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 .
Application Status
In response to Non-Final Office Action mailed on 11/09/2025, applicants’ response and amendments dated 04/20/2026 is acknowledged; in said amendment applicants’ have amended claims 16-17 and 24. Thus, amended claims 16-30 are pending in this application and is now under consideration for examination. Rejections and/or objections not reiterated from previous office action are hereby withdrawn.
Claims 16-30 are pending in this application, elected Group I, claims 16-19 and 24, and SEQ ID NOs 1, 2, 3, 29 and 36 reading on the elected invention is now under consideration for examination, examiner also reiterates the election is a SEQUENCE election and not a species election; and claims 20-23 and 25-30 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 10/30/2025.
Maintained-Priority
Acknowledgment is also made of applicants’ claim for foreign priority under 35 U.S.C. 119(a)-(d). This application is 371 of PCT/EP2021/064642 filed 06/01/2021 and claims the priority date of EPO Applications: 20178333.9 filed on 06/04/2020 and 21160103.4 filed on 03/02/2021. Note elected SEQ ID NOs: 29 and 36 are only granted the priority date of EPO Application 21160103.4 filed on 03/02/2021.
Maintained-Claim Rejections: 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(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.
Enablement
Claims 16-19 and 24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112, first paragraph, because the specification, while being enabling for an isolated wild-type santalene synthase comprising the amino acid sequence of SEQ ID NO: 1 and specific variants of said santalene synthase comprising the amino acid sequences of SEQ ID NOs: 2, 3, 29 and 36, does not reasonably provide enablement for any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”). The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and or use the invention commensurate in scope with the claim.
Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 8 USPQ 2nd 1400 (Fed. Cir. 1988)) as follows: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claim(s).
Claims 16-19 and 24 are so broad as to encompass: any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”). The scope of the claims is not commensurate with the enablement provided by the disclosure with regard to the extremely large number polypeptides and encoding polynucleotides broadly encompassed by the claims. Since the amino acid sequence of a protein encoded by a polynucleotide determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires knowledge and guidance with regard to which amino acids in the protein's sequence and the respective codons in its polynucleotide, if any, are tolerant of modification and which are conserved (i.e., expectedly intolerant to modification), and detailed knowledge of the ways in which the encoded proteins' structure relates to its function. In view of the broad breadth of the claims, the amount of experimentation required to determine the structure of all the polypeptides or the encoding polynucleotides from any plant source including variants, mutants and recombinants, the lack of guidance, working examples, and unpredictability of the art in predicting function from a polypeptide primary structure (e.g., see Whisstock et al., Q Rev Biophys. 2003 Aug; 36(3): 307-340), practicing the claimed invention would require undue experimentation. As such, the specification fails to enable the entire scope of the claimed invention.
However, in this case the disclosure is limited to an isolated wild-type santalene synthase comprising the amino acid sequence of SEQ ID NO: 1 and specific variants of said santalene synthase comprising the amino acid sequences of SEQ ID NOs: 2, 3, 29 and 36, but provides no guidance with regard to the making and using of any santalene synthase comprising said motifs including variants and mutants and having the recited catalytic activity and biochemical properties; i.e., any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”) or with regard to other uses. In view of the great breadth of the claims, amount of experimentation required to make the claimed polypeptides and encoding polynucleotides, the lack of guidance, working examples, and unpredictability of the art in predicting function from a polypeptide primary structure (e.g., see Whisstock et al., Q Rev Biophys. 2003 Aug; 36(3): 307-340), the claimed invention would require undue experimentation. As such, the specification fails to teach one of ordinary skill how to make and use the full scope of polypeptides and encoding polynucleotides encompassed by the claims.
While enzyme isolation techniques, recombinant and mutagenesis techniques are known, and it is not routine in the art to screen for multiple substitutions or multiple modifications as encompassed by the instant claim, the specific amino acid positions within a protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions or deletions.
The specification does not support the broad scope of the claims which encompass: any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”) because the specification does not establish: (A) regions of the protein/polynucleotide structure which may be modified without affecting the activity of the encoded santalene synthase; (B) the general tolerance of the polypeptide and the polynucleotide encoding santalene synthase to modification and extent of such tolerance; (C) a rational and predictable scheme for modifying any amino acid residue or the respective codon in the polynucleotide with an expectation of obtaining the desired biological function; and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful.
Thus, applicants’ have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claim broadly including polypeptides and encoding polynucleotides with an enormous number of modifications including variants, mutants and recombinants of undefined and undefined structures with the associated function. The scope of the claim must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of polypeptides having the desired biological characteristics is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Applicants’ have traversed the above 35 U.S.C. 112(a) rejection for enablement with the following arguments and submission of a Rule 1.132 Declaration of inventor Dr. Mathew Styles: (see pages 10-11 of Applicants’ REMARKS dated 04/20/2026).
Applicants’ argue: “As noted above, submitted herewith is a Rule 1.132 Declaration of Dr. Matthew Styles. Dr. Styles notes in part that "[t]erpene synthases tend to share very high structural homology but rather low sequence identity." Decl. at para. 10. As such, it was determined that increased flexibility corresponding to a specific portion of that structural homology was able to, for the first time, lead to production of more beta-santalene than alpha-santalene. Id. at para. 11 and 12. With this information it is possible to extend to all existing santalene synthase enzymes. Id. at 13. As seen in paragraph 12 of the declaration, the instant inventors determined that an increase in fluctuation in the protein region of a particular location led to an increase in beta santalene production, when previously no enzymes were known that could produce an even or greater amount of beta santalene. "Once it was determined which portion of the structure is amenable to such alteration, it is possible to apply this teaching to all existing santalene synthase enzymes. Decl. at 13. Once this effect is found, the ordinary skilled artisan would be able to identify mutations that would lead to that increased flexibility, and apply the teachings to all known santalene synthases. Id. at 14. This effect can be seen in similar publications, even with a relatively low sequence identity. Id. at 15. In short, with the relative structural similarity of known santalene synthase enzymes, the ordinary skilled artisan would have easily been able to apply the teachings of the instant application to all known santalene synthases, and the inventors had possession of the full scope of the claimed invention.”
Reply: Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Examiner is maintaining the rejection for reasons made of record in the Office-action dated 11/19/2025 and additionally for the following reasons.
The Declaration under 37 CFR 1.132 filed 04/20/2026 is insufficient to overcome the rejection of claims16-19 and 24 based upon 35 U.S.C. 112(a) for enablement as set forth in the last Office action dated 11/19/2025 because: At the outset claim 16 as amended i.e., “comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1”, is not clear and confusing, because the resulting claims do not define the metes and bound of the desired patent protection. It is not clear whether the phrase “tertiary portion” refers to tertiary structure/3-D configuration formed by the amino acids residues 272-291 spanning the region of SEQ ID NO: 1? and examiner maintains the position for amino acid residues 272-291 of SEQ ID NO: 1 to adopt any tertiary structure/3-D configuration remainder of the molecule structure should be defined. It is also not clear regarding the scope of the phrase “corresponding” and is interpreted as not limited to 272 to 291 of SEQ ID NO: 1, as “corresponding” is not limited to “comprising or consisting of” and includes any synthetic beta santalene synthase of undefined and limited structures and includes many undefined “tertiary” structural region/amino acid residues. Examiner maintains the position that “calculating the Root Mean Squared Fluctuation (RMSF) for the parent synthase” is limited to a method of screening and does not provide any support for any specific structure or any mutant structure and thus the claimed subject-matter and claims as written encompasses any synthetic beta santalene synthase of unlimited and undefined structures characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24) and not limited to specific mutants of SEQ ID NOs: 1-3, 29, 57 or 58. The Declaration under 37 CFR 1.132 filed on 04/20/2026 provides arguments and cites the study/evidence of a recent publication CN119391681 A, and examiner takes the position that the cited reference CN119391681 A is also limited a specific wild-type santalene synthase having a specific structure and specific defined mutations in said wild-type santalene synthase and thus supports examiner’s position (see pages 3-4 and Table 1 of Declaration under 37 CFR 1.132 filed 04/20/2026).
Maintained-Written Description
Claims 16-19 and 24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112, first paragraph, as containing 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(s), at the time the application was filed, had possession of the claimed invention.
Claims 16-19 and 24 as interpreted is directed to encompass: any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”).
In University of California v. Eli Lilly & Co., 43 USPQ2d 1938, 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”. As indicated in MPEP § 2163, 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 that Applicant was in possession of the claimed genus. In addition, MPEP § 2163 states that 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.
In the instant case the scope of the instant claims encompass a genus of structures (no structural limitation) for polypeptides and the encoding polynucleotides of interest with associated function, i.e., any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”).
No information, beyond the characterization of an isolated wild-type santalene synthase comprising the amino acid sequence of SEQ ID NO: 1 and specific variants of said santalene synthase comprising the amino acid sequences of SEQ ID NOs: 2, 3, 29 and 36, has been provided by the applicants’, which would indicate that they had possession of the claimed genus of structures (no structural limitation) for polypeptides of interest with associated function and their encoding polynucleotides, i.e., any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”).
The art also teaches, even highly structurally homologous polypeptides do not necessarily share the same function and conversely functionally similar molecules do not necessarily have similar structures. For example proteins having similar structure have different activities; Witkowski et al., (Biochemistry 38:11643-11650, 1999) teaches that one conservative amino acid substitution transforms a b-ketoacyl synthase into a malonyl decarboxylase and completely eliminates b-ketoacyl synthase activity. Similarly, Wishart et al., (J. Biol. Chem., 1995, Vol. 270(10): 26782-26785) teach that a single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase.
Hence, the recited genera of polypeptides and the encoding polynucleotides are interpreted to have widely variable structures, since minor changes may result in changes affecting function and no additional information correlating structure with function has been provided. Therefore, given the lack of description of representative species encompassed by the genus of polypeptides, encoding polynucleotides and modifications, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants’ were in possession of the claimed invention. Applicants’ are referred to the revised guidelines concerning compliance with the written description requirement of 35 U.S.C. 112(a) or 35 U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Applicants’ have traversed the above 35 U.S.C. 112(a) rejection for written-description with the following arguments and submission of a Rule 1.132 Declaration of inventor Dr. Mathew Styles: (see pages 11-12 of Applicants’ REMARKS dated 04/20/2026).
Applicants’ argue: “As noted above, submitted herewith is a Rule 1.132 Declaration of Dr. Matthew Styles. Dr. Styles notes in part that "[t]erpene synthases tend to share very high structural homology but rather low sequence identity." Decl. at para. 10. As such, it was determined that increased flexibility corresponding to a specific portion of that structural homology was able to, for the first time, lead to production of more beta-santalene than alpha-santalene. Id. at para. 11 and 12. With this information it is possible to extend to all existing santalene synthase enzymes. Id. at 13. As seen in paragraph 12 of the declaration, the instant inventors determined that an increase in fluctuation in the protein region of a particular location led to an increase in beta santalene production, when previously no enzymes were known that could produce an even or greater amount of beta santalene. "Once it was determined which portion of the structure is amenable to such alteration, it is possible to apply this teaching to all existing santalene synthase enzymes. Decl. at 13. Once this effect is found, the ordinary skilled artisan would be able to identify mutations that would lead to that increased flexibility, and apply the teachings to all known santalene synthases. Id. at 14. This effect can be seen in similar publications, even with a relatively low sequence identity. Id. at 15. In short, with the relative structural similarity of known santalene synthase enzymes, the ordinary skilled artisan would have easily been able to apply the teachings of the instant application to all known santalene synthases, and the inventors had possession of the full scope of the claimed invention.”
Reply: Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Examiner is maintaining the rejection for reasons made of record in the Office-action dated 11/19/2025 and additionally for the following reasons.
The Declaration under 37 CFR 1.132 filed 04/20/2026 is insufficient to overcome the rejection of claims16-19 and 24 based upon 35 U.S.C. 112(a) for enablement as set forth in the last Office action dated 11/19/2025 because: At the outset claim 16 as amended i.e., “comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1”, is not clear and confusing, because the resulting claims do not define the metes and bound of the desired patent protection. It is not clear whether the phrase “tertiary portion” refers to tertiary structure/3-D configuration formed by the amino acids residues 272-291 spanning the region of SEQ ID NO: 1? and examiner maintains the position for amino acid residues 272-291 of SEQ ID NO: 1 to adopt any tertiary structure/3-D configuration remainder of the molecule structure should be defined. It is also not clear regarding the scope of the phrase “corresponding” and is interpreted as not limited to 272 to 291 of SEQ ID NO: 1, as “corresponding” is not limited to “comprising or consisting of” and includes any synthetic beta santalene synthase of undefined and limited structures and includes many undefined “tertiary” structural region/amino acid residues. Examiner maintains the position that “calculating the Root Mean Squared Fluctuation (RMSF) for the parent synthase” is limited to a method of screening and does not provide any support for any specific structure or any mutant structure and thus the claimed subject-matter and claims as written encompasses any synthetic beta santalene synthase of unlimited and undefined structures characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24) and not limited to specific mutants of SEQ ID NOs: 1-3, 29, 57 or 58. The Declaration under 37 CFR 1.132 filed on 04/20/2026 provides arguments and cites the study/evidence of a recent publication CN119391681 A, and examiner takes the position that the cited reference CN119391681 A is also limited a specific wild-type santalene synthase having a specific structure and specific defined mutations in said wild-type santalene synthase and thus supports examiner’s position (see pages 3-4 and Table 1 of Declaration under 37 CFR 1.132 filed 04/20/2026).
Maintained-Claim Rejections: 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title
Claims 16-19 and 24 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Claims 16-19 and 24 is directed to a law of nature or a natural phenomenon. Claims 16-19 and 24 as interpreted are directed to any synthetic beta santalene synthase of unlimited and undefined structures comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1, characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase from which the synthetic beta santalene synthase is derived, wherein the flexibility is determined by root mean square fluctuation analysis… has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24); any synthetic beta santalene synthase of unlimited structures producing beta-santalene and alpha-santalene from farnesyl pyrophosphate, wherein the santalene synthase has at least 50% sequence identity to a. the amino acid positions 261 to 278, 261 to position 272, of SEQ ID NO: 2, 3, 29, 57 or 58 wherein the position corresponding to position 261 of SEQ ID NO. 2, 3, 29, 57 or 58 is an Arginine residue and the position corresponding to position 278 of SEQ ID NO: 2, 3, 29, 57 or 58 is a Proline residue and said Arginine and said Proline are used to align the two protein sequences for the sequence identity determination; or b. … or c. a combination of a. and b. above; or d. the full-length of SEQ ID NO: 1 e. a combination of any of a. to c. above with d (as in claim 17, the limitations in claim 17 are recited in the alternative forms “or”). The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception for the reasons stated below.
The “2014 Interim Guidance on Patent Subject Matter Eligibility” 79 FR 74618 (Dec. 16, 2014) directs that claims drawn to 1) a composition of matter, 2) a law of nature or a natural phenomenon and 3) lacking recitation of additional elements that make the claims directed to significantly more than a judicial exception are ineligible for patenting under 35 U.S.C. 101. See, 79 FR, page 74621 (flow chart). Nature-based compositions of matter are not directed to significantly more than a judicial exception when the claimed "naturally occurring products and some man-made products ... are essentially no different from a naturally occurring product ... that fall under the laws of nature or natural phenomena exception.” 79 FR, page 74623, left column. That is, a patent-eligible composition of matter must be "markedly different" in terms of the "product's structure, function, and/or other properties." 79 FR, page 74623, center column. Further, processes directly to isolating nature-based compositions of matter have also been found to be directed to nothing more than a judicial exception when only routine purification techniques are employed. 79 FR, page 74622, center column (e.g. isolating DNA or other nature-based products).
Here, naturally-occurring variant polypeptides of SEQ ID NO: 1 (wild-type sequence) annotated as santalene synthase, and variants comprising an amino acid substitution corresponding to amino acid residues N267S and I291V of SEQ ID NO: 1, annotated as terpinol synthase and encoding polynucleotide sequence is disclosed: see (i) Di Girolamo et al., UniProtKB/TrEMBL Accesion#A0A7S6HRZ4 having 100% sequence identity to SEQ ID NO: 1 and naturally-occurring variant UniProtKB/TrEMBL Accession# A0A7S6L0M3 having 95.8% to SEQ ID NO: 1 and comprising amino acid residue 267S of the instant application; and (ii) Chaw et al., UniProtKB/TrEMBL Accesion#A0A3S3Q284 disclose naturally-occurring variants having 92.8%-89.8% sequence identities to SEQ ID NOs: 1-3, 29 and 36 of the instant invention, comprising amino acid substitutions corresponding to N267S and I291V of SEQ ID NO: 1, annotated as terpinol synthase and encoding polynucleotide. The features of claims 16-19 and 24 is met by the reference polypeptides in the disclosed references above. Since the features of the claims are met by the structure of a polypeptides of SEQ ID NO: 1-3, 29 and 36 of the instant application and the claims do not recite additional features or elements that amount to significantly more than the judicial exception, since the structure recited in claims 16-19 and 24 is "essentially no different from a naturally occurring product” such that there is no marked difference in the "product's structure, function, and/or other properties. As such, the claims 16-19 and 24 recite patent ineligible subject matter for the reasons stated.
Examiner also takes the following position regarding claims 16-19 and 24 are directed to a composition/product; Structure and function are inseparable, and if the structure is disclosed in the art, the claim is anticipated or reads on naturally-occurring polypeptide(s) and a method of determination of the property of the claimed polypeptide(s) language in preamble is given no patentable weight i.e., “characterized by the fact…, wherein the flexibility is determined by root mean square fluctuation analysis using simulations for 500 ns for both the synthetic and the naturally occurring santalene synthase with these settings: pH 8.0, 300 K, 1 atm, water environment, ions present without substrate, and evaluation for each enzyme structure on the last 450 ns of simulation; and wherein said synthetic beta santalene synthase is further characterized by its ability to produce beta-santalene and alpha-santalene in a ratio that is equal to or greater than 1 under typical conditions suitable for the production of both these santalenes, wherein beta-santalene is (-)-p-santalene” is not given any patentable weight as the claims are directed to a product.
• The body of the claim following the preamble is a self-contained description of the structure and does not depend on the preamble for completeness.
• A preamble that describes the purpose or intended use of the claimed invention generally does not limit the claims.
• The preamble merely extols benefits or features of the claimed invention and there is no clear reliance on those benefits or features as patentably significant (e.g., preamble recites, “[a] head for a lacrosse stick which provides improved handling and playing characteristics.”).
See: MPEP 2111.02 & 2111.02(II)
II. PREAMBLE STATEMENTS RECITING PURPOSE OR INTENDED USE
The claim preamble must be read in the context of the entire claim. The determination of whether preamble recitations are structural limitations or mere statements of purpose or use “can be resolved only on review of the entirety of the [record] to gain an understanding of what the inventors actually invented and intended to encompass by the claim.” Corning Glass Works, 868 F.2d at 1257,9 USPQ2d at 1966. If the body of a claim fully and intrinsically sets forth all of the limitations of the claimed invention and the preamble merely states, for example, the purpose or intended use of the invention, rather than any distinct definition of any of the claimed invention’s limitations, then the preamble is not considered a limitation and is of no significance to claim construction. Pitney Bowes, Inc. v. Hewlett-Packard Co., 182 F.3d1298, 1305, 51 USPQ2d 1161, 1165 (Fed. Cir. 1999). See also Rowe v. Dror, 112 F.3d 473, 478, 42 USPQ2d 1550,1553 (Fed. Cir. 1997) (“where a patentee defines a structurally complete invention in the claim body and uses the preamble only to state a purpose or intended use for the invention, the preamble is not a claim limitation”); Kropa v. Robie, 187 F.2d at 152, 88 USPQ2d at 480-81 (preamble is not a limitation where claim is directed to a product and the preamble merely recites a property inherent in an old product defined by the remainder of the claim); STX LLC. v. Brine, 211 F.3d 588, 591, 54USPQ2d 1347, 1350 (Fed. Cir. 2000) (holding that the preamble phrase “which provides improved playing and handling characteristics” in a claim drawn to a head fora lacrosse stick was not a claim limitation).
During examination, statements in the preamble reciting the purpose or intended use of the claimed invention must be evaluated to determine whether the recited purpose or intended use results in a structural difference (or, in the case of process claims, manipulative difference) between the claimed invention and the prior art. In re Sinex, 309 F.2d 488, 492, 135 USPQ 302, 305(CCPA 1962) (statement of intended use in an apparatus claim did not distinguish over the prior art apparatus). If a prior art structure is capable of performing the intended use as recited in the preamble, then it meets the claim.
See also Catalina Mktg. Int’l v. Coolsavings.com, Inc.,289 F.3d at 808-09, 62 USPQ2d at 1785 (“[C]lear reliance on the preamble during prosecution to distinguish the claimed invention from the prior art transforms the preamble into a claim limitation because such reliance indicates use of the preamble to define, in part, the claimed invention.…Without such reliance, however, a preamble generally is not limiting when the claim body describes a structurally complete invention such that deletion of the preamble phrase does not affect the structure or steps of the claimed invention.” Consequently, “preamble language merely extolling benefits or features of the claimed invention does not limit the claim scope without clear reliance on those benefits or features as patentably significant.”).
Applicants’ have traversed the above 35 U.S.C. 101 with the following arguments and submission of a Rule 1.132 Declaration of inventor Dr. Mathew Styles: (see page 12 of Applicants’ REMARKS dated 04/20/2026).
Applicants’ argue: “Claim 16 requires in part (a) a synthetic santalene synthase and (b) increased flexibility in a structural portion of that synthase compared to the naturally occurring enzyme from which it is derived. As such, the claim requires altering a naturally occurring enzyme by increasing flexibility in a certain portion. As set forth by Dr. Styles, it is only through this alteration that it was possible to produce beta santalene in an amount that equated or exceeded production of alpha santalene. This amounts to significantly more than any known naturally occurring santalene synthase, and withdrawal of the rejection is respectfully requested.”
Reply: Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Examiner is maintaining the rejection for reasons made of record in the Office-action dated 11/19/2025 and additionally for the following reasons. Examiner maintains the position that the cited references meets the limitation of claims as written 16-19 and 24 and as interpreted (see provided sequence alignments).
The Declaration under 37 CFR 1.132 filed 04/20/2026 is insufficient to overcome the rejection of claims16-19 and 24 based upon 35 U.S.C. 112(a) for enablement as set forth in the last Office action dated 11/19/2025 because: At the outset claim 16 as amended i.e., “comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1”, is not clear and confusing, because the resulting claims do not define the metes and bound of the desired patent protection. It is not clear whether the phrase “tertiary portion” refers to tertiary structure/3-D configuration formed by the amino acids residues 272-291 spanning the region of SEQ ID NO: 1? and examiner maintains the position for amino acid residues 272-291 of SEQ ID NO: 1 to adopt any tertiary structure/3-D configuration remainder of the molecule structure should be defined. It is also not clear regarding the scope of the phrase “corresponding” and is interpreted as not limited to 272 to 291 of SEQ ID NO: 1, as “corresponding” is not limited to “comprising or consisting of” and includes any synthetic beta santalene synthase of undefined and limited structures and includes many undefined “tertiary” structural region/amino acid residues. Examiner maintains the position that “calculating the Root Mean Squared Fluctuation (RMSF) for the parent synthase” is limited to a method of screening and does not provide any support for any specific structure or any mutant structure and thus the claimed subject-matter and claims as written encompasses any synthetic beta santalene synthase of unlimited and undefined structures characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24) and not limited to specific mutants of SEQ ID NOs: 1-3, 29, 57 or 58. The Declaration under 37 CFR 1.132 filed on 04/20/2026 provides arguments and cites the study/evidence of a recent publication CN119391681 A, and examiner takes the position that the cited reference CN119391681 A is also limited a specific wild-type santalene synthase having a specific structure and specific defined mutations in said wild-type santalene synthase and thus supports examiner’s position (see pages 3-4 and Table 1 of Declaration under 37 CFR 1.132 filed 04/20/2026).
Maintained-Claim Rejections: 35 USC § 102 (AIA )
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 16-19 and 24 are rejected under 35 U.S.C. 102(a)(1) and 35 U.S.C. 102(a)(2) as being anticipated by (i) Chaw et al., UniProtKB/TrEMBL Accesion#A0A3S3Q284 disclose naturally-occurring variants having 92.8%-89.8% sequence identities to SEQ ID NOs: 1-3, 29 and 36 of the instant invention, comprising amino acid substitutions corresponding to N267S and I291V of SEQ ID NO: 1, annotated as terpinol synthase and encoding polynucleotide (see provided sequence alignments); and (ii) Beekwilder et al., (US 11,390,863), disclose santalene synthase having 100% sequence identity to SEQ ID NO: 1 of the instant invention, and additionally variant having 95.9% sequence identity to SEQ ID NO: 1 and comprising an amino acid substitution corresponding to amino acid residue N267S of SEQ ID NO: 1 and encoding polynucleotide sequence of the instant application (see Fig. 10-11; col. 4, lines 16-42; and provided sequence alignments), and the cited references are deemed to anticipate claims 16-19 and 24 as written and when given the broadest reasonable interpretation.
2112 [R-3] Requirements of Rejection Based on Inherency; Burden of Proof The express, implicit, and inherent disclosures of a prior art reference may be relied upon in the rejection of claims under 35 U.S.C. 102 or 103. “The inherent teaching of a prior art reference, a question of fact, arises both in the context of anticipation and obviousness.” In re Napier, 55 F.3d 610, 613, 34 USPQ2d 1782, 1784 (Fed. Cir. 1995) (affirmed a 35 U.S.C. 103 rejection based in part on inherent disclosure in one of the references). See also In re Grasselli, 713 F.2d 731, 739, 218 USPQ 769, 775 (, X7Fed. Cir. 1983).
I. SOMETHING WHICH IS OLD DOES NOT BECOME PATENTABLE UPON THE DIS-COVERY OF A NEW PROPERTY
II. INHERENT FEATURE NEED NOT BE RECOGNIZED AT THE TIME OF THE INVENTION
III. A REJECTION UNDER 35 U.S.C. 102/103 CAN BE MADE WHEN THE PRIOR ART PRODUCT SEEMS TO BE IDENTICAL EXCEPT THAT THE PRIOR ART IS SILENT AS TO AN INHERENT CHARACTERISTIC
Applicants’ have traversed the above 35 U.S.C. 102 with the following arguments and submission of a Rule 1.132 Declaration of inventor Dr. Mathew Styles: (see pages 12-13 of Applicants’ REMARKS dated 04/20/2026).
Applicants’ argue: “Claim 16 requires (a) a synthetic santalene synthase, (b) increased flexibility in a structural portion of that synthase compared to the naturally occurring enzyme from which it is derived, and (c) wherein said synthetic beta santalene synthase is further characterized by its ability to produce beta-santalene and alpha-santalene in a ratio that is equal to or greater than 1 under typical conditions suitable for the production of both these santalenes, wherein beta- santalene is (-)-B-santalene (CAS number 511-59-1). As noted by Dr. Styles in his declaration, until the instant inventors determined the effect of increasing flexibility in a certain portion of santalene synthase enzymes (of which all known enzymes have similar structure), there were no enzymes that were capable of producing 50% or more beta santalene when compared with alpha santalene. Decl. at 9 ("Up to this point, the only known santalene synthase enzymes produced a majority of alpha-santalene.") and 10. This would have been the case for the prior art enzymes relied upon by the Examiner, and withdrawal of the rejection is respectfully requested.”
Reply: Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Examiner is maintaining the rejection for reasons made of record in the Office-action dated 11/19/2025 and additionally for the following reasons. Examiner maintains the position that the cited references meets the limitation of claims as written 16-19 and 24 and as interpreted (see provided sequence alignments).
The Declaration under 37 CFR 1.132 filed 04/20/2026 is insufficient to overcome the rejection of claims16-19 and 24 based upon 35 U.S.C. 112(a) for enablement as set forth in the last Office action dated 11/19/2025 because: At the outset claim 16 as amended i.e., “comprising a tertiary portion corresponding to amino acid positions 272 to 291 of SEQ ID NO: 1”, is not clear and confusing, because the resulting claims do not define the metes and bound of the desired patent protection. It is not clear whether the phrase “tertiary portion” refers to tertiary structure/3-D configuration formed by the amino acids residues 272-291 spanning the region of SEQ ID NO: 1? and examiner maintains the position for amino acid residues 272-291 of SEQ ID NO: 1 to adopt any tertiary structure/3-D configuration remainder of the molecule structure should be defined. It is also not clear regarding the scope of the phrase “corresponding” and is interpreted as not limited to 272 to 291 of SEQ ID NO: 1, as “corresponding” is not limited to “comprising or consisting of” and includes any synthetic beta santalene synthase of undefined and limited structures and includes many undefined “tertiary” structural region/amino acid residues. Examiner maintains the position that “calculating the Root Mean Squared Fluctuation (RMSF) for the parent synthase” is limited to a method of screening and does not provide any support for any specific structure or any mutant structure and thus the claimed subject-matter and claims as written encompasses any synthetic beta santalene synthase of unlimited and undefined structures characterized by the fact that the tertiary structure of the part of said synthetic beta santalene synthase that correspond to the stretch from amino acid positions 272 to position 291 of SEQ ID NO: 1 has an increased flexibility compared to the flexibility of the same tertiary structure in a naturally occurring santalene synthase (only partial structure has been provided comprising certain amino acid residues and motif; remainder of the structure is undefined; as in claim 16, 18-19 and 24) and not limited to specific mutants of SEQ ID NOs: 1-3, 29, 57 or 58. The Declaration under 37 CFR 1.132 filed on 04/20/2026 provides arguments and cites the study/evidence of a recent publication CN119391681 A, and examiner takes the position that the cited reference CN119391681 A is also limited a specific wild-type santalene synthase having a specific structure and specific defined mutations in said wild-type santalene synthase and thus supports examiner’s position (see pages 3-4 and Table 1 of Declaration under 37 CFR 1.132 filed 04/20/2026).
Summary of Pending Issues
The following is a summary of issues pending in the instant application
Claims 16-19 and 24 are rejected under 35 U.S.C. 112(a) for enablement and written-description.
Claims 16-19 and 24 are rejected under 35 U.S.C. 101.
Claims 16-19 and 24 are rejected under 35 U.S.C. 102(a)(1) and 35 U.S.C. 102(a)(2) as being anticipated by (i) Chaw et al., UniProtKB/TrEMBL Accesion#A0A3S3Q284 disclose naturally-occurring variants having 92.8%-89.8% sequence identities to SEQ ID NOs: 1-3, 29 and 36 of the instant invention, comprising amino acid substitutions corresponding to N267S and I291V of SEQ ID NO: 1, annotated as terpinol synthase and encoding polynucleotide (see provided sequence alignments); and (ii) Beekwilder et al., (US 11,390,863), disclose santalene synthase having 100% sequence identity to SEQ ID NO: 1 of the instant invention, and additionally variant having 95.9% sequence identity to SEQ ID NO: 1 and comprising an amino acid substitution corresponding to amino acid residue N267S of SEQ ID NO: 1 and encoding polynucleotide sequence of the instant application.
Conclusion
None of the claims are allowable. Claims 16-19 and 24 are rejected for the reasons identified in the Rejections and Summary sections of this Office Action. Applicants’ must respond to the rejections in each of the sections in this Office Action to be fully responsive for prosecution.
THIS ACTION IS MADE FINAL. 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 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Regarding filing an After Final amendment, Applicants are directed to MPEP 714.13, which states:
II. ENTRY NOT A MATTER OF RIGHT
It should be kept in mind that applicant cannot, as a matter of right, amend any finally rejected claims, add new claims after a final rejection (see 37 CFR 1.116) or reinstate previously canceled claims. Except where an amendment merely cancels claims, adopts examiner suggestions, removes issues for appeal, or in some other way requires ONLY A CURSORY REVIEW by the examiner (e.g., typographical errors), compliance with the requirement of a showing under 37 CFR 1.116(b)(3) is expected in all amendments after final rejection. An affidavit or other evidence filed after a final rejection, but before or on the same date of filing an appeal, may be entered upon a showing of good and sufficient reasons why the affidavit or other evidence is necessary and was not earlier presented in compliance with 37 CFR 1.116(e). See 37 CFR 41.33 and MPEP § 1206 for information on affidavit or other evidence filed after appeal. (Examiner's emphasis) If more than a cursory review is required, Applicants are referred to CFR §1.114.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to GANAPATHIRAMA RAGHU whose telephone number is (571)272-4533. The examiner can normally be reached on M-F 8:30am-5pm 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, Robert Mondesi can be reached on 408-918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/GANAPATHIRAMA RAGHU/ Primary Examiner, Art Unit 1652
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