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 2/20/2026 is acknowledged.
4. Claim filed on 1/28/2025 is acknowledged.
5. Claims 10 and 11 have been cancelled.
6. New claims 16-22 have been added.
7. Claims 1-9 and 12-22 are pending in this application.
8. Claims 4-6, 8, 9, 12-15, 17 and 19-22 are withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to non-elected inventions, there being no allowable generic or linking claim. Claims 3, 7, 16 and 18 are withdrawn from consideration as being drawn to non-elected species.
9. Claims 1 and 2 are under examination.
Election/Restrictions
10. Applicant’s election without traverse of Group 1 (claims 1-3, 7, 16 and 18) and election without traverse of SEQ ID NO: 64 as species of polypeptide in the reply filed on 2/20/2026 is acknowledged. The requirement is made FINAL in this office action.
Group 1 is drawn to a polypeptide comprising a zinc finger peptide having from 8 to 32 zinc finger domains (F1 to F32) according to Formula 2: X0-2 C X1-5 C X2-7 X-1 X+1 X+2 X+3 X+4 X+5 X+6 H X3-6 H/c where X is any amino acid, numbers in subscript indicate a number of residues represented by X, and numbers in superscript indicate a position of the amino acid in the α-helix; wherein the polypeptide binds to a 5'-GCG-3' nucleic acid repeat sequence; and at least 8 adjacent zinc finger domains, F1 to F8, have a recognition sequence X-1 X+1 X+2 X+3 X+4 X+5 X+6 according to the patterns as recited in instant claim 1. 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 1; and prior art was found. Claims 3, 7, 16 and 18 are withdrawn from consideration as being drawn to non-elected species. Claims 1 and 2 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, various nucleic acid sequences are disclosed in instant Figure 2 and on page 96, lines 23 and 24 of instant specification. However, these nucleic acid sequences are not disclosed in the filed sequence listing.
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 the following minor informality: The specification discloses various nucleic acid sequences on page 96, lines 23 and 24 of instant specification. However, these nucleic acid sequences are not disclosed in the filed sequence listing; and they are missing the respective sequence identifier.
Furthermore, the instant specification discloses various peptides on page 37, Table 2; page 42, Table 4; page 77, line 31; and page 89, lines 3, 4, 18 and 19 of instant specification. However, they are missing the respective sequence identifier.
Applicant is required to amend the specification to comply with 37 CFR 1.821(c) and 1.821(d).
13. The specification is objected to for the following minor informality: There is no subscript and/or superscript in Formula 2 recited on page 6, lines 5-6 and 28 of instant specification. Applicant is required to correct this error.
14. The specification is objected to for the following minor informality: The amino acid sequence of instant SEQ ID NO: 1, 4 or 5 on page 32, lines 8, 14 and 15 of instant specification is not the same as the amino acid sequence of instant SEQ ID NO: 1, 4 or 5 in the filed sequence listing and the rest of the specification. Applicant is required to correct this error.
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).
15. The drawings are objected to for the following minor informality:
Figure 2: the various nucleic acid sequences disclosed in instant Figure 2 are not disclosed in the filed sequence listing; and they are missing the respective sequence identifier. Applicant is required to amend Figure 2 to comply with 37 CFR 1.821(c) and 1.821(d).
Figures 3, 5 and 6: The legend of Y-axis is missing.
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.
16. Claim 1 is objected to for the following minor informality: Applicant is suggested to amend claim 1 as: “An engineered zinc finger peptide comprising at least 8 zinc finger domains according to Formula 2: X0-2CX1-5CX2-7X-1X+1X+2X+3X+4X+5X+6HX3-6H/c, wherein: X is any amino acid; the numbers in subscript indicate number of residues represented by X, and the numbers in superscript indicate position of the amino acid in α-helix; H/c indicates the amino acid at the C-terminus of Formula 2 is C or H; wherein the number of zinc finger domains in the engineered zinc finger peptide is no more than 32; wherein the sequence X-1X+1X+2X+3X+4X+5X+6 in at least 8 adjacent zinc finger domains in the engineered zinc finger peptide is selected from the followings patterns (i)-(vi):
1st zinc finger domain
2nd, 4th, 6th and 8th Zinc finger domains
3rd, 5th and 7th Zinc finger domains
(i)
SEQ ID NO: 1
SEQ ID NO: 1
SEQ ID NO: 1
(ii)
SEQ ID NO: 6
SEQ ID NO: 6
SEQ ID NO: 6
(iii)
SEQ ID NO: 2
SEQ ID NO: 2
SEQ ID NO: 6
(iv)
SEQ ID NO: 2
SEQ ID NO: 6
SEQ ID NO: 2
(v)
SEQ ID NO: 4
SEQ ID NO: 4
SEQ ID NO: 6
(vi)
SEQ ID NO: 4
SEQ ID NO: 6
SEQ ID NO: 4
; and wherein the engineered zinc finger peptide binds to a 5'-GCG-3' nucleic acid repeat sequence“.
In the instant case, SEQ ID NOs: 2-5 are subgenus of the genus of instant SEQ ID NO: 1.
17. Claim 2 is objected to for the following minor informality: Applicant is suggested to amend claim 2 as “The engineered zinc finger peptide according to claim 1, wherein: (i) the number of the zinc finger domain in the engineered zinc finger peptide is 10, 11, 12 or 18; (ii) the number of the zinc finger domain in the engineered zinc finger peptide is 10 to 18., wherein…”.
Please note: in the instant case, it is unclear to the Examiner what the pattern and/or arrangement in (iv) and (v) should be. Therefore, it is impossible for the Examiner to make any suggestion on (iv) and (v) of instant claim 2.
Rejections
Claim Rejections - 35 U.S.C. § 112 paragraph (b)
18. 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.
19. Claims 1 and 2 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 pre-AIA the applicant regards as the invention.
20. Claim 1 is indefinite for the following reasons:
First, the amino acid sequence of instant SEQ ID NO: 1, 4 or 5 appears to be inconsistent in that: the amino acid sequence of instant SEQ ID NO: 1, 4 or 5 recited on page 32, lines 8, 14 and 15 of instant specification is not the same as amino acid sequence of instant SEQ ID NO: 1, 4 or 5 in the filed sequence listing and the rest of the specification. Therefore, it is unclear what the patterns including any of instant SEQ ID NO: 1, 4 or 5 should be.
Second, claim 1 recites “at least 8 adjacent zinc finger domains, F1 to F8, have a recognition sequence…”. It is unclear whether this recitation means the 8 adjacent zinc finger domains needs to be the 1st to 8th zinc finger domains in the claimed polypeptide, or it can be any 8 adjacent zinc finger domains in the claimed polypeptide.
Third, each of the recited patterns includes 32 zinc finger domains. It is unclear whether the instant claimed polypeptide needs to have 32 zinc finger domains as defined in the various patterns recited in instant claim 1 or not.
Taken all these together, the metes and bounds of instant claim 1 is vague and indefinite. Because claim 2 depends from indefinite claim 1, and it does not clarify the point of confusion, it must also be rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph.
Furthermore, for the purpose of this examination, in particular, for applying prior art reference, claim 1 is interpretating as the one set forth in Section 16 above.
21. Claim 2 is indefinite for the following reasons:
First, the recited “(i) comprises from 10 to 18 zinc finger domains” and “(ii) comprises 10, 11, 12 or 18 zinc finger domains” are indefinite. In this case, as an example, it is unclear whether a polypeptide comprising 20 zinc finger domains reads on these limitations or not.
Second, as stated in Section 20 above, the amino acid sequence of instant SEQ ID NO: 1, 4 or 5 appears to be inconsistent. Therefore, it is unclear what the patterns including any of instant SEQ ID NO: 1, 4 or 5 in (iv) are.
Third, based on instant specification and/or instant claim 1, each of the patterns and/or arrangements recited in (iv) and (v) of instant claim 2 includes 32 zinc finger domains. It is unclear whether the polypeptide recited in (iv) and (v) of instant claim 2 needs to have 32 zinc finger domains or not.
Taken all these together, the metes and bounds of instant claim 2 is vague and indefinite.
Claim Rejections - 35 U.S.C. § 112 paragraph (a)
Written Description
22. 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.
23. Claims 1 and 2 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 and 2 are drawn to a polypeptide comprising a zinc finger peptide having from 8 to 32 zinc finger domains (F1 to F32) according to Formula 2: X0-2 C X1-5 C X2-7 X-1 X+1 X+2 X+3 X+4 X+5 X+6 H X3-6 H/c where X is any amino acid, numbers in subscript indicate a number of residues represented by X, and numbers in superscript indicate a position of the amino acid in the α-helix; wherein the polypeptide binds to a 5'-GCG-3' nucleic acid repeat sequence; and at least 8 adjacent zinc finger domains, F1 to F8, have a recognition sequence X-1 X+1 X+2 X+3 X+4 X+5 X+6 according to the patterns as recited in instant claim 1.
The genus of instant claimed polypeptide is extremely broad, other than at least 8 adjacent zinc finger domains having a recognition sequence X-1 X+1 X+2 X+3 X+4 X+5 X+6 according to the patterns as recited in instant claim 1, X in the recited Formula 2 can be any amino acid.
With regards to the term “amino acid”, the instant specification discloses that “The term 'amino acid' in the context of the present invention is used in its broadest sense and is meant to include naturally occurring L a-amino acids or residues.”; and “The general term 'amino acid' further includes D-amino acids, retro-inverse amino acids as well as chemically modified amino acids such as amino acid analogues, naturally occurring amino acids that are not usually incorporated into proteins such as norleucine, and chemically synthesised compounds having properties known in the art to be characteristic of an amino acid, such as β-amino acids.” (see page 16, lines 10-11 and 15-19 of instant specification).
The instant specification discloses that peptides of instant SEQ ID NOs: 64 and 67-74 as polypeptide binding to a 5'-GCG-3' nucleic acid repeat sequence.
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 binding to a 5'-GCG-3' nucleic acid repeat sequence 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: 64 and 67-74 as polypeptide binding to a 5'-GCG-3' nucleic acid repeat sequence.
The instant specification further discloses that any one or more of the residues in the -1, 2, 3 or 6 positions of each finger may be replaced with an A or G residue in order to weaken the binding interaction. And SEQ ID NOs: 67-74 are such variant of instant SEQ ID NO: 64.
Furthermore, peptide of instant SEQ ID NO: 64 is tested in the working examples in instant specification. Instant SEQ ID NO: 64 comprises 11 zinc figure domains with peptide RSDELTR or RSDERKR as the 5'-GCG-3' recognition sequence.
Taken all these together, other than the limited examples, the instant specification fails to describe a general correlation between structure and function for the claimed genus of polypeptide to have the functional characteristics of binding to a 5'-GCG-3' nucleic acid repeat sequence.
(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 binding to a 5'-GCG-3' nucleic acid repeat sequence or not.
With regards to the instant claimed polypeptide to have the functional characteristics of binding to a 5'-GCG-3' nucleic acid repeat sequence, Eisenberg et al (US 2003/0092000 A1) teach peptide RSDELTR or RSDERKR as 5'-GCG-3' recognition sequence in zinc finger peptide, for example, pages 20-21, paragraphs [0206]-[0208]. Desjarlais et al (Proc Natl Acad Sci U S A, 1993, 90, pages 2256-2260) teach a peptide comprising three zinc finger domains with the amino acid sequence RSDELQR being the recognition sequence binds to 5'-GCG-GCG-GCG-3', for example, page 2257, Figure 1A. However, the amino acid sequence RSDELQR in Desjarlais et al does not read on instant SEQ ID NOs: 1-6.
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) 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 polypeptide binding to a 5'-GCG-3' nucleic acid repeat sequence, 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 to have the functional characteristics of binding to a 5'-GCG-3' nucleic acid repeat sequence or not.
(d) representative number of samples:
In the instant case, the genus of instant claimed polypeptide is extremely broad, other than at least 8 adjacent zinc finger domains having a recognition sequence X-1 X+1 X+2 X+3 X+4 X+5 X+6 according to the patterns as recited in instant claim 1, X in the recited Formula 2 can be any amino acid.
And, as discussed in (a) and (b) above, the instant specification discloses peptides of instant SEQ ID NOs: 64 and 67-74 as polypeptide binding to a 5'-GCG-3' nucleic acid repeat sequence.
The instant specification further discloses that any one or more of the residues in the -1, 2, 3 or 6 positions of each finger may be replaced with an A or G residue in order to weaken the binding interaction. And SEQ ID NOs: 67-74 are such variant of instant SEQ ID NO: 64.
Furthermore, peptide of instant SEQ ID NO: 64 is tested in the working examples in instant specification. Instant SEQ ID NO: 64 comprises 11 zinc figure domains with peptide RSDELTR or RSDERKR as the 5'-GCG-3' recognition sequence.
Considering the broadness of the genus of instant claimed polypeptide, the instant specification fails to provide sufficient examples to describe the entire genus of instant claimed polypeptide to have the functional characteristics of binding to a 5'-GCG-3' nucleic acid repeat sequence 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 to have the functional characteristics of binding to a 5'-GCG-3' nucleic acid repeat sequence; 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. § 103
24. 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 of this title, 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.
25. The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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.
26. Claims 1 and 2 are rejected under 35 U.S.C. 103 as being unpatentable over Müller et al (Muscle Nerve, 2001, 24, pages 120-122) in view of Desjarlais et al (Proc Natl Acad Sci U S A, 1993, 90, pages 2256-2260), Eisenberg et al (US 2003/0092000 A1) and Garriga-Canut et al (PNAS, 21012, pages E3136-E3145, filed with IDS).
The instant claims 1 and 2 drawn to are a polypeptide comprising a zinc finger peptide having from 8 to 32 zinc finger domains (F1 to F32) according to Formula 2: X0-2 C X1-5 C X2-7 X-1 X+1 X+2 X+3 X+4 X+5 X+6 H X3-6 H/c where X is any amino acid, numbers in subscript indicate a number of residues represented by X, and numbers in superscript indicate a position of the amino acid in the α-helix; wherein the polypeptide binds to a 5'-GCG-3' nucleic acid repeat sequence; and at least 8 adjacent zinc finger domains, F1 to F8, have a recognition sequence X-1 X+1 X+2 X+3 X+4 X+5 X+6 according to the patterns as recited in instant claim 1.
Müller et al, throughout the literature, teach short GCG repeat expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy (OPMD) in French-Canadian and Italian pedigrees; and patients with OPMD contain GCG repeats of (GCG)8-13, for example, Title; Abstract; and the 1st paragraph in Section “RESULTS”.
The difference between the reference and instant claims 1 and 2 is that the reference does not teach the polypeptide recited in instant claims 1 and 2.
However, Desjarlais et al, throughout the literature, teach a designed zinc-finger protein comprising three zinc fingers with the amino acid sequence CPECGKSFS RSDELQRHQRTH binds to the sequence 5'-GCG-GCG-GCG-3', wherein the binding/recognition sequence is RSDELQR, for example, Abstract; and page 2257, Figure 1A. Desjarlais et al further teach such designed zinc-finger protein as a powerful vehicle for the production of desired site-specific DNA binding proteins, for example, Abstract; and page 2260, Section “Conclusions”.
Furthermore, Eisenberg et al teach that similar to the binding/recognition sequence RSDELQR in Desjarlais et al, RSDELTR or RSDERKR is binding/recognition sequence for -GCG-, for example, pages 20-21, paragraphs [0206-[0208]. The binding/recognition sequence RSDELTR or RSDERKR in Eisenberg et al meets the limitations of instant SEQ ID NO: 1. Therefore, in view of the combined teachings of Desjarlais et al and Eisenberg et al, it would have been obvious to one of ordinary skilled in the art to develop a designed zinc-finger protein comprising three zinc fingers with the amino acid sequence CPECGKSFSRSDELTRHQRTH or CPECGKSFS RSDERKRHQRTH, wherein the designed zinc-finger protein binds to the sequence 5'-GCG-GCG-GCG-3'. The designed zinc-finger protein developed from the combined teachings of Desjarlais et al and Eisenberg et al is a simple substitution of one known element for another to obtain predictable results (see MPEP § 2143 I).
In addition, Garriga-Canut et al, throughout the literature, teach Huntington’s disease (HD) is a dominantly inherited neurodegenerative disorder caused by expanded CAG repeats in the huntingtin (HTT) gene; and synthetic zinc finger proteins (ZFPs) comprising multiple zinc finger peptides having binding/recognition sequence that binds to CAG repeats in the huntingtin (HTT) gene, wherein such synthetic zinc finger proteins can be used for optimizing longer-term therapeutic benefit for treating HD, for example, Abstract; and page E3143, left column, the 2nd paragraph. Garriga-Canut et al further teach using long artificial ZFP chains to bind longer CAG repeats more strongly than shorter repeats, including various synthetic zinc finger proteins with 4, 6, 11 or 18 binding/recognition sequence for binding to (CAG)5, (CAG)7, and/or (CAG)13, for example, Abstract; and Figures 1-3.
Therefore, it would have been obvious to one of ordinary skilled in the art to combine the teachings of Müller et al, Desjarlais et al, Eisenberg et al and Garriga-Canut et al to develop a designed zinc-finger protein comprising at least 8, such as 11 or 18, zinc fingers with the amino acid sequence CPECGKSFSRSDELTRHQRTH or CPECGKSFSRSDERKRHQRTH, wherein the designed zinc-finger protein binds to the longer 5'-GCG-3' repeat sequence in patients with OPMD and can be used to treat OPMD.
One of ordinary skilled in the art would have been motivated to combine the teachings of Müller et al, Desjarlais et al, Eisenberg et al and Garriga-Canut et al to develop a designed zinc-finger protein comprising at least 8, such as 11 or 18, zinc fingers with the amino acid sequence CPECGKSFSRSDELTRHQRTH or CPECGKSFS RSDERKRHQRTH, wherein the designed zinc-finger protein binds to the longer 5'-GCG-3' repeat sequence in patients with OPMD and can be used to treat OPMD, because Desjarlais et al, throughout the literature, teach a designed zinc-finger protein comprising three zinc fingers with the amino acid sequence CPECGKSFS RSDELQRHQRTH binds to the sequence 5'-GCG-GCG-GCG-3', wherein the binding/recognition sequence is RSDELQR. Desjarlais et al further teach such designed zinc-finger protein as a powerful vehicle for the production of desired site-specific DNA binding proteins. Eisenberg et al teach that similar to the binding/recognition sequence RSDELQR in Desjarlais et al, RSDELTR or RSDERKR is binding/recognition sequence for -GCG-. Therefore, in view of the combined teachings of Desjarlais et al and Eisenberg et al, it would have been obvious to one of ordinary skilled in the art to develop a designed zinc-finger protein comprising three zinc fingers with the amino acid sequence CPECGKSFSRSDELTRHQRTH or CPECGKSFS RSDERKRHQRTH, wherein the designed zinc-finger protein binds to the sequence 5'-GCG-GCG-GCG-3'. The designed zinc-finger protein developed from the combined teachings of Desjarlais et al and Eisenberg et al is a simple substitution of one known element for another to obtain predictable results (see MPEP § 2143 I). Garriga-Canut et al, throughout the literature, teach Huntington’s disease (HD) is a dominantly inherited neurodegenerative disorder caused by expanded CAG repeats in the huntingtin (HTT) gene; and synthetic zinc finger proteins (ZFPs) comprising multiple zinc finger peptides having binding/recognition sequence that binds to CAG repeats in the huntingtin (HTT) gene, wherein such synthetic zinc finger proteins can be used for optimizing longer-term therapeutic benefit for treating HD. Garriga-Canut et al further teach using long artificial ZFP chains to bind longer CAG repeats more strongly than shorter repeats, including various synthetic zinc finger proteins with 4, 6, 11 or 18 binding/recognition sequence for binding to (CAG)5, (CAG)7, and/or (CAG)13.
A person of ordinary skilled in the art would have reasonable expectation of success in combining the teachings of Müller et al, Desjarlais et al, Eisenberg et al and Garriga-Canut et al to develop a designed zinc-finger protein comprising at least 8, such as 11 or 18, zinc fingers with the amino acid sequence CPECGKSFSRSDELTRHQRTH or CPECGKSFSRSDERKRHQRTH, wherein the designed zinc-finger protein binds to the longer 5'-GCG-3' repeat sequence in patients with OPMD and can be used to treat OPMD.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to LI N KOMATSU whose telephone number is (571)270-3534. The examiner can normally be reached Mon-Fri 8am-4pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melissa Fisher can be reached at 5712707430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/LI N KOMATSU/Primary Examiner, Art Unit 1658