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 .
DETAILED ACTION
Application Status
This application is a DIV of US patent application 16/928,696, filed on 10/24/2023.
Claims 1, 3-19 and 20 are currently pending in this patent application.
In response to a previous Office action, a Non-Final Rejection Office action (mailed on 07/30/2025), Applicants filed a response and an amendment on January 21, 2026, amending claims 1, 7, 9, and 11, and canceling claim 2 is acknowledged.
Applicants' arguments filed on January 21, 2026, have been fully considered and are deemed persuasive to overcome some of the rejections previously applied. Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.
Claims 13-20 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim.
Claims 1, 3-11 and 12 are present for examination.
Priority
Acknowledgement is made of applicants claim for domestic priority under 35 USC 120/121 to US patent applications 16/928,696, filed on 07/14/2020, now US patent 11827900, 15/685,580, filed on 08/24/2017, now US patent 10975393, and US Provisional Applications 62/378,978, filed on 08/24/2016 and 62/443,981, filed on 01/09/2017.
Withdrawn-Drawings objection
Drawings submitted on 01/08/2024 are now accepted by the Examiner for submitting new Fig. 5A.
Maintained-Claim Rejections - 35 USC § 112(b)
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 previous rejection of Claims 1, 3-7, 9, 11 and 12 under 35 U.S.C. 112(b), 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, is maintained, and the rejection has been at length in the previous Office action, and the rejection is maintained as discussed previously and for the following reasons.
Claim 1 is indefinite and vague in the recitation “a mutation in any one or more of amino acid residues (-5), (-9) and (-14)”, which is confusing because absent a reference to a sequence of the wild type zinc finger DNA-binding domain, known and not an invention) to which the amino acid numbering refers? What is the amino acid sequence of unmutated and wild-type zinc finger DNA-binding domain? In the art, wild-type (known) zinc finger DNA-binding domain protein can be multiple forms derived from many unknown sources as well as many mutants, variants and fragments thereof, which are unknown, rendering the metes and bounds of the term unclear and confusing. Therefore, mutation at position -14, -9 and -5 of zinc finger DNA-binding domain protein is indefinite. The amino acid sequence of wild-type-zinc finger DNA-binding domain protein must be with SEQ ID No. and numbering should be corresponding to a particular sequence with SEQ ID No., for precise analysis of the mutations (minus positions) for art rejection. Clarification is required.
Arguments: Applicants argue that Zif268 Backbone and Mutations at Amino Acid Residues (-5), (-9), or (-14) as provided in Applicant's Specification, zinc finger proteins that employ the well- known Zif268 backbone have an arginine as the amino terminal residue of their second strand of (3-sheet, which is also the second position carboxyl-terminal to the second invariant cysteine. Applicant's Specification, at paragraph [0006] and FIG. 5A. This position is referred to as (-5) within each zinc finger domain, as it is 5th residue preceding the start of the a-helix. Id. Further, zinc finger proteins in the Zif268 backbone also have a lysine at a position that is 4 residues amino-terminal to the first invariant cysteine, which is referred to as (-14) within each finger as it is the 14-residue preceding the alpha helix. Likewise, the arginine that is 2 residues terminal to the second invariant cysteine is commonly referred to as (-9) as it is the 9 preceding the alpha helix.
Response: Applicants arguments have been fully considered, but are not deemed persuasive to overcome the rejection on 35 USC 112(b) issues because Claim 1 is indefinite and vague in the recitation “any mutation in any one or more of amino acid residues (-5), (-9) and (-14)”, which is confusing because absent a reference to a sequence of the wild type zinc finger DNA-binding domain (well-known and not an invention) to which the amino acid numbering refers? What is the amino acid sequence of unmutated and wild-type zinc finger DNA-binding domain? In the art, zinc finger DNA-binding domain protein can be multiple forms derived from many unknown sources as well as many mutants, variants and fragments thereof, which are unknown, rendering the metes and bounds of the term unclear and confusing. Therefore, mutation at position -14, -9 and -5 of zinc finger DNA-binding domain protein is indefinite. The amino acid sequence of zinc finger DNA-binding domain protein must be with SEQ ID No. and numbering should be corresponding to a particular sequence with SEQ ID No., for precise analysis of the mutations (minus positions) for art rejection.
The previous rejection of Claims 1, 3-7, 9, 11 and 12 under 35 U.S.C. 112(b), 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, is maintained, and the rejection has been at length in the previous Office action, and the rejection is maintained as discussed previously and for the following reasons.
Claim 1 is indefinite and vague in the recitation “start of the alpha-helix”, which is confusing in the context of an alpha-helix of a zinc finger DNA-binding domain, which comprises mutations in any one or more of amino acid residues (-5), (-9) and (-14)”. Since, there is no amino acid sequence of an wild-type alpha-helix of an alpha-helix of a zinc finger DNA-binding domain, and the recitation of “the start of the alpha-helix” is unclear and confusing. What is the amino acid sequence of unmutated alpha-helix of a zinc finger DNA-binding domain? In the art, alpha-helix of a zinc finger DNA-binding domain protein can be multiple forms derived from many unknown sources as well as many mutants, variants and fragments thereof. Therefore, “the start of the alpha-helix” is unclear and confusing. Besides, the amino acid sequence of wild-type alpha helix is also required because an ordinary skilled in the art would not understand “the start of the alpha-helix”. Clarification is required.
Arguments: Applicants argue that as shown in Fig. 5A of Applicants specification and further described in detail description , ZFPs having the well-known Zif268 backbone invariably possess an alpha helix that is carboxyl terminal a second beta sheet, of which the position of the alpha helix region as well as the amino acid residues preceding the start of the alpha helix within ZFPs possessing the Zif268 backbone are well-known to those of skill in the art. Accordingly, the skilled artisan could readily ascertain the meaning of the phrase "the start of the alpha helix region" when referenced in connection with the Zif268 backbone of a ZFP.
Response: Applicants arguments have been fully considered, but are not deemed persuasive to overcome the rejection on 35 USC 112(b) issues because Claim 1 is indefinite and vague in the recitation “a mutation in any one or more of amino acid residues (-5), (-9) and (-14)”, which is confusing because absent a reference to a sequence of the wild type zinc finger DNA-binding domain (well-known and not an invention) to which the amino acid numbering refers? What is the amino acid sequence of unmutated and wild-type zinc finger DNA-binding domain? In the art, zinc finger DNA-binding domain protein can be multiple forms derived from many unknown sources as well as many mutants, variants and fragments thereof, which are unknown, rendering the metes and bounds of the term unclear and confusing. Therefore, mutation at position -14, -9 and -5 of zinc finger DNA-binding domain protein is indefinite. The amino acid sequence of zinc finger DNA-binding domain having alpha helix of the protein must be with SEQ ID No. and numbering should be corresponding to a particular sequence with SEQ ID No., for precise analysis of the mutations (minus positions) for art rejection.
The previous rejection of Claims 6 and 11 under 35 U.S.C. 112(b), 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, is maintained, and the rejection has been at length in the previous Office action, and the rejection is maintained as discussed previously and for the following reasons.
Claims 6 and 11 are indefinite and vague in the recitation “FokI cleavage domains ---- one or more mutation at positions ---- 432, 441, 483, 486, --- or 559, which is confusing because absent a reference to a sequence of the wild-type FokI cleavage domain protein to which the amino acid numbering refers? What is the wild-type amino acid sequence of FokI cleavage domain protein? In the art, FokI cleavage domain protein can be multiple forms derived from many unknown sources as well as many mutants, variants and fragments thereof. Therefore, one or more mutation at positions ---- 432, 441, 483, 486, --- or 559 of FokI cleavage domain protein is confusing. The amino acid sequence of FokI cleavage domain protein must be with SEQ ID Number to analyze the patentability of a mutation at a specific positions. Clarification is required.
Arguments: Applicants argue that Zif268 Backbone and Mutations at Amino Acid Residues (-5), (-9), or (-14) as provided in Applicant's Specification, zinc finger proteins that employ the well- known Zif268 backbone have an arginine as the amino terminal residue of their second strand of (3-sheet, which is also the second position carboxyl-terminal to the second invariant cysteine. Applicant's Specification, at paragraph [0006] and FIG. 5A. This position is referred to as (-5) within each zinc finger domain, as it is 5th residue preceding the start of the a-helix. Id. Further, zinc finger proteins in the Zif268 backbone also have a lysine at a position that is 4 residues amino-terminal to the first invariant cysteine, which is referred to as (-14) within each finger as it is the 14-residue preceding the alpha helix. Likewise, the arginine that is 2 residues terminal to the second invariant cysteine is commonly referred to as (-9) as it is the 9 preceding the alpha helix.
Response: Applicants arguments have been fully considered, but are not deemed persuasive to overcome the rejection on 35 USC 112(b) issues because Claim 1 is indefinite and vague in the recitation “a mutation in any one or more of amino acid residues (-5), (-9) and (-14)”, which is confusing because absent a reference to a sequence of the wild type zinc finger DNA-binding domain (well-known and not an invention) to which the amino acid numbering refers? What is the amino acid sequence of unmutated and wild-type zinc finger DNA-binding domain? In the art, zinc finger DNA-binding domain protein can be multiple forms derived from many unknown sources as well as many mutants, variants and fragments thereof, which are unknown, rendering the metes and bounds of the term unclear and confusing. Therefore, mutation at position -14, -9 and -5 of zinc finger DNA-binding domain protein is indefinite. The amino acid sequence of zinc finger DNA-binding domain protein must be with SEQ ID No. and numbering should be corresponding to a particular sequence with SEQ ID No., for precise analysis of the mutations (minus positions) for art rejection. Furthermore, Applicants cannot overcome the 112(b)-rejection citing sequence in Fig. 5A because Table or Figure are also indefinite.
Maintained-Claim Rejections - 35 USC § 112(a)
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.
A. Written Description
The previous rejection of Claims 1, 3-7, 9, 11 and 12 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 (WD) requirement, is 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.
Claim 1 is directed to a zinc finger protein comprising 4 zinc finger DNA-binding domains, wherein each zinc finger DNA-binding domain comprises two beta sheets, an alpha helix, and a recognition helix region that binds to a nucleotide sequence, and further wherein one or more of the zinc finger DNA-binding domains comprise mutations in any one or more of amino acid residues (-5), (-9), or (-14), numbered relative to the start of the alpha helix.
The Court of Appeals for the Federal Circuit has held that a “written description of an invention involving a chemical genus, like a description of a chemical species, ‘requires a precise definition, such as by structure, formula [or] chemical name,’ of the claimed subject matter sufficient to distinguish it from other materials.” University of California v. Eli Lilly and Co., 1997 U.S. App. LEXIS 18221, at *23, quoting Fiers v. Revel, 25 USPQ2d 1601, 1606 (Fed. Cir. 1993). To fully describe a genus of genetic material, which is a chemical compound, applicants must (1) fully describe at least one species of the claimed genus sufficient to represent said genus whereby a skilled artisan, in view of the prior art, could predict the structure of other species encompassed by the claimed genus and (2) identify the common characteristics of the claimed molecules, e.g., structure, physical and/or chemical characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or a combination of these (paraphrased from Enzo Biochemical).
Thus, Claims are drawn to any zinc finger protein having any structural feature comprising 4 any zinc finger DNA-binding domains, or zinc finger nuclease wherein each zinc finger DNA-binding domain comprises two beta sheets, an alpha helix, and a recognition helix region that binds to a nucleotide sequence, and further wherein one or more of the zinc finger DNA-binding domains comprise mutations in any one or more of amino acid residues (-5), (-9), or (-14), numbered relative to the start of the alpha helix region, which can have wide variety of unknown structures, i.e., No Structure-Function correlation of the claimed mutated zinc finger protein or nuclease (polypeptide) that is required for fulfilling Written Description requirement.
As discussed in the written description guidelines the Written Description requirement for a claimed genus may 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. A representative number of species means that the species, which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
Furthermore, the genus of polypeptides required in the claimed invention is an extremely large structurally and functionally variable genus. While the argument can be made that the recited genus of polypeptides is adequately described by the disclosure of the structures of prior art. However, the art clearly teaches the “Practical Limits of Function Prediction”: Whisstock et al., (2003) highlight the difficulties associated with “Prediction of protein function from protein sequence and structure”; “To reason from sequence and structure to function is to step onto much shakier ground”, closely related proteins can change function, either through divergence to a related function or by recruitment for a very different function, in such cases, assignment of function on the basis of homology, in the absence of direct experimental evidence, will give the wrong answer, it is difficult to state criteria for successful prediction of function, since function is a vague concept. This finding is reinforced in the following scientific teachings for specific proteins in the art that suggest, even highly structurally homologous polypeptides do not necessarily share the same function and many functionally similar proteins will have little or no structural homology to disclosed proteins. For example, proteins having similar structure have different activities (structure does not always correlate to function); Witkowski et al., (1999) teaches that one conservative amino acid substitution transforms a -ketoacyl synthase into a malonyl decarboxylase and completely eliminates -ketoacyl synthase activity. Similarly, the art also teaches that functionally similar molecules have different structures; Kisselev L., (2002) teach that polypeptide release factors in prokaryotes and eukaryotes have same function but different structures.
Claims are drawn to very broadly any or all zinc finger protein or nuclease (polypeptide) derived from many unknown sources having any unknown structure, any FokI cleavage domain and any zinc finger DNA-binding domain numbered relative to alpha-helix region comprises at least one or more mutations in amino acid residues (-5), (-9) and/or (-14), numbered relative to the start of any alpha helix region, which can have wide variety of unknown structure, whose structures are not fully described in the specification. No information, beyond the characterization of zinc finger protein or nuclease (polypeptide) having 4 zinc finger DNA-binding domain comprising FokI cleavage domain, with few substitution mutations has been provided, which would indicate that applicants had possession of the claimed genus. The specification does not contain sufficient disclosure of the structure with function of all the zinc finger proteins or nucleases (polypeptides) having FokI cleavage domain s within the scope of the claimed genus. The genus of polypeptides claimed is a large variable genus including many mutants, variant and fragments thereof, which can have wide variety of structures. Therefore, many structurally unrelated zinc finger protein or nucleases (polypeptides) enzymes having FokI cleavage domain within the scope of these claims. The specification discloses the structure of only few representative species of the claimed genus with few mutations, which is insufficient to put one of skill in the art in possession of the attributes and features of all species within the claimed genus. Therefore, one skilled in the art cannot reasonably conclude that applicant had possession of the claimed invention at the time the instant application was filed.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Arguments: Applicants argue that The Office alleged that the claims are drawn to any zinc finger protein having any structural feature comprising 3 to 6 any zinc finger DNA-binding domains wherein each zinc finger DNA- binding domain comprises two beta sheets, an alpha helix, and a recognition helix region that binds to a nucleotide sequence, and further wherein one or more of the zinc finger DNA-binding domains comprise mutations in any one or more of amino acid residues (-5), (-9), or (-14), numbered relative to the start of the alpha helix region, which can have wide variety of unknown structures. Therefore, the Office alleged that the specification is insufficient to put one of skill in the art in possession of the attributes and features of all species within the claimed genus. Applicant respectfully disagrees, and in a sincere effort to advance prosecution, claim 1 is amended to recite A zinc finger protein comprising at least 4 zinc finger DNA-binding domains, wherein each zinc finger DNA-binding domain comprises two beta sheets, an alpha helix, and a recognition helix region that binds to a nucleotide sequence, and further wherein one or more of the zinc finger DNA-binding domains comprise a mutation in any one or more of amino acid residues (-5), (-9), or (-14), numbered relative to the start of the alpha helix of a Zif268 backbone, wherein the one or more of amino acid residues (-5), (-9), or (-14) are mutated to an alanine (A), a leucine (L), a serine (S), an aspartic acid (N), glutamine (E), tyrosine (Y), or glutamine (Q) residue. Accordingly, claim 1 is directed to a zinc finger protein comprising specific mutations numbered relative to the start of an alpha helix region of the Zif268 backbone, wherein positions (-5), -(9), and (-14) are modified with negatively charged residues A, L, S, N, E, Y, or Q. Moreover, Applicant has demonstrated that the claimed modifications result reduced off-target binding and increased specificity of ZFPs across various target sites. Thus, the skilled artisan would readily understand upon reviewing Applicant's specification and experimental data that the claimed modifications numbered relative to the alpha helix region of the Zif268 backbone would invariably result in increased specificity and decreased off-target binding regardless of the specific sequence of the DNA binding domain or functional domain of the ZFP, which is due to the abatement of the non-specific ion pair interactions that result from interactions between the DNA phosphate backbone and the positively charged residues at positions (-5), -(9), and (-14). As described in Applicant's specification, Applicant discovered that the DNA binding domains in zinc finger sequences comprise amino acid residues that take part in non-specific ion pair interactions with the phosphates of the DNA backbone. Applicant's Specification, at paragraph [0006] ("Since phosphate groups are found all along the DNA backbone, this type of interaction between the zinc finger and a DNA molecule is generally considered to be non- sequence specific."). Further, these interactions may give rise to off-target activity of the DNA binding domains. Id. Applicant has discovered that mutations at specific positions within the zinc finger sequence backbone can maintain on-target activity while decreasing off-target activity. Id at Example 3. As provided in the experimental examples, novel engineered zinc finger proteins with backbone mutations at positions (-5), (-9) and/or (-14) demonstrated highly specific cleavage and significant decreases in off-target activity. Id. at In fact, Applicant tested both on target and off- target cleavage results among mutants across a variety of residues (e.g., an alanine (A), a leucine (L), a serine (S), an aspartic acid (D), glutamic acid (E), tyrosine (Y) or glutamine (Q)) and target sites, confirming maintained on-target and reduced off-target cleavage when residues at positions (-5), (-9) and/or (-14) were replaced with negatively charged or neutral residues. Id. at example 3, as well as Tables 1OA and 1OB. Moreover, Tables 6A-C and FIGs. 7A and 7B demonstrate that on-target cleavage activity remained robust, while activity at key off-target sites decreased substantially: These experiments demonstrated that these mutations could have an impact on off-target cleavage. For example, while on-target cleavage was maintained at a robust level for the 52742-F 1RQ;F3RQ;F5RQ mutant (69.96% on-target activity compared with 62.59% activity for the parent proteins at the 6 g dose), off-target cleavage dropped (OT16 showed 19.16% cleavage activity for the parent proteins and 1.43% activity in the triple mutant). Therefore, Applicant has sufficiently demonstrated that substitutions of positively charged residues at positions (-5), (-9) and/or (-14) in the zinc finger backbone with negative or neutral residues, such as alanine (A), a leucine (L), a serine (S), an aspartic acid (N), glutamine (E), tyrosine (Y) and/or glutamine (Q) residue demonstrate maintained specificity alongside decreased off-target activity. Moreover, the skilled artisan would recognize that mutations at the recited positions may be combined with various DNA-binding domains or functional domains while still maintaining increased specificity and decreased off-target activity regardless of the specific target sequence. This is evidenced by way of the experimental examples demonstrating increased specificity and binding affinity of ZFPs including the claimed substitutions across a variety of target sites and ZFP mutants that invariably results from the substitution of positively charged residues at positions (-5), (-9), or (-14) with negatively or neutrally charged residues A, L, S, N,E,Y,or Q. Thus, the skilled artisan would readily expect that a ZFP comprising two beta sheets, an alpha helix, and a recognition helix would inherently benefit from the incorporation of the claimed substitutions at the claimed positions relative to the start of the alpha helix region of the Zif268 backbone regardless of any additional mutations present in the ZFP. Specifically, the skilled artisan would readily understand a ZFP comprising the claimed substitutions would outperform analogous ZFPs lacking the claimed modifications with respect to binding activity due to negation of the non-specific ion pair interactions with the phosphates of the DNA backbone present in ZFPs lacking the claimed modification.
Response: Applicant’s lengthy arguments have been fully considered but are not deemed persuasive to overcome the rejection of claims 1, 3-6 (
Note: The rejection of claims
The examiner acknowledges the amendment to the claims 1 (Broad independent claim), no description about Structure-Function Correlation of ZFP protein, and disagrees with the applicants contention in a long arguments that the claimed invention is adequately described. The Examiner draws the attention of the Applicants for withdrawn rejection under 112(a) of claims (
Claim 1 is directed a genus of protein any or all zinc finger protein or nuclease (polypeptide) derived from many unknown sources having any structure, and any FokI cleavage domain and any zinc finger DNA-binding domain numbered relative to alpha-helix region comprises at least one or more mutations in amino acid residues (-5), (-9) and/or (-14), numbered relative to the start of any alpha helix region, which can have wide variety of unknown structure, whose structures are not fully described in the specification. No information, beyond the characterization of zinc finger protein or nuclease (polypeptide) having 3-6 zinc finger DNA-binding domain comprising FokI cleavage domain, with few substitution mutations has been provided, which would indicate that applicants had possession of the claimed genus. The specification does not contain sufficient disclosure of the structure with function of all the zinc finger proteins or nucleases (polypeptides) having FokI cleavage domains within the scope of the claimed genus. The genus of polypeptides claimed is a large variable genus including many mutants, variant and fragments thereof, which can have wide variety of structures. Therefore, many structurally unrelated zinc finger protein or nucleases (polypeptides) enzymes having FokI cleavage domain within the scope of these claims. The specification discloses the structure of only few representative species of the claimed genus with few mutations, which is insufficient to put one of skill in the art in possession of the attributes and features of all species within the claimed genus. Therefore, one skilled in the art cannot reasonably conclude that applicant had possession of the claimed invention at the time the instant application was filed because ZFP protein of SEQ ID NO: 1 composed of 579 amino acids, and applicants .described only 3 positions such as (-5), (-9) and/or (-14), which does not represent entire genus.
As discussed in the written description guidelines the written description requirement for a claimed genus may 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. A representative number of species means that the species, which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. The genus of proteins ZFP, folk1 or nuclease that comprise the claimed protein is a large variable genus with potentiality of encoding many different proteins from different sources (such as human, bacterial strains like E. coli. Therefore, many functionally unrelated and many non-functional proteins are encompassed within the scope of these claims. The specification discloses only a single species of the claimed genus of protein of the sequence encoding SEQ ID NO: 1, which is insufficient to put one of skill in the art in possession of the attributes and features of all species within the claimed genus. Thus, the claimed genus is not sufficiently described in either structure or function. Therefore, one skilled in the art cannot reasonably conclude that the applicant had possession of the claimed invention at the time the instant application was filed.
Therefore, the rejection on WD under 112(a) is maintained.
Conclusion
Status of the claims:
Allowable Subject Matter
Claims 7, 8, 10, and 11 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Claims 1, 3-6, 9, and 12 stand/are rejected.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action.
Applicants must respond to the objections/rejections in each of the sections in this Office action to be fully responsive in prosecution. 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 extension fee pursuant to 37 C.F.R. § 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to IQBAL H CHOWDHURY whose telephone number is (571)272-8137. The examiner can normally be reached on M-F, from 9:00-5:00 PM.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao, can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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Iqbal H. Chowdhury, PhD.
Primary Patent Examiner
Art Unit 1656 (Recombinant Enzymes and Protein Crystallography)
US Patent and Trademark Office
Ph. (571)-272-8137 and Fax (571)-273-8137
/IQBAL H CHOWDHURY/
Primary Examiner, Art Unit 1656
Prosecution Insights