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
Claims 1-3 and 6-16 are pending and under examination.
The rejection of claims 4-5 under 35 U.S.C. 101 is withdrawn in light of the cancellation of the claims in the amendment dated 7/14/2026.
The rejection of claim 5 under 35 U.S.C. 112(d) is withdrawn in light of the cancellation of the claim in the amendment dated 7/14/2026.
The rejection of claims 1-2 and 5-6 under 35 U.S.C. 102(a)(1) is withdrawn in light of the claim amendment cancelling claim 5 and amending claims 1-2 to require a sequence identity of 90% or more to SEQ ID NO:1, and amending claim 6 to require a sequence identity of 95% or more to SEQ ID NO:1. Vrljic et al. does not teach an amino acid sequence having 90% or more identity to SEQ ID NO:1.
Priority
This application, filed on 4/3/2024, is a 371 of PCT/KR2022/016438 filed on 10/26/2022 and claims priority to REPUBLIC OF KOREA 10-2021-0143660 filed on 10/26/2021. The effective filing date is October 26, 2022.
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 1-3, 6-9 and new claims 11-13 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception, a naturally occurring protein, without significantly more.
The claims are directed to a LysE variant having a sequence identity of 90% of more with the amino acid sequence of SEQ ID NO:1, wherein an amino acid corresponding to position 50 of SEQ ID NO:1 is substituted with another amino acid (Step 1: Yes).
As identified by GenBank reference corresponding to accession number HLR48383 (deposited in GenBank on January 31, 2024; previously cited), a LysE family transporter from Corynebacterium sp. containing an F50I substitution was isolated from soil (Step 2A prong one: Yes). Sequence 1 (Subject) from KR102139806 B1 (published 7/30/2020) has 100% sequence identity with instant SEQ ID NO:1 (Query), as shown in the alignment below.
PNG
media_image1.png
334
792
media_image1.png
Greyscale
This judicial exception is not integrated into a practical application because the claims are drawn to a naturally occurring protein having a sequence identity of 90% or more with SEQ ID NO:1, and comprising a substitution in the amino acid corresponding to position 50 of SEQ ID NO:1, which is a naturally occurring mutation, and the claims do not recite any additional elements that integrate the judicial exception into a practical application (Step 2A prong two: No). Dependent claims 2-9 do not include any additional elements that are sufficient to amount to significantly more than the judicial exception.
The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception, because there is no difference in characteristics (structural, functional or otherwise) between the claimed polypeptide and the naturally occurring Corynebacterium glutamicum polypeptide (Step 2B: No).
Thus, claims 1-3, 6-9 and 11-13 are not eligible.
Response to Arguments
Applicant argues that applicant has amended independent claim 1, from which the remaining rejected claims depend, to recite at least one substitution for an amino acid corresponding to position 50, 153 or 215 of SEQ ID NO:1; accordingly the pending claims are directed to LysE variants having the recited substitution, and therefore are not directed to naturally occurring proteins (See Remarks dated 7/14/2026, p.5 – 35 US 101).
Applicant's arguments filed July 14, 2026 have been fully considered but they are not persuasive. As discussed in the rejection above, a naturally occurring LysE variant comprising an F50I substitution was isolated from soil, and LysE variants having 99% sequence identity to instant SEQ ID NO:1 occur naturally. Thus, the claimed LysE variants do not vary structurally, functionally or otherwise from the naturally occurring Corynebacterium glutamicum polypeptide, and is directed to a judicial exception.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 1-3 and 6-16 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claims contain 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, at the time the application was filed, had possession of the claimed invention.
Applicant is referred to MPEP 2163(II)(A)(3)(a)(i and ii), which states that 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 disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure indicates that the patentee has invented species sufficient to constitute the genus. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus.
Claims 1-3 are drawn to a LysE variant having a sequence identity of 90% or more with the amino acid sequence of SEQ ID NO:1, wherein any one or more amino acids of amino acids corresponding to positions 50, 153 and 215 of SEQ ID NO:1 are substituted with another amino acid.
Claim 6 is drawn to the LysE variant of claim 1, having 95% or more sequence identity to SEQ ID NO:1.
Claim 7 is drawn to a polynucleotide encoding the variant of claim 1.
Claims 8-9 are drawn to a microorganism of the genus Corynebacterium comprising a LysE variant, wherein any one or more amino acids of amino acids corresponding to positions 50, 153 and 215 of SEQ ID NO:1 are substituted with another amino acid, or a polynucleotide encoding the LysE variant.
Claim 10 is drawn to a method of producing L-arginine, the method comprising the step of culturing a microorganism of the genus Corynebacterium, the microorganism including a LysE variant, wherein any one or more amino acids of amino acids corresponding to positions 50, 153 and 215 of SEQ ID NO:1 are substituted with another amino acid, or a polynucleotide encoding the LysE variant.
Claim 11 is drawn to the LysE variant of claim 1, having 99% or more sequence identity to SEQ ID NO:1.
Claim 12 is drawn to the microorganism of claim 8, wherein the LysE variant has 95% or more sequence identity to SEQ ID NO:1.
Claim 13 is drawn to the microorganism of claim 8, wherein the LysE variant has 99% or more sequence identity to SEQ ID NO:1.
Claim 14 is drawn to the method of claim 10, wherein the microorganism is Corynebacterium glutamicum.
Claim 15 is drawn to the method of claim 10, wherein the LysE variant has 95% or more sequence identity to SEQ ID NO:1.
Claim 16 is drawn to the method of claim 10, wherein the LysE variant has 99% or more sequence identity to SEQ ID NO:1.
The current specification defines the term “variant” as a polypeptide which has an amino acid sequence different from that of the variant before modification by conservative substitution and/or modification of one or more amino acids but maintains the functions or properties (Specification p.6, 1st full paragraph). The current specification further identifies a LysE variant as a polypeptide including an amino acid disclosure in which any one or more amino acids of amino acids corresponding to positions 50, 153 and 215 of SEQ ID NO:1 are substituted with another amino acid (p.6 last sentence – p.7 top sentence). The specification describes that variant may have substitution of one or more amino acids in the amino acid residues of positions 50, 153 or 215 in the amino acid sequences of SEQ ID NO:1 and may have at least 60% identity to SEQ ID NO:1 (Specification p.9 first paragraph). The specification identifies that a variant having an amino acid sequence having deletion, modification, substitution, conservative substitution, or addition of some sequence also falls within the scope of the present invention so long as the amino acid sequence has homology or identity and exhibits efficacy corresponding to that of the variant of the present disclosure (Specification p.9, 3rd paragraph). The specification provides examples of several variants containing a single amino acid substitution at one of three positions in Table 1; LysE F50L; LysE F50I; LysE F50V; LysE N153S; LysE N153T; LysE N153Q; LysE N215T; LysE N215S and LysE N215Q.
The specification does not provide any guidance on the structure-function relationship of SEQ ID NO:1, does not provide any information on which amino acids can be varied or deleted while preserving the exporter function of the protein, nor provide any guidance on which amino acid residues of SEQ ID NO:1 are critical to determine the minimum amino acid sequence identity to SEQ ID NO:1 that is required in other proteins that would meet the required limitation. The specification does not provide any structural guidance on required features or parameters for a LysE variant, including: a required minimum sequence length required of a variant; a minimum sequence homology or identity; whether the LysE variant is required to be functional or retain any functional features; whether any portions of the sequence must be modified or must be preserved. Based on the lack of art-recognized structure-function relationship of SEQ ID NO:1 to other functional variants, it is highly unpredictable what percent identity to SEQ ID NO:1 is required to determine what other proteins would provide a functional LysE variant.
The disclosure of examples containing a single amino acid substitution at one of positions 50, 153 or 215 relative to instant SEQ ID NO:1 is not considered to constitute a representative number of species of the genus of LysE variants containing any one or more amino acids of amino acids selected from positions 50, 153 and 215 of SEQ ID NO:1. Thus, one of ordinary skill in the art could not conclude that Applicant was in possession of any species of the claimed genus of LysE variants containing a substitution of any one or more amino acids of amino acids corresponding to positions 50, 153 and 215 of SEQ ID NO:1. This disclosure does not constitute a representative number of species of the genus in view of the potential breadth and variability of the genus, and so there is a failure to satisfy the written description requirement for the genus.
Response to Arguments
Applicant argues applicant has amended the independent claims, from which the remaining rejected claims depend, rending this rejection moot (See Remarks dated 7/14/2026, p.5 – written description requirement).
Applicant's arguments filed July 14, 2026 have been fully considered but they are not persuasive. As discussed in the rejection above, the current specification does not provide any guidance on the structure-function relationship of SEQ ID NO:1, does not provide any information on which amino acids can be varied or deleted while preserving the exporter function of the protein, nor provide any guidance on which amino acid residues of SEQ ID NO:1 are critical to determine the minimum amino acid sequence identity to SEQ ID NO:1 that is required in other proteins that would meet the required limitation. The specification does not provide any structural guidance on required features or parameters for a LysE variant, including: a required minimum sequence length required of a variant; a minimum sequence homology or identity; whether the LysE variant is required to be functional or retain any functional features; whether any portions of the sequence must be modified or must be preserved. Based on the lack of art-recognized structure-function relationship of SEQ ID NO:1 to other functional variants, it is highly unpredictable what percent identity to SEQ ID NO:1 is required to determine what other proteins would provide a functional LysE variant.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-2, 6, and new claims 11-13 and 15-16 are rejected under 35 U.S.C. 103 as being unpatentable over GenBank reference corresponding to accession number BAV23079 (submitted on June 17, 2017) in view of Vrljic et al. (“The LysE Superfamily: Topology of the Lysine Exporter LysE of Corynebacterium glutamicum, a Paradyme for a Novel Superfamily of Transmembrane Solute Translocators”, J. Mol. Microbiol. Biotechnol. 1999, Vol. 1, No. 2, pp. 327-336; previously cited) as evidenced by French et al. (“What is conservative substitution?”, Journal of Molecular Evolution, 1983, vol. 19, pp. 171-175) and Bachem (Amino Acids Chart, Amino acids chart - Bachem, July 26, 2021; previously cited).
Regarding claims 1-2, 6, 11-13 and 15-16, GenBank teaches a lysine exporter protein from Corynebacterium glutamicum (subject) having 100% sequence identity to instant SEQ ID NO:1 (query), as shown in the alignment below.
PNG
media_image2.png
341
789
media_image2.png
Greyscale
GenBank does not teach the amino acid corresponding to position 50 is substituted with isoleucine.
However, Vrljic teaches lysine exporter LysE of Corynebacterium glutamicum (title). Vrljic teaches LysE is a member of a family of proteins which exhibit similar sizes, hydropathy profiles and sequence motifs comprise the LysE superfamily (abstract). Vrljic teaches that in in aligning the sequences of proteins that comprise the LysE family, the consensus amino acid in position 50 is I (isoleucine) (p.328, Figure 1 replicated below).
PNG
media_image3.png
188
817
media_image3.png
Greyscale
As evidenced by French, protein sequence changes that conserve certain physical and chemical properties of residues are considered “conservative substitution” (p. 171, introduction, top of column 2). French further identifies that many evolutionary changes in proteins are conservative (abstract). French states that evolution of proteins in general has tended to conserve the degree of hydrophobicity of a residue, the conformational preferences of its backbone and its bulk (p.175, 1st column, Conclusion 1st paragraph).
As evidenced by Bachem, nonpolar amino acids include phenylalanine (F), alanine, valine, proline, methionine, tryptophan, leucine, isoleucine and proline.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to replace phenylalanine in position 50 taught by GenBank with isoleucine as taught by Vrljic, because Vrljic teaches that the consensus amino acid in position 50 is I (isoleucine), and that the family of LysE proteins exhibit similar sizes, hydropathy profiles and sequence motifs. Each of GenBank and Vrljic teach LysE proteins. One of ordinary skill in the art would reasonably expect that replacing phenylalanine in the sequence of GenBank with isoleucine taught by Vrljic would predictably result in a LysE variant having the desired substitution and a sequence identity of 99% with SEQ ID NO:1, because it was known in the art at the time of invention that LysE had isoleucine as the consensus residue in position 50 of the LysE protein sequence.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over GenBank reference corresponding to accession number BAV23079 (submitted on June 17, 2017) in view of Vrljic et al. (“The LysE Superfamily: Topology of the Lysine Exporter LysE of Corynebacterium glutamicum, a Paradyme for a Novel Superfamily of Transmembrane Solute Translocators”, J. Mol. Microbiol. Biotechnol. 1999, Vol. 1, No. 2, pp. 327-336; previously cited) as applied to claim 1 above, and further in view of French et al. (“What is conservative substitution?”, Journal of Molecular Evolution, 1983, vol. 19, pp. 171-175; previously cited) as evidenced by Bachem (Amino Acids Chart, Amino acids chart - Bachem , July 26, 2021; previously cited).
The teachings of GenBank and Vrljic et al. are discussed above.
Regarding claim 3, GenBank and Vrljic do not teach wherein the amino acid corresponding to position 50 is substituted with a leucine or a valine.
However, French teaches that protein sequence changes that conserve certain physical and chemical properties of residues are conserved are considered “conservative substitution” (p. 171, introduction, top of column 2). French further teaches that many evolutionary changes in proteins are conservative (abstract). French teaches that evolution of proteins in general has tended to conserve the degree of hydrophobicity of a residue, the conformational preferences of its backbone and its bulk (p.175, 1st column, Conclusion 1st paragraph). As evidenced by Bachem, nonpolar amino acids include phenylalanine (F), alanine, valine, proline, methionine, tryptophan, leucine, isoleucine and proline.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to replace phenylalanine taught by GenBank or isoleucine taught by Vrljic in position 50 with another nonpolar amino acid of leucine or valine taught by French in the amino acid sequence of LysE taught by GenBank, because French teaches that conservative substitution tends to conserve the degree of hydrophobicity of a residue, the conformational preferences of its backbone and its bulk. One of ordinary skill in the art would reasonably expect that substituting one non-polar amino acid for another non-polar amino acid would predictably result in a mutant LysE variant having the desired conservative substitution.
Claim 7 is rejected under 35 U.S.C. 103 as being unpatentable over GenBank reference corresponding to accession number BAV23079 (submitted on June 17, 2017) in view of Vrljic et al. (“The LysE Superfamily: Topology of the Lysine Exporter LysE of Corynebacterium glutamicum, a Paradyme for a Novel Superfamily of Transmembrane Solute Translocators”, J. Mol. Microbiol. Biotechnol. 1999, Vol. 1, No. 2, pp. 327-336; previously cited).
GenBank teaches a lysine exporter protein from Corynebacterium glutamicum (subject) having 100% sequence identity to instant SEQ ID NO:1 (query), as shown in the alignment presented in Claim 1 above.
GenBank does not teach a polynucleotide encoding the LysE variant.
However, Vrljic teaches lysine exporter LysE of Corynebacterium glutamicum (title). Vrljic teaches LysE is a member of a family of proteins which exhibit similar sizes, hydropathy profiles and sequence motifs comprise the LysE superfamily (abstract). Vrljic teaches that in aligning the sequences of proteins that comprise the LysE family, the consensus amino acid in position 50 is I (isoleucine) (p.328, Figure 1).
Vrljic further teaches fragments to be inserted into pPA4 were generated via PCR using pSPORTlysE as a template (p.335, 2nd column – Fusion Constructs). Vrljic teaches that after construction of the plasmids in E. coli DH5αmcr, plasmids were introduced into E. coli CC118 which lacks endogenous alkaline phosphatase activity (p.335, 2nd column – Fusion constructs). Vrljic teaches determining enzyme activity and immunodetection of fusion proteins from recombinant CC118 strains using SDS/PAGE (p.335, 2nd column – Enzyme activity determinations and immunodetection of fusion proteins).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to translate the amino acid sequence taught by GenBank and Vrljic into a coding sequence (i.e. polynucleotide) as Vrljic suggests making fusion constructs using plasmids (i.e. polynucleotide). One of ordinary skill in the art would reasonably expect that translating a desired amino acid sequence into a polynucleotide sequence would predictably result in a polynucleotide encoding the desired protein sequence, because it was well-known in the art at the time of invention that amino acid sequences could be translated into a coding sequence to create plasmids that could be inserted into microorganisms.
Claims 8-10 and new claim 14 are rejected under 35 U.S.C. 103 as being unpatentable over GenBank reference corresponding to accession number BAV23079 (submitted on June 17, 2017) in view of Vrljic et al. (“The LysE Superfamily: Topology of the Lysine Exporter LysE of Corynebacterium glutamicum, a Paradyme for a Novel Superfamily of Transmembrane Solute Translocators”, J. Mol. Microbiol. Biotechnol. 1999, Vol. 1, No. 2, pp. 327-336; previously cited) and Kim et al. (AU 2018353929 A1, published on July 4, 2019; previously cited).
The teachings of GenBank and Vrljic et al. are discussed above.
Regarding claims 8-10 and 14, GenBank teaches a lysine exporter protein from Corynebacterium glutamicum (subject) having 100% sequence identity to instant SEQ ID NO:1 (query), as shown in the alignment presented in Claim 1 above.
GenBank does not teach a microorganism of the genus Corynebacterium comprising a LysE variant.
Vrljic teaches lysine exporter LysE of Corynebacterium glutamicum (title). Vrljic teaches LysE is a member of a family of proteins which exhibit similar sizes, hydropathy profiles and sequence motifs comprise the LysE superfamily (abstract). Vrljic teaches that in aligning the sequences of proteins that comprise the LysE family, the consensus amino acid in position 50 is I (isoleucine) (p.328, Figure 1). Vrljic further teaches making fragments to be inserted into pPA4 were generated via PCR using pSPORTlysE as a template (p.335, 2nd column – Fusion Constructs). Vrljic teaches determining enzyme activity and immunodetection of fusion proteins from recombinant E. coli CC118 strains using SDS/PAGE (p.335, 2nd column – Enzyme activity determinations and immunodetection of fusion proteins).
Vrljic does not teach a microorganism of the genus Corynebacterium comprising a LysE variant.
Kim teaches a microorganism of genus Corynebacterium producing L-arginine and method for producing L-arginine using the same (title). Kim teaches microorganisms of the genus Corynebacterium, in particular Corynebacterium glutamicum, are gram-positive microorganisms widely used in the production of L-amino acids (p.1, lines 19-20). Kim teaches a plasmid was transformed into a parent strain by an electric pulse method to obtain about 20,000 colonies (p.10, lines 2-7). Kim teaches each of about 20,000 colonies were inoculated onto 300µL of selective medium and cultured in a 96-deep-well plate at 30°C at 1,000 rpm for about 24 hours (p.10, lines 14-16). Kim further teaches selecting the top ten mutant strains having increased L-arginine productivity compared to the Corynebacterium glutamicum KCCM10741P strain, and analyzing the concentration of L-arginine in the culture by HPLC (p.11, lines 3-5 and 10-11).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine a LysE protein having the amino acid sequence taught by GenBank including amino acid isoleucine in position 50 taught by Vrljic with the Corynebacterium glutamicum mutant microorganism taught by Kim, because Vrljic teaches that the consensus amino acid for position 50 is isoleucine, and . One of ordinary skill in the art would reasonably expect that substituting one known Corynebacterium glutamicum LysE mutant for another would predictably result in a Corynebacterium glutamicum LysE mutant that would produce L-arginine, because Kim teaches Corynebacterium glutamicum mutants were able to secrete L-arginine.
Response to Arguments
Regarding claims 1-2 and 6, Applicant argues that Vrljic does not disclose a LysE variant having 90% or more sequence identity to the amino acid sequence of SEQ ID NO:1 and including at least one substitution for an amino acid corresponding to position 50, 153 or 215 of SEQ ID NO:1 (See Remarks dated 7/14/2026, p.6, paragraph 3).
Regarding claim 7, Applicant argues that Vrljic fails to teach or suggest the LysE variant of claim 1 and because claim 7 is directed to a polynucleotide encoding that variant, Vrljic likewise fails to teach or suggest the polynucleotide of claim 7 (See Remarks dated 7/14/2026, p.6 “The pending claims are not obvious” item (i)).
Regarding claims 8-10, Applicant argues that as discussed above, Vrljic fails to teach or suggest the LysE variant of claim 1, and Kim fails to cure this deficiency (See Remarks dated 7/14/2026, p.7 1st paragraph). Applicant argues that the presently claimed microorganism exhibits unexpectedly superior L-arginine production, of at least a 19% increase compared to the parent strain, and reproduces Table 4 of the specification (See Remarks dated 7/14/2026, p.7 paragraphs 1-3 and table).
Regarding claims 3-4, Applicant argues Vrljic fails to teach or suggest a LysE variant in which the amino acid corresponding to position 50 is substituted with leucine or valine as set forth in the present claims, and the remaining references fail to cure this deficiency (See Remarks dated 7/14/2026, p.7 item (iii)).
Applicant's arguments filed July 14, 2026 have been fully considered but they are not persuasive. As discussed in the rejection above, GenBank teaches a lysine exporter protein from Corynebacterium glutamicum having 100% sequence identity to instant SEQ ID NO:1. Vrljic teaches that a consensus amino acid for position 50 is isoleucine. French teaches conservative substitutions, and that evolution of proteins in general has tended to conserve the degree of hydrophobicity of a residue, the conformational preferences of its backbone and its bulk. Thus, one of ordinary skill in the art would have found it obvious to modify the sequence taught by GenBank to include a an F50I taught by Vrljic because French teaches conservative substitutions generally conserve the degree of hydrophobicity of a residue, and as evidenced by Bachem, phenylalanine, isoleucine, valine and leucine are all nonpolar amino acids.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. 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 nonprovisional extension fee (37 CFR 1.17(a)) 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DEEPA MISHRA whose telephone number is (571) 272-6464. The examiner can normally be reached Monday - Friday 8:30am - 1:30pm 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, Louise W. Humphrey can be reached at (571) 272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/DEEPA MISHRA/Examiner, Art Unit 1657
Prosecution Insights