is at least 95% identical to the amino acid sequence of SEQ ID NO: 1…or SEQ ID NO: 2, and wherein the peptide blocks the function of human GEF-H1”.
17. Claim 7 is objected to for the following minor informality: Applicant is suggested to amend claim 7 as “…wherein the peptide comprises the sequence of SEQ ID NO: 1…”, or “…wherein the peptide consists of the sequence of SEQ ID NO: 1…”.
Furthermore, for the purpose of this examination and in the broadest reasonable interpretation, the Examiner is interpretating the peptide recited in instant claim 7 is one comprising the sequence of SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 2, or SEQ ID NO: 7.
18. Claims 12 and 22 are objected to for the following minor informality: Claims 12 and 22 contain more than the elected invention. Applicant is required to delete the non-elected invention recited in these claims.
Rejections
Claim Rejections - 35 U.S.C. § 112 paragraph (a)
Written Description
19. 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.
20. Claims 1-4, 7, 12 and 22 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
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 1-4, 7, 12 and 22 recite a peptide that blocks the function of human Guanine Nucleotide Exchange Factor-H1 (GEF-H1), wherein the peptide comprises an amino acid sequence that has at least 80% sequence identity to SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2; and claims 2-4 and 7 further limit the recited peptide to one comprising the amino acid sequence that is at least 90%, 95% or 100% identical to the recited SEQ ID NOs.
The genus of instant claimed peptide is extremely broad, including any peptide comprising the amino acid sequence that is at least 80% identical to any one of the recited SEQ ID NOs.
The instant specification discloses that peptides of instant SEQ ID NO: 2 and SEQ ID NO: 3 (P5) are identified as a peptide that blocks the function of human GEF-H1; peptides of instant SEQ ID NOs: 1, 6 and 13-15 are peptides comprising or consisting of a stapled-P5 consensus amino acid sequence; peptide of instant SEQ ID NO: 5 comprising P5 and TAT; and peptide of instant SEQ ID NO: 7 comprising instant SEQ ID NO: 2 and TAT. And these peptides as the examples of instant claimed peptide.
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 peptide to have the functional characteristics of blocking the function of human GEF-H1 or not.
(a) actual reduction to practice and (b) disclosure of drawings or structural chemical formulas:
In the instant case, the instant specification discloses peptides of instant SEQ ID NOs: 1-3, 5-7 and 13-15 as examples of the instant claimed peptide.
Furthermore, peptides of instant SEQ ID NOs: 2, 3 and 5-7 are tested in the working examples in instant specification.
Taken all these together, other than the limited examples, the instant specification fails to disclose the effect of either altering the amino acid sequence or the length of any one of instant claimed SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2 on the functional characteristics of blocking the function of human GEF-H1. The instant specification does not describe a general correlation between structure and function for the claimed genus of peptide comprising an amino acid sequence that has at least 80% sequence identity to SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2.
(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 the effect of either altering the amino acid sequence or the length of any one of instant claimed SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2 on the functional characteristics of blocking the function of human GEF-H1.
With regards to the instant claimed peptide to have the property of blocking the function of human GEF-H1, using peptide of instant SEQ ID NO: 2 as an example, Tsapara et al (Molecular Biology of the Cell, 2010, 21, pages 860-870, filed with IDS) teach a dominant-negative (DN) construct containing the C-terminal domain (CTD) of GEF-H1 and a C-terminal VSV epitope as a tag (DN-GEF-H1), which is disclosed in Aijaz et al (Developmental Cell, 2005, 8, pages 777-786, filed with IDS), wherein the DN-GEF-H1 has the property of blocking the function of human GEF-H1, for example, page 861, right column, Section “Inhibition of α-SMA Expression by DN-GEF-H1”; and page 865, Figure 1. And as evidenced by both Aijaz et al and the rho guanine nucleotide exchange factor 2 isoform A [Canis lupus familiaris] document (from NCBI, 2020, enclosed pages 1-5), the DN-GEF-H1 in Tsapara et al comprises amino acids 577-986 of the rho guanine nucleotide exchange factor 2 isoform A [Canis lupus familiaris] (see for example, pages 783-784, Section “cDNA Constructs, RNA Interference, and Cell Lines” in Aijaz et al; and the amino acid sequence on page 5 of the rho guanine nucleotide exchange factor 2 isoform A [Canis lupus familiaris] document); and peptide of instant SEQ ID NO: 2 is identical to amino acids 576-707 of the rho guanine nucleotide exchange factor 2 isoform A [Canis lupus familiaris] (see for example, the amino acid sequence on page 5). Therefore, the DN-GEF-H1 in Tsapara et al comprises the amino acid sequence that is about 99.2% identical to the amino acid sequence of instant SEQ ID NO: 2. However, Tsapara et al fail to teach which amino acids in the DN-GEF-H1 are important and/or essential to the property of blocking the function of human GEF-H1.
In addition, the Blast search result for SEQ ID NO: 2 document (2025, enclosed pages 1-6, from https://blast.ncbi.nlm.nih.gov/Blast.cgi) discloses many proteins comprising the amino acid sequence that is at least 80% identical to the amino acid sequence of instant SEQ ID NO: 2. However, there is no evidence that any of these proteins has the property of blocking the function of human GEF-H1. This also applies to other SEQ IDs recited in instant claims.
And, 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) 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). 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 peptide that blocks the function of human GEF-H1, 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 the effect of either altering the amino acid sequence or the length of any one of instant claimed SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2 on the functional characteristics of blocking the function of human GEF-H1.
(d) representative number of samples:
In the instant case, the genus of instant claimed peptide is extremely broad, including any peptide comprising the amino acid sequence that is at least 80% identical to any one of the recited SEQ ID NOs.
And, as discussed in (a) and (b) above, the instant specification discloses peptides of instant SEQ ID NOs: 1-3, 5-7 and 13-15 as examples of the instant claimed peptide.
Furthermore, peptides of instant SEQ ID NOs: 2, 3 and 5-7 are tested in the working examples in instant specification.
However, the instant specification does not disclose any variant of instant SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2 to have the property of blocking the function of human GEF-H1.
Considering the broadness of the genus of instant claimed peptide, the instant specification fails to provide sufficient examples to describe the entire genus of peptide comprising an amino acid sequence that has at least 80% sequence identity to SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2 to have the property of blocking the function of human GEF-H1 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 peptide comprising an amino acid sequence that has at least 80% sequence identity to SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2 to have the property of blocking the function of human GEF-H1; 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.
Claim Rejections - 35 U.S.C. § 102(a)(1)
21. 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.
22. Claims 1-4, 7, 12 and 22 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Aijaz et al (Developmental Cell, 2005, 8, pages 777-786, filed with IDS), and as evidenced by the rho guanine nucleotide exchange factor 2 isoform A [Canis lupus familiaris] document (from NCBI, 2020, enclosed pages 1-5) and Tsapara et al (Molecular Biology of the Cell, 2010, 21, pages 860-870, filed with IDS).
The instant claims 1-4, 7, 12 and 22 are drawn to a peptide that blocks the function of human Guanine Nucleotide Exchange Factor-H1 (GEF-H1), wherein the peptide comprises an amino acid sequence that has at least 80% sequence identity to SEQ ID NO: 1, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, or SEQ ID NO: 2; a pharmaceutical composition comprising such peptide and a pharmaceutically acceptable carrier; and a kit comprising such peptide or a pharmaceutical composition comprising (a) the peptide and (b) a pharmaceutically acceptable carrier, and instructions for use.
Aijaz et al, throughout the literature, teach various variants of GEF-H1, such as GEF-ΔNTD-VSV by deleting residues 2 to 216 of canine GEF-H1, GEF-H1-ΔPH by deleting residues 447 to 575 of canine GEF-H1, and a peptide containing the C-terminal domain (CTD) of GEF-H1 and a C-terminal VSV epitope as a tag, wherein the CTD domain is residues 557 to 986 of canine GEF-H1, for example, pages 784-785, Section “cDNA Constructs, RNA Interference, and Cell Lines”. And as evidenced by the rho guanine nucleotide exchange factor 2 isoform A [Canis lupus familiaris] document, the amino acid sequence of instant SEQ ID NO: 2 is identical to residues 576-707 of the canine GEF-H1 in Aijaz et al (see for example, the amino acid sequence on page 5). Therefore, the peptides of GEF-ΔNTD-VSV and GEF-H1-ΔPH in Aijaz et al comprise the amino acid sequence of instant SEQ ID NO: 2; and the peptide containing the C-terminal domain (CTD) of GEF-H1 and a C-terminal VSV epitope as a tag in Aijaz et al comprises the amino acid sequence that is about 99.2% identical to the amino acid sequence of instant SEQ ID NO: 2. It meets the structural limitations of the peptide recited in instant claims 1-4 and 7. And further as evidenced by Tsapara et, the peptide containing the C-terminal domain (CTD) of GEF-H1 and a C-terminal VSV epitope as a tag in Aijaz et al is a dominant-negative form that has the property of blocking the function of human GEF-H1 (see for example, page 861, right column, Section “Inhibition of α-SMA Expression by DN-GEF-H1”; and page 865, Figure 1). It meets the limitations of the peptide recited in instant claims 1-3.
With regards to the limitation “a peptide that blocks the function of human Guanine Nucleotide Exchange Factor-H1 (GEF-H1)” and “wherein the peptide blocks the function of GEFH1” recited in instant claims, in the instant case, since the peptides of GEF-ΔNTD-VSV and GEF-H1-ΔPH in Aijaz et al meet all the structural limitations of the peptide recited in instant claims 1-4 and 7, the peptides of GEF-ΔNTD-VSV and GEF-H1-ΔPH in Aijaz et al would necessarily have the same properties and functionality of the peptide recited in instant claims 1-4 and 7. Therefore, the peptides of GEF-ΔNTD-VSV and GEF-H1-ΔPH in Aijaz et al would have the property of blocking the function of human GEF-H1. Furthermore, the MPEP states “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). "When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Therefore, the prima facie case can be rebutted by evidence showing that the prior art products do not necessarily possess the characteristics of the claimed product. In re Best, 562 F.2d at 1255, 195 USPQ at 433. See also Titanium Metals Corp. v. Banner, 778 F.2d 775, 227 USPQ 773 (Fed. Cir. 1985) (Claims were directed to a titanium alloy containing 0.2-0.4% Mo and 0.6-0.9% Ni having corrosion resistance. A Russian article disclosed a titanium alloy containing 0.25% Mo and 0.75% Ni but was silent as to corrosion resistance. The Federal Circuit held that the claim was anticipated because the percentages of Mo and Ni were squarely within the claimed ranges. The court went on to say that it was immaterial what properties the alloys had or who discovered the properties because the composition is the same and thus must necessarily exhibit the properties.)” (see MPEP § 2112.01 I). And, since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
In the broadest reasonable interpretation, the cells expressing GEF-ΔNTD-VSV, GEF-H1-ΔPH and the peptide containing the C-terminal domain (CTD) of GEF-H1 and a C-terminal VSV epitope as a tag in Aijaz et al is the pharmaceutical composition recited in instant claim 12; and the petri dish containing such cells is the kit recited in instant claim 22.
Additionally, for a better understanding of how the examiner views the kit recited in instant claim 22, it should be noted that the claim is to a product, and products are not limited or novel based on the product’s non-functional instructions on how to use the product by being in a kit. “Where the only difference between a prior art product and a claimed product is printed matter that is not functionally related to the product, the content of the printed matter will not distinguish the claimed product from the prior art.” In re Ngai, 367 F.3d 1336, 2004 WL 1068957 (Fed. Cir. May 13, 2004) (see MPEP § 2112.01 III).
Since the reference teaches all the limitations of instant claims 1-4, 7, 12 and 22; the reference anticipates instant claims 1-4, 7, 12 and 22.
Conclusion
No claim is allowed.
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/LI N KOMATSU/ Primary Examiner, Art Unit 1658