DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 3/6/26 has been entered.
Election/Restrictions and Claim Status
Applicants’ amendments and arguments filed 2/9/26 are acknowledged. Any objection or rejection from the 12/8/25 office action that is not addressed below is withdrawn based on the amendments and/or arguments
Previously, Group 1 and the species of SEQ ID NO: 16 were elected.
Claims 38 and 41-44 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 3/20/24.
Claims to the elected species are rejected as set forth below. Any relevant art that was uncovered during the search for the elected species is cited herein in order to advance prosecution. Claims 34-37 and 45 are drawn to non-elected species since they require additional features not present in the elected species. Since SEQ ID NO:16 was elected, claim 51 has been interpreted as being drawn to non-elected species. Although unclear, claims 50 and 52-53 have been interpreted as reading on the elected species.
Claims 34-37, 45 and 51 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 3/20/24.
Claims 1-25, 27-33, 39-40 and 46-49 have been canceled.
Claims 26, 50 and 52-53 are being examined.
Priority
The priority information is found in the filing receipt of 2/15/24.
Claim Warning
Applicant is advised that should claim 50 be found allowable, claim 53 will be objected to under 37 CFR 1.75 as being a substantial duplicate thereof. When two claims in an application are duplicates or else are so close in content that they both cover the same thing, despite a slight difference in wording, it is proper after allowing one claim to object to the other as being a substantial duplicate of the allowed claim. See MPEP § 608.01(m).
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 50 and 52-53 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 50 and 53 refer to ‘alignment of SEQ ID NOs: 2-14 and SEQ ID NO:21 with SEQ ID NO:1 of Figure 1’. Claim 52 incorporates such limitation. First, Figure 1 does not refer to SEQ ID NO:12. As such, the claims are unclear. Further, MPEP 2173.05(s) states that claims are to be complete in themselves and reference to a figure is permitted in only exceptional circumstances where there is no practical way to define the invention in words. There is nothing exceptional about the instant circumstances. Claims 50 and 52-53 are drawn to polypeptides which can be described in words for example by sequence or sequence identifier. It is not clear if claim 52 encompasses anything other than SEQ ID NO:16.
Claims 50 and 53 refer to ‘variant of a protein….wherein the protein is selected from the group consisting of SEQ ID NO:s 1-14 and SEQ ID NO:21’ and refer to residue position in relation to SEQ ID NO:1. A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claims 50 and 53 recites the broad recitation SEQ ID NO:s 1-14 and SEQ ID NO:21, and the claim also recites SEQ ID NO:1 which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
SEQ ID NOs: 1-14 and 21 are of various lengths including 60, 61, 62, 64, 65 and 66 residues. Acceptable locations of modifications are unclear because even though the claim refers to ‘determined by sequence alignment’ such language does not specify how the specific numeric value (for example residue 40) is determined for proteins of different length. Figure 1 shows gaps (i.e. ‘-‘) in certain sequences including SEQ ID NO:1. It is unclear if the dash is to be considered in the counting. The mixing and matching of sequences and residues makes the scope of the claim unclear. Dependent claim 52 does not clarify the claim scope.
Claims 50 and 53 recite ‘at least one additional mutation at positions’. The use of the plural ‘positions’ suggest that more than one additional mutation is required. However, the claims also recite ‘at least one’ which encompasses one. It is unclear which language is controlling allowing for more than one interpretation of the claims. Further, it is unclear if the mutations can be to anything or if the mutations are to naturally occurring amino acids. Claim 50 previously referred to ‘mutations correspond to..’. It is unclear if the amendment to claim 50 broadens the possible mutations.
Although unclear, claims 50 and 53 have been interpreted as encompassing at least SEQ ID NOs: 16-20. Claim 52 has been interpreted as encompassing at least SEQ ID NO:16. Although unclear, claims 50 and 52-53 have been interpreted as being 101 compliant and 112(a)/1st compliant.
Response to Arguments - 112
Applicant's arguments filed 2/9/26 have been fully considered but they are not persuasive with respect to the rejection above.
Although applicants argue that the claims have been amended, the amended claims are addressed above.
Although applicants argue about reference to figure 1 for precision, as discussed above the reference to figure 1 causes confusion. Claims 50 and 52-53 are drawn to polypeptides which can be described in words for example by sequence or sequence identifier.
Although applicants refer to other patents that refer to figures, MPEP 2173.05(s) states that claims are to be complete in themselves and reference to a figure is permitted in only exceptional circumstances where there is no practical way to define the invention in words. There is nothing exceptional about the instant circumstances. Applicant has not provided any references on an IDS nor set forth the relevance of any of the cited patents to polypeptide sequences.
Although applicants argue about a reliance on drawings for a precise structural or positional relationship, Claims 50 and 52-53 are drawn to polypeptides which can be described in words for example by sequence or sequence identifier. A drawing is not required to describe a polypeptide.
Although applicants argue about specification teachings related to introducing mutated amino acids into a scaffold, the instant claims are not drawn to methods of mutating amino acids into a scaffold. The word scaffold is not recited in the instant claims. Limitations from the specification are not read into the claims.
Although applicants argue that the alignment in figure 1 is to identify corresponding positions across different scaffolds, Claims 50 and 53 refer to ‘alignment of SEQ ID NOs: 2-14 and SEQ ID NO:21 with SEQ ID NO:1 of Figure 1’. Claim 52 incorporates such limitation. Figure 1 does not refer to SEQ ID NO:12. Thus, the claims are unclear.
Although applicants argue that figure 1 conveys placements, insertions, deletions and correspondence, it is unclear how such information is conveyed. The figure 1 caption merely states ‘alignment of proteins of the Sac7d family’.
Although applicants argue about alignment in reference to SEQ ID NO:1, claims 50 and 53 recites ‘variant of a protein….wherein the protein is selected from the group consisting of SEQ ID NO:s 1-14 and SEQ ID NO:21’. Thus, the variants do not appear to be limited to SEQ ID NO:1.
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.
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.
Claim(s) 26, 50 and 53 is/are rejected under 35 U.S.C. 103 as being unpatentable over Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’).
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach that the invention provides means for obtaining stable molecules (abstract).
Pecorari does not provide an example that reads on claims 26, 50 and 53.
Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42. Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Pecorari based on the specific teachings and suggestions of Pecorari. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42. Claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Thus one would have been motivated to modify the residues suggested by Pecorari. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26, 50 and 53, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b. Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claim(s) 26, 50 and 52-53 is/are rejected under 35 U.S.C. 103 as being unpatentable over Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Pecorari does not recite the elected species in a specific example.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Pecorari based on the specific teachings and suggestions of Pecorari. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26, 50 and 53, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Response to Arguments - 103
Applicant's arguments filed 2/9/26 have been fully considered but they are not persuasive with respect to the rejections set forth above.
Although applicants argue about a lack of teaching of the residue patterns at 31/33/40/42, claim 7 of Pecorari expressly teach randomization of residues of Sac7d at positions including S31, T33, T40 and R42. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b. The previous office action and current office action expressly refer to MPEP 2144.05 which recites: “When there is a design need or market pressure to solve a problem and there are a finite number of identified, predictable solutions, a person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense.” Instant claims 50b and 53b are in no way limited to only modifications at positions 31/33/40/42.
Although applicants argue about a lack of teaching of selecting mutants with certain properties, instant claims 26, 50 and 52-53 are product claims. As product claims they do not require methods of selection.
Although applicants argue about obvious to try, MPEP 2145 XB refers to 2 main kind of errors with obvious to try – “vary all parameters or try each of numerous possible choices until one possibly arrived at a successful result, where the prior art gave either no indication of which parameters were critical or no direction as to which of many possible choices is likely to be successful.... In others, what was ‘obvious to try’ was to explore a new technology or general approach that seemed to be a promising field of experimentation, where the prior art gave only general guidance as to the particular form of the claimed invention or how to achieve it”. However, that is not the case here. In the instant case, the prior art teach a specific protein (Sac7d) and teach very specific residues for modification (see claim 13 of Pecorari). This is not asking to vary all parameters, this is referring to specific residues of a specific protein. The teachings of Pecorari do provide direction as claim 13 recites “which corresponds to the randomization of the residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 of Sac7d”. There is no reasonable basis to conclude that Pecorari provides no indication of which parameters were critical.
Although applicants argue about a lack of teaching of achieving functional selectivity at the trimerization interface, instant claims 26, 50 and 52-53 are product claims. As product claims they do not require methods of achieving selectivity.
Although applicants argue that a 15-20 position library presents vast combinatorial space not a finite, identified set for achieving selectivity, Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). A 20 position library with any 20 amino acids at each position includes a finite number of sequences (i.e. 2020). With respect to achieving selectivity, MPEP 2144 IV recognizes that a rationale different from applicant’s is permissible and that it is not necessary that the prior art suggest the same advantage or result discovered by the applicant. Pecorari expressly teach libraries for a purpose of binding to a target (claims 1-7).
Although applicants argue that the claimed functional limitation is not met, MPEP 2112.01 recognizes that a chemical composition and its properties are inseparable. The elected species is SEQ ID NO:16. The rejection above addresses how the claim limitations are met. Since the prior art suggest SEQ ID NO:16 (and other species within the scope of claims 26 and 50) such proteins would function as claimed. US 10,548,945 is cited as part of a double patenting rejection below. Prior to issuance, the Board affirmed a 103 rejection based on a Pecorari reference over claims drawn to a genus of proteins (see claim set of 1/29/18 and board decision of 7/17/19 in application 14/786,287). A copy of the Examiner’s Answer (Examiner’s Answer in application 14786287, 11/19/18, 32 total pages) and Board Decision (Board decision in application 14786287, 7/17/19, 12 total pages with last page numbered page 11) are provided herein. The Examiner’s Answer includes a 103 rejection where one of the references is Pecorari et al. (pages 12-16) where Pecorari et al. is the US equivalent of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’ which is used in rejections above). As stated on page 9 of the board decision of 7/17/19: “Appellant’s contention is also not persuasive because Pecorari suggests compositions within the scope of Appellant’s claim 1, such as a Sac7d OB-fold protein that has been modified at 5 residues selected from the group consisting of V2, K3, K5, K7, Y8, K9, G10, E14, T17, K21, K22, W24, V26, G27, K28, M29, S31, T33, D36, N37, G38, K39, T40, R42, A44, S46, E47, K48, D49, A50, and P51 of Sac7d (see FF 7-11). “From the standpoint of patent law, a compound and all of its properties are inseparable; they are one and the same thing.” In re Papesch, 315 F.2d 381, 391 (CCPA 1963). Thus, absent evidence to the contrary, Pecorari’s composition will exhibit the same properties as Appellant’s claimed composition.”. The instant facts considerably align with such case, specifically a 103 rejection of a genus claim encompassing Sac7d variants based on a Pecorari reference. The properties recited in the claims of application 14/786,287 were not sufficient to overcome the 103 rejection and there is no adequate and sufficient reason why one would come to a different conclusion in the instant case.
Although applicants argue that merely generating or manipulating sequences does not equate to what is claimed, instant claims 26, 50 and 52-53 are product claims. Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Thus, one would have had a reasonable expectation of success in generating polypeptides.
Although applicants argue about unexpected properties, such arguments were addressed in a previous office action (see 7/16/25).
Although applicants argue that there is no reasonable expectation of success with respect to selective binding, the instant claims are not drawn to methods of selective binding. The instant claims are drawn to polypeptides. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
Double Patenting
Claims were previously rejected under double patenting based on patents, applications and references cited below. Since the claims have been amended, the rejections are updated to correspond to the instant claims.
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 26, 50 and 52-53 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 10,293,025 (025) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
025 recites Sac7d (claim 2) with 5-32 mutated residues (claim 1).
025 does not recite any species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 025 because 025 specifically recites Sac7d (claim 2) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10 of U.S. Patent No. 10,548,945 (945) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
945 recites methods that require variant proteins that are variants of Sac7d specifically those with particular mutated residues (claim 1).
945 does not recite any species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 945 because 945 specifically recites Sac7d (claim 1) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 10,898,542 (542) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
542 recites methods that require variant proteins that are variants of Sac7d specifically those with particular mutated residues (claim 1).
542 does not recite any species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 542 because 542 specifically recites Sac7d (claim 1) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 11,932,674 (674) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
674 recites Sac7d (claim 6) with 5-20 mutated residues (claims 6-7).
674 does not recite any species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 674 because 674 specifically recites Sac7d (claim 6) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of copending Application No. 18/435,494 (494) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
This is a provisional nonstatutory double patenting rejection.
494 recites Sac7d (claim 1) with specific mutated residues (claim 2).
494 does not recite any species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 494 because 494 specifically recites Sac7d (claim 1) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-25 of copending Application No. 17/906,000 (000) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
This is a provisional nonstatutory double patenting rejection.
000 recites Sac7d (claim 1) with specific mutated residues (claim 1).
000 does not recite the elected species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 000 because 000 specifically recites Sac7d (claim 1) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 18/715,929 (929) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
This is a provisional nonstatutory double patenting rejection.
929 recites Sac7d with mutated residues (claim 1).
929 does not recite the elected species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 929 because 929 specifically recites Sac7d (claim 1) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-19 of copending Application No. 18/282,613 (613) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
This is a provisional nonstatutory double patenting rejection.
613 recites Sac7d with mutated residues (claim 1).
613 does not recite the elected species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 613 because 613 specifically recites Sac7d (claim 1) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Claims 26, 50 and 52-53 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 18/277,126 (126) in view of Pecorari et al. (EP 1930342 as cited with IDS 4/7/21; ‘Pecorari’) in view of Kitten O (WO 2016/062874) in view of Borns M (US 2007/0141591; ‘Borns’).
Kitten O (WO 2016/062874) is not in the English language. The English language equivalent is US 20180085427 (‘Kitten’) which will be referred to herein.
This is a provisional nonstatutory double patenting rejection.
126 recites Sac7d with mutated residues (claim 1).
126 does not recite the elected species in the claims.
Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach methods of obtaining molecules through a combinatorial mutation/selection approach (abstract). Pecorari teach that various libraries were designed and made (examples 1-5) where the substitutions allow representation of all amino acids (section 0058). Pecorari teach 5 to 32 residues that are modified (section 0010). Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15) and the variants offer numerous advantageous properties (section 0084). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9). In figure 8, Pecorari shows regions for modification. Pecorari teach that the invention provides means for obtaining stable molecules (abstract). In claim 9, Pecorari specifically recites at least residues K7, Y8, K9, W24, V26, M29, S31, T33, R42, A44 and S46 and claim 13 recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46. Claim 11 depends on claim 9 and recites two or three additional residues of Sac7d selected amongst K21, K22 and T40.
Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010).
Borns teach Sac7d and teach that a residue for modification is G41 (section 0041).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 126 because 126 specifically recites Sac7d (claim 1) and the other references provide known additional details about such protein. Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010). In claim 8, Pecorari recites specific residues for modification including S31, T33, T40 and R42. Thus one would have been motivated to modify the residues suggested by Pecorari. Further, since Kitten and Borns teach known modifications of Sac7d, one would have been motivated to incorporate known modifications. One would have had a reasonable expectation of success since Pecorari teach that Sac7d is tolerant to substitution and variants retained satisfactory properties (page 13 lines 13-15). Pecorari teach that methods of making the libraries and individual proteins were known (pages 8-9).
In relation to claims 26 and 50, Pecorari teach combinatorial libraries which correspond to randomization of certain residues of Sac7d (claim 7 for example). Pecorari teach 5 to 32 residues that are modified (section 0010) (compare MPEP 2144.05). Pecorari recites specific residues for modification including K7, S31, T33, T40 and R42 (claim 8) (compare instant SEQ ID NO: 17 which in relation to SEQ ID NO:1 requires modifications at positions 31, 33, 40 and 42 and allows any residue at positions 7-9, 11, 21-22, 24, 26, 29, 35, 41, 44 and 46). Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since Pecorari suggest sequences as claimed they have been interpreted as meeting the functional limitation. Further, claim 13 of Pecorari recites residues K7, Y8, K9, K21, K22, W24, V26, M29, S31, T33, T40, R42, A44 and S46 which are residues as recited in claims 50a-b and 53a-b.
In relation to claims 26, 50 and 52-53 and the elected species, Pecorari teach 5 to 32 residues that are modified (section 0010) thus one would have been motivated to choose any combination of such residues (compare MPEP 2144.05). Further, Pecorari expressly teach specific residues for modification including K7 and Y8 and K9 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and T40 and R42 and A44 and S46 (claim 7). Further, Pecorari recognizes modifications in the region of residues 35-40 (section 0014) which includes residue 35. Kitten teach Sac7d and recite that E11 is in the binding domain (section 0010). Borns teach Sac7d and teach that a residue for modification is G41 (section 0041). Thus, the prior art suggest modifications at K7 and Y8 and K9 and E11 and K21 and K22 and W24 and V26 and M29 and S31 and T33 and D35 and T40 and G41 and R42 and A44 and S46. Pecorari teach that the substitutions allow representation of all amino acids (section 0058). Since there are 20 possible encoded amino acids there are a finite number of amino acids at each position for substitution. Since the prior art suggest sequences as claimed they have been interpreted as meeting the functional limitation.
Response to Arguments – double patenting
Applicant's arguments filed 2/9/26 have been fully considered but they are not persuasive with respect to the rejections set forth above.
Although applicants argue about the reasons set forth in the reply to the obviousness rejection, such arguments are addressed above.
Conclusion
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RONALD T. NIEBAUER
Primary Examiner
Art Unit 1658
/RONALD T NIEBAUER/Examiner, Art Unit 1658
Prosecution Insights