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 .
Priority
This application is a CON of PCT/CN2025/090656 filed 04/23/2025 which claims the benefit of the priority of China Patent Application No. 202410900732X filed 07/05/2024.
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statements submitted on 08/26/2025, and 07/28/2026 have been considered by the examiner.
Election/Restrictions
Claims 10-14, 16-20 are withdrawn from further consideration pursuant to 37 CFR
1.142(b) as being drawn to a nonelected Group II and III or based on the elected species, there being no allowable generic or linking claim.
Applicant’s election of Group I drawn to a light sensitive channel protein in the reply filed on 07/28/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Applicant further elects the species of SEQ ID NO: 33, and the disease retinitis pigmentosa.
Claim Status
Claims 1-20 are pending. Claims 10-14, 16-20 are withdrawn. Claims 1-9, 15 are being examined on the merits in this office action.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-9, and 15 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP § 2137 states that "the written description requirement for a genus must be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus (see i)(C), above). See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
For written description, the analysis (a) considers 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, functional characteristics when coupled with known or disclosed and (d) representative number of examples.
Actual reduction to practice and (b) disclosure of drawings or structural chemical formulas:
The claims are directed to a light-sensitive channel protein comprising 1-33 amino acids truncation at the N-terminus, or 1-29 amino acids truncation at the C-terminus, mutations introduced around the retinal binding site of SEQ ID NO: 1, or a protein having from 70% to 99% sequence identity to the above variants. Examiner notes that SEQ ID NO: 1 comprises 305 amino acids and thus, the recited truncations allow for significant variability amounting to numerous variants. Additionally, the claims recite 70% to 99% sequence identity to the above variants. 70% identity of SEQ ID NO: 1 with 1 amino acid truncation at both the C and N terminus allows for 91 possibilities leading to numerous possible variants. Additionally, Examiner notes that it is uncertain if the numerous variants would have the function of light activation.
(c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties
There doesn’t appear to be a clear structure-function relationship that would allow a skilled artisan to make the recited truncations and mutations to arrive to a protein that would have the recited function. Thus, there is no clear structure function relationship that would reasonably allow one of ordinary skill in the art to modify the protein of SEQ ID NO: 1 by truncation one or both terminals, as well as mutate the retinal binding site without affecting the recited function of the protein.
(d) Representative number of examples
Applicant has reduced to practice seven-point mutations, nine N-terminal truncations (1, 13, 18, 20, 22, 27, and 34), 6 C-terminal truncations (29, 23, 18, 16, 13, and 9) which is a small fraction of the possible variants and thus not a “representative number of species”. A “representative number of species” means the species which are adequately described are a representative of the entire genus. Therefore, when there is a substantial variation within a genus, the applicant must describe a sufficient variety of species to reflect the variation within the genus. The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure "indicates that the patentee has invented species sufficient to constitute the gen[us]." See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) ("[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated."). See MPEP 2163.3 (ii). Thus, the instant application shows possession of a limited number of species from a wide genus. Given this lack of description in the specification, the application fails to describe the claimed invention in such full, clear, and concise and exact terms that a skilled artisan would recognize that applicants were in possession of the genus of claimed invention.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-9 and 15 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites the limitation "the following PsCatCh variants" in line. Examiner notes that it is unclear what PsCatCh refers to. Examiner notes that it is known in the art that PsChR2 refers to the Platymonas subcordiformis channelrhodopsin-2 protein, but it is unclear what PsCatCh means. Claims 2-9, and 15 have a similar issue. The specification does not clearly indicate what the term or acronym means. Claim 1 further recites “of the reference protein”. There is insufficient antecedent basis for this limitation in the claim.
Additionally, claim 1 recites “…by mutations introduced around the retinal binding site…”. Examiner notes that the specification does not define this limitation and thus one of ordinary skill in the art would not be able to ascertain if the mutation is at the binding site, adjacent to the binding site or if the limitation encompasses a specific number of amino acids from the binding site. Therefore, it is unclear how close the mutation can be from the retinal binding site to meet the limitation of “around”. Claims 2-9, and 15 are also rejected because they depend on a rejected claim 1.
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.
Claim Interpretation
The claim scope has been interpreted as set forth below per the guidance set forth at MPEP § 2111. If Applicant disputes any interpretation, Applicant is invited to unambiguously identify any alleged misinterpretations or specialized definitions in the subsequent response to the instant action. Applicant is advised that a specialized definition should be properly supported and specifically identified (see, e.g., MPEP § 211 l.0l(IV), describing how Applicant may act as their own lexicographer).
Independent claim 1 recite the article “comprising”. "Comprising" is an open-ended transitional term (see, e.g., MPEP § 2111.03(1)), wherein additional amino acid residues are not excluded. However, "'[c]omprising' is a term of art used in claim language which means that the named elements are essential" (see, e.g., id.; see also Genentech, Inc. v. Chiron Corp., 112 F.3d 495, 501, 42 USPQ2d 1608, 1613 (Fed. Cir. 1997)).
Claims 1-9 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Xiadong Duan Thesis published online 2021 – hereinafter “Duan”).
Regarding claim 1, Duan teaches the sequence of a channelrhodposin protein PsChR (See Page 73 of thesis), which is identical to the instant SEQ ID NO: 1. Duan further teaches variants of this polypeptide, wherein in the variants, 12, 19, 33 amino acids are truncated or deleted from the N-terminus and 18-29 amino acids are truncated from the C-terminal and that specifically the variant N19 and C16 amino acid truncation was the best performer giving to 5.5-fold larger photocurrent than PsCatCh and named this variant PsCatCh 2.0e (See Page 57 of thesis and Figure 3.11a). Duan further teaches the addition of a C165L mutation around the retinal biding site which gave rise to nearly two times larger photocurrent (See Page 58 of Thesis; and Figure 3.11b). Duan anticipates claim 1, since the variant PsCatCh 2.0e comprises N19 and C16 amino acid truncation of the instant SEQ ID NO: 1.
Regarding claims 2-4, Duan teaches the sequence of a channelrhodposin protein PsChR (See Page 73 of thesis), which is identical to the instant SEQ ID NO: 1. Duan further teaches variants of this polypeptide, wherein the variants where 12, 19, 33 amino acids are truncated or deleted from the N-terminus and 18-29 amino acids are truncated from the C-terminal (See Page 57 of Thesis, Section 3.2.2).
Regarding claims 5, Duan teaches the sequence of a channelrhodposin protein PsChR (See Page 73 of thesis), which is identical to the instant SEQ ID NO: 1. Duan further teaches variants of this polypeptide, wherein the variants where 12, 19, 33 amino acids are truncated or deleted from the N-terminus and 18-29 amino acids are truncated from the C-terminal and that specifically the variant N19 and C16 amino acid truncation was the best performer giving to 5.5-fold larger photocurrent than PsCatCh and named this variant PsCatCh 2.0e (See Page 57 of thesis and Figure 3.11a). Examiner notes that the teachings of Duan include 18 amino acid truncations at the C-terminal anticipating the claim.
Regarding claim 6, Duan teaches the sequence of a channelrhodposin protein PsChR (See Page 73 of thesis), which is identical to the instant SEQ ID NO: 1. Duan further teaches variants of this polypeptide, wherein the variants where 12, 19, 33 amino acids are truncated or deleted from the N-terminus and 18-29 amino acids are truncated from the C-terminal and that specifically the variant N19 and C16 amino acid truncation was the best performer giving to 5.5-fold larger photocurrent than PsCatCh and named this variant PsCatCh 2.0e (See Page 57 of thesis and Figure 3.11a).
Regarding claim 7, Duan teaches the sequence of a channelrhodposin protein PsChR (See Page 73 of thesis), which is identical to the instant SEQ ID NO: 1. Duan further teaches variants of this polypeptide, wherein the variants where 12, 19, 33 amino acids are truncated or deleted from the N-terminus and 18-29 amino acids are truncated from the C-terminal and that specifically the variant N19 and C16 amino acid truncation was the best performer giving to 5.5-fold larger photocurrent than PsCatCh and named this variant PsCatCh 2.0e (See Page 57 of thesis and Figure 3.11a). Duan further teaches the addition of a C165L mutation around the retinal biding site which gave rise to nearly two times larger photocurrent (See Page 58 of Thesis; and Figure 3.11b). Duan further teaches variants with the E66D mutation (See Table 3.3 on Page 60).
Regarding claim 8, Duan teaches the variants N19 and C16 amino acid truncation was the best performer giving to 5.5-fold larger photocurrent than PsCatCh and named this variant PsCatCh 2.0e (See Page 57 of thesis and Figure 3.11a). Duan further teaches the addition of a C165L mutation around the retinal biding site which gave rise to nearly two times larger photocurrent (See Page 58 of Thesis; and Figure 3.11b). Examiner notes that this variant of Duan is 100% identical to the instant SEQ ID NO: 33, which has 19 amino acids truncated at the N-terminal and 16 amino acids truncated at the C-terminal and has the C165L mutation, thus anticipating the claim.
Regarding claim 9, Duan teaches the sequence of a channelrhodposin protein PsChR (See Page 73 of thesis), which is identical to the instant SEQ ID NO: 1. Duan further teaches variants of this polypeptide, wherein the variants where 12, 19, 33 amino acids are truncated or deleted from the N-terminus and 18-29 amino acids are truncated from the C-terminal and that specifically the variant N19 and C16 amino acid truncation was the best performer giving to 5.5-fold larger photocurrent than PsCatCh and named this variant PsCatCh 2.0e (See Page 57 of thesis and Figure 3.11a). Duan further teaches the addition of a C165L mutation around the retinal biding site which gave rise to nearly two times larger photocurrent (See Page 58 of Thesis; and Figure 3.11b). Duan further teaches modifying the polypeptide with the addition of the LR signal peptide sequence and teaches that the LR contributed to three to ten-fold larger photocurrents, that the peptide was added to the N-terminal (Page 1, 2nd paragraph, line 4-5; Page 38-41, that the LR signal peptide sequence has the amino acid sequence MRPQILLLLALLTLGLANGTEGPNFYVPFSNKTGVVRS (See Fig. 3.4 C)
Claims 1, 4-5, 8, and 15 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Klapoetke et al. (US20120214188A1 – hereinafter “Klapoetke”).
Regarding claim 1, Klapoetke teaches an ultraviolet-light-activated ion channel polypeptide, wherein the sequence of the light-activated ion channel polypeptide comprises an amino acid sequence set forth as SEQ ID NO:4 [0015-0017]. The sequence of Klapoetke comprises 95% identity to the instant SEQ ID NO: 1 (See query match below), and has 11 amino acids truncated at the C-terminus.
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The teachings of Klapoetke anticipate instant claim 1 because the reference teaches a sequence that comprises a truncation of 11 amino acids at the C-terminus and comprises 95% identity to SEQ ID NO: 1.
Regarding claims 4-5, Klapoetke teaches an ultraviolet-light-activated ion channel polypeptide, wherein the sequence of the light-activated ion channel polypeptide comprises an amino acid sequence set forth as SEQ ID NO:4 [0015-0017]. The sequence of Klapoetke comprises 95% identity to the instant SEQ ID NO: 1 (See query match below) and has 11 amino acids truncated at the C-terminus.
Regarding claim 8, Klapoetke teaches an ultraviolet-light-activated ion channel polypeptide, wherein the sequence of the light-activated ion channel polypeptide comprises an amino acid sequence set forth as SEQ ID NO:4 [0015-0017]. The sequence of Klapoetke comprises 98% identity to the instant SEQ ID NO: 33.
Regarding claim 15, Klapoetke teaches pharmaceutical composition comprising the ultraviolet-light-activated ion channel polypeptide and pharmaceutical carriers [0124-0126].
Claims 1, 9, and 15 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Shen et al. (CN113173984B – hereinafter “Shen”).
Regarding claim 1, Shen teaches a light-sensitive channel protein VR1.0, characterized in that: the amino acid sequence is as shown in SEQ ID NO.1 (claim 1). Examiner notes that the sequence of Shen comprises the instant SEQ ID NO: 1, and has 2 amino acids truncated from the C-terminus.
Regarding claim 9, Shen teaches a light-sensitive channel protein VR1.0 , characterized in that: the amino acid sequence is as shown in SEQ ID NO.1 (claim 1). Examiner notes that the sequence of Shen comprises the instant SEQ ID NO: 1, and has 2 amino acids truncated from the C-terminus. Additionally, the sequence of Shen has the fragment on the N-terminus with the amino acids MRPQILLLLALLTLGLANGTEGPNFYVPFSNKTGVVRS, which is identical to the instant SEQ ID NO: 2, thus anticipating claim 9.
Regarding claim 15, Shen teaches a medicament comprising the light-sensitive channel protein (claim 7).
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Mercy H. Sabila whose telephone number is (571)272-2562. The examiner can normally be reached Monday - Friday 5:00 am - 3:00 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko G. Garyu can be reached at (571)270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/MERCY H SABILA/Examiner, Art Unit 1654
/TARA L MARTINEZ/Primary Examiner, Art Unit 1654
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