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 .
Status of Claims
Receipt of Arguments/Remarks filed on 2/13/2026 is acknowledged. Claims 1-3, 6-11, 13-16, and 18-22 are pending. Claims 1-3, 6-8, 10, 11, and 20 were amended. New claims 21 and 22 were added. Claims 4, 5, and 12 were canceled. Claims 13-16 and 18-19 are withdrawn.
Withdrawn Rejections
The rejection of claims 4, 8, and 11 under 35 U.S.C. § 112(a) is withdrawn.
The rejection of claims 1-3, 5-7, 9, 10, 12, and 20 under 35 U.S.C. § 101 is withdrawn.
New and modified rejections necessitated by amendment
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-3 and 6-8 are rejected under 35 U.S.C. 103 as being unpatentable over Hogenhaug et al., US 8,080,390 B2 in view of Pietzsch et al., WO 2009030211 A2 and Deweid et al., Biological Chemistry; 400(3):257-74.
Regarding claim 1, Hogenhaug’s disclosure is directed to antimicrobial polypeptides and compositions (Hogenhaug col. 1 “SUMMARY OF THE INVENTION”). Hogenhaug teaches a composition comprising a transglutaminase (Hogenhaug col. 19 lines 5-21). Hogenhaug teaches that the composition further comprises another biocidal agent, including non-polypeptide chemical agents (Hogenhaug col. 19 lines 22-40). Thus, Hogenhaug teaches a composition comprising (a) a transglutaminase in combination with (c) at least one chemical preservative and/or antimicrobial chemical. Given the recitation of option (b) and/or (c), it is considered that only one of (b) or (c) is required. Therefore, as Hogenhaug teaches a composition comprising (a) and (c), this meets the claim. Regarding the limitation “wherein the transglutaminase zymogen interacts with the TAMEP and the TAP to produce an active transglutaminase having at least one activity chosen from preservative activity and antimicrobial activity”, this limitation is directed to option (b), and as Hogenhaug teaches option (c) it is not required.
Regarding claims 6-8, Hogenhaug teaches that the composition comprises polymyxins (Hogenhaug col. 19 lines 22-33).
Hogenhaug does not teach that the transglutaminase is in the form of a zymogen or that the transglutaminase zymogen comprises an amino acid sequence that is not a wild-type amino acid sequence (claim 1), that the active transglutaminase has a sequence according to SEQ ID NO: 2 (claim 2), or that the zymogen has a sequence according to SEQ ID NO: 3 (claim 3).
Regarding claim 1, Pietzsch teaches microbial transglutaminases derived from Streptomyces mobaraensis (Pietzch para. 2). Pietzsch teaches modified transglutaminases with higher thermostability compared to wild-type (Pietzsch para. 8). Pietzsch teaches that thermostable transglutaminases are made by amino acid substitutions to the pro-transglutaminase (i.e. zymogen) sequence (Pietszch claim 1). Thus, these mutated transglutaminase zymogens have sequences that are not the same as the wildtype sequence.
Regarding claim 2, SEQ ID NO: 4 of Pietzsch is 100% identical to instant SEQ ID NO: 2, comprising a mutation of S2P and exhibiting increased activity and thermostability compared to wildtype (Pietzch para. 77, para. 100; Fig. 2; see sequence alignment in OA appendix).
Regarding claim 3, Pietzch teaches modifying the pro-transglutaminase (i.e. zymogen) sequence to create thermostable mutants, including a mutation of S2P (Pietszch claim 1, 6). Pietzch teaches activation of the pro-transglutaminase using TAMEP (Pietszch para. 40). Instant SEQ ID NO: 2 (active form) differs from instant SEQ ID NO: 3 (zymogen) in that the active form has undergone cleavage to become activated. Residues 1-331 of instant SEQ ID NO: 2 are 100% identical to residues 47-377 of instant SEQ ID NO: 3. Pietzsch teaches a pro-transglutaminase wildtype sequence, SEQ ID NO: 1, which is 99.7% identical to instant SEQ ID NO: 3, with the only difference being the mutation of S2P (see sequence alignment in OA appendix). Thus, it is considered that the zymogen form of the mutated transglutaminase of Pietzsch SEQ ID NO: 4 would have a sequence according to instant SEQ ID NO: 3, since SEQ ID NO: 4 of Pietzsch is 100% identical to the cleaved active form, instant SEQ ID NO: 2.
Regarding claim 1, Deweid teaches that microbial transglutaminase (mTG) from S. mobaraensis is secreted as an inactive zymogen that must be activated extracellularly by TGase-activating protease (TAMEP) and a tripeptidyl aminopeptidase (SM-TAP) to produce the mature enzyme (Deweid p. 2 “Protein structure and substrate Preference”). Deweid teaches that mTG has many applications in pharmaceutic and biotechnological research, but engineering of mTG is hindered by the intracellular toxicity of the mature enzyme in bacterial hosts, resulting in poor product yields and making proteolytic activation of the inactive zymogen necessary (Deweid p. 11 “Engineering of microbial transglutaminase”).
It would have been obvious for a skilled artisan to modify the teachings of Hogenhaug and utilize a zymogen form of the transglutaminase in a composition with an antimicrobial chemical. It is known in the art that transglutaminase is expressed as a proenzyme or zymogen that is then activated enzymatically, as taught by Pietzsch and Deweid. A skilled artisan would have found it obvious to create a composition with the zymogen form of transglutaminase, such as the transglutaminase according to SEQ ID NO: 3, as the enzyme must be produced by the bacterial host in a zymogen form. It would have further been obvious to use a transglutaminase with a modified sequence resulting in higher thermostability and activity (SEQ ID NOs: 2 and 3) in place of a wildtype transglutaminase to confer these beneficial properties to the composition.
A person of ordinary skill in the art would have been motivated to use a zymogen form of transglutaminase according to SEQ ID NO: 3, which is then processed into an active form with a sequence according to SEQ ID NO: 2, as taught by Pietzsch. The transglutaminase zymogen or active form according to SEQ ID NOs: 2 and 3 has a mutation that results in increased thermostability and activity, and would therefore be beneficial to include in a composition with an antimicrobial chemical as taught by Hogenhaug. Further, a skilled artisan would have been motivated to use transglutaminase in a zymogen form because the active form cannot be produced by bacteria due to intracellular toxicity, so in order to create a composition using transglutaminase the zymogen would need to be produced and later activated. Additionally, use of a zymogen form in the composition of Hogenhaug allows for regulation of when the enzyme is activated which would be desirable for greater control of the activity of the composition.
A skilled artisan would have had a reasonable expectation of success in using a zymogen form of the enzyme having a sequence according to SEQ ID NO: 3 which is converted to an active form having a sequence according to SEQ ID NO: 2 because the transglutaminase from S. mobaraensis is known to have many pharmaceutical and food industry uses as taught by Pietzsch and Deweid, and therefore it is expected that such a zymogen could be successfully incorporated in a composition with an antimicrobial chemical.
Regarding the limitations “a transglutaminase activating metalloprotease (TAMEP) and a tripeptidyl aminopeptidase (TAP)” and “wherein the transglutaminase zymogen interacts with the TAMEP and the TAP to produce an active transglutaminase having at least one activity chosen from preservative activity and antimicrobial activity”, as discussed above these limitations are not required given the and/or language used in claim 1. However, it is noted that it would have been obvious to incorporate TAMEP and TAP in a composition with the zymogen form of transglutaminase because it is known in the art that the active form of mTG is toxic to host cells and therefore mTG is produced by host cells in zymogen form and must be activated by TAMEP and TAP, as taught by Deweid. Thus, a skilled artisan would have been aware that if a zymogen form of the mTG is used in a composition, it would need to be activated by TAMEP and TAP, making it obvious to include these enzymes in a composition with the zymogen form of transglutaminase.
Claims 1-3, 9-11, and 20-22 are rejected under 35 U.S.C. 103 as being unpatentable over Thijssen et al., US 2012/0027694 A1 in view of Pietzsch et al., WO 2009030211 A2 and Deweid et al., Biological Chemistry; 400(3):257-74.
Regarding claim 1, Thijssen teaches a composition comprising a carbohydrate polymer with (a) a transglutaminase, and (c) an active component which may be an antimicrobial compound (Thijssen p. 1 para. 11). As discussed above, given the recitation of option (b) and/or (c), it is considered that only one of (b) or (c) is required.
Regarding claims 9-11, Thijssen teaches that the composition comprises an organic acid as an active component (Thijssen p. 2 para. 61).
Regarding claims 20-22, Thijssen teaches that the composition comprises chitosan (Thijssen p. 1 para. 11).
Thijssen does not teach that the transglutaminase is in the form of a zymogen or that the transglutaminase zymogen comprises an amino acid sequence that is not a wild-type amino acid sequence (claim 1), that the active transglutaminase has a sequence according to SEQ ID NO: 2 (claim 2), or that the zymogen has a sequence according to SEQ ID NO: 3 (claim 3).
Regarding claim 1, Pietzsch teaches microbial transglutaminases derived from Streptomyces mobaraensis (Pietzch para. 2). Pietzsch teaches modified transglutaminases with higher thermostability compared to wild-type (Pietzsch para. 8). Pietzsch teaches that thermostable transglutaminases are made by amino acid substitutions to the pro-transglutaminase (i.e. zymogen) sequence (Pietszch claim 1). Thus, these transglutaminase zymogens have sequences that are not the same as the wildtype sequence.
Regarding claim 2, SEQ ID NO: 4 of Pietzsch is 100% identical to instant SEQ ID NO: 2, comprising a mutation of S2P and exhibiting increased activity and thermostability compared to wildtype (Pietzch para. 77, para. 100; Fig. 2; see sequence alignment in OA appendix).
Regarding claim 3, Pietzch teaches modifying the pro-transglutaminase (i.e. zymogen) sequence to create thermostable mutants, including a mutation of S2P (Pietszch claim 1, 6). Pietzch teaches activation of the pro-transglutaminase using TAMEP (Pietszch para. 40). Instant SEQ ID NO: 2 (active form) differs from instant SEQ ID NO: 3 (zymogen) in that the active form has undergone cleavage to become activated. Residues 1-331 of instant SEQ ID NO: 2 are 100% identical to residues 47-377 of instant SEQ ID NO: 3. Pietzsch teaches a pro-transglutaminase wildtype sequence, SEQ ID NO: 1, which is 99.7% identical to instant SEQ ID NO: 3, with the only difference being the mutation of S2P (see sequence alignment in OA appendix). Thus, it is considered that the zymogen form of the mutated transglutaminase of Pietzsch SEQ ID NO: 4 would have a sequence according to instant SEQ ID NO: 3, since SEQ ID NO: 4 of Pietzsch is 100% identical to the cleaved active form, instant SEQ ID NO: 2.
Regarding claim 1, Deweid teaches that microbial transglutaminase (mTG) from S. mobaraensis is secreted as an inactive zymogen that must be activated extracellularly by TGase-activating protease (TAMEP) and a tripeptidyl aminopeptidase (SM-TAP) to produce the mature enzyme (Deweid p. 2 “Protein structure and substrate Preference”). Deweid teaches that mTG has many applications in pharmaceutic and biotechnological research, but engineering of mTG is hindered by the intracellular toxicity of the mature enzyme in bacterial hosts, resulting in poor product yields and making proteolytic activation of the inactive zymogen is necessary (Deweid p. 11 “Engineering of microbial transglutaminase”).
It would have been obvious for a skilled artisan to modify the teachings of Thijssen and utilize a zymogen form of the transglutaminase in a composition in combination with an organic acid or chitosan. It is known in the art that transglutaminase is expressed as a proenzyme or zymogen that is then activated enzymatically, as taught by Pietzsch and Deweid. A skilled artisan would have found it obvious to create a composition with the zymogen form of transglutaminase, such as the transglutaminase according to SEQ ID NO: 3, as the enzyme is produced by the bacterial host in a zymogen form. It would have further been obvious to use a transglutaminase with a modified sequence resulting in higher thermostability and activity in place of a wildtype transglutaminase to confer these beneficial properties to the composition.
A person of ordinary skill in the art would have been motivated to use a zymogen form of transglutaminase according to SEQ ID NO: 3, which is then processed into an active form with a sequence according to SEQ ID NO: 2, as taught by Pietzsch. The transglutaminase zymogen or active form according to SEQ ID NOs: 2 and 3 has a mutation that results in increased thermostability and activity, and would therefore be beneficial to include in a composition with an organic acid or chitosan as taught by Thijssen. Further, a skilled artisan would have been motivated to use transglutaminase in a zymogen form because the active form cannot be produced by bacteria due to intracellular toxicity, so in order to create a composition using transglutaminase the zymogen would need to be produced and later activated. Additionally, use of a zymogen form in the composition of Thijssen allows for regulation of when the enzyme is activated which would be desirable for greater control of the activity of the composition.
A skilled artisan would have had a reasonable expectation of success in using a zymogen form of the enzyme having a sequence according to SEQ ID NO: 3 which is converted to an active form having a sequence according to SEQ ID NO: 2 because the transglutaminase from S. mobaraensis is known to have many pharmaceutical and food industry uses as taught by Pietzsch and Deweid, and therefore it is expected that such a zymogen could be successfully incorporated in a composition with an organic acid or chitosan.
Double Patenting
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.
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Claims 1-3, 9-11, and 20-22 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of U.S. Patent No. 12256741 B2 in view of Pietzsch et al., WO 2009030211 A2 and Deweid et al., Biological Chemistry; 400(3):257-74.
Regarding instant claim 1, claim 1 of ‘741 recites a method for preserving a product comprising incorporating at least one cross-linking enzyme in an effective amount to provide antimicrobial activity, wherein the cross-linking enzyme is selected from microbial transglutaminase, tyrosinase, and lysyl oxidase. Claim 3 of ‘741 recites the method of claim 1, wherein the method further comprises incorporating at least one other antimicrobial substance in addition to the cross-linking enzyme. Thus, ‘741 recites a composition comprising (a) transglutaminase, in combination with (c) at least one chemical preservative and/or antimicrobial chemical.
Regarding instant claims 9-11 and 20-22, claims 2 and 4 of ‘741 recite that the enzyme composition comprises a polymeric support, which is a biocidal polymer. Claim 5 of ‘741 recites that the biocidal polymer is chitin, chitosan, carboxymethylchitosan, polylysine, cellulose, quaternary ammonium cellulose, alginate, pectin, carboxycellulose, or a combination thereof.
‘741 does not recite that the transglutaminase is in the form of a zymogen or that the transglutaminase zymogen comprises an amino acid sequence that is not a wild-type amino acid sequence (claim 1), that the active transglutaminase has a sequence according to SEQ ID NO: 2 (claim 2), or that the zymogen has a sequence according to SEQ ID NO: 3 (claim 3).
Regarding claim 1, Pietzsch teaches microbial transglutaminases derived from Streptomyces mobaraensis (Pietzch para. 2). Pietzsch teaches modified transglutaminases with higher thermostability compared to wild-type (Pietzsch para. 8). Pietzsch teaches that thermostable transglutaminases are made by amino acid substitutions to the pro-transglutaminase (i.e. zymogen) sequence (Pietszch claim 1). Thus, these transglutaminase zymogens have sequences that are not the same as the wildtype sequence.
Regarding claim 2, SEQ ID NO: 4 of Pietzsch is 100% identical to instant SEQ ID NO: 2, comprising a mutation of S2P and exhibiting increased activity and thermostability compared to wildtype (Pietzch para. 77, para. 100; Fig. 2; see sequence alignment in OA appendix).
Regarding claim 3, Pietzch teaches modifying the pro-transglutaminase (i.e. zymogen) sequence to create thermostable mutants, including a mutation of S2P (Pietszch claim 1, 6). Pietzch teaches activation of the pro-transglutaminase using TAMEP (Pietszch para. 40). Instant SEQ ID NO: 2 (active form) differs from SEQ ID NO: 3 (the inactive form) in that the active form has undergone cleavage, and residues 1-331 of SEQ ID NO: 2 are 100% identical to residues 47-377 of SEQ ID NO: 3 (see sequence alignment in OA appendix). Thus, it is considered that the mutant of Pietzsch SEQ ID NO: 4 in zymogen form (i.e. inactivated) would have a sequence according to instant SEQ ID NO: 3, since SEQ ID NO: 4 of Pietzsch is 100% identical to instant SEQ ID NO: 2.
Regarding claim 1, Deweid teaches that microbial transglutaminase (mTG) from S. mobaraensis is secreted as an inactive zymogen that must be activated extracellularly by TGase-activating protease (TAMEP) and a tripeptidyl aminopeptidase (SM-TAP) to produce the mature enzyme (Deweid p. 2 “Protein structure and substrate Preference”). Deweid teaches that mTG has many applications in pharmaceutic and biotechnological research, but engineering of mTG is hindered by the intracellular toxicity of the mature enzyme in bacterial hosts, resulting in poor product yields and making proteolytic activation of the inactive zymogen is necessary (Deweid p. 11 “Engineering of microbial transglutaminase”).
It would have been obvious for a skilled artisan to combine ‘741 with the teachings of Pietzsch and Deweid, arriving at a method using a composition comprising a zymogen form of the transglutaminase in combination with an antimicrobial chemical. It is known in the art that transglutaminase is expressed as a proenzyme or zymogen that is then activated enzymatically, as taught by Pietzsch and Deweid. A skilled artisan would have found it obvious to create a composition with the zymogen form of transglutaminase, such as the transglutaminase according to SEQ ID NO: 3, as the enzyme is produced by the bacterial host in a zymogen form. A skilled artisan would have been motivated to do so given the higher thermostability and activity of the modified transglutaminase zymogen to confer these beneficial properties to the composition. Further, an ordinary artisan would have been motivated to use a zymogen form of transglutaminase because the mature active form cannot be produced by bacterial hosts.
Claims 1-3 and 6-11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 23, and 28-30 of copending Application No. 17/910,952 in view of Pietzsch et al., WO 2009030211 A2.
Regarding instant claim 1, claim 1 and 3 of ‘952 recites (a) a transglutaminase enzyme variant comprising the sequence according to SEQ ID NO: 1 and further comprising one or more recited mutations. SEQ ID NO:1 of ‘952 is 99.6% identical to instant SEQ ID NO: 2. Claim 23 of ‘952 recites a composition comprising the transglutaminase enzyme variant of claim 1 in combination with (c) one or more antimicrobial enzyme, peptide, or protein, wherein the composition comprises preservative, biocidal, antimicrobial, or virucidal activity. Claim 28 of ‘952 recites a composition comprising the transglutaminase enzyme variant of claim 1 in combination with one or more biocidal chemicals.
Regarding instant claim 5, claims 2 and 4 of ‘952 recites the transglutaminase enzyme variant of claim 1, further comprising a pro-sequence (i.e. zymogen).
Regarding instant claims 6-8, claim 30 of ‘952 recites that the composition comprises an antimicrobial enzyme, peptide, or protein which includes polymyxin, see specification paragraph 14.
Regarding instant claims 9-11, claim 29 of ‘952 recites the biocidal chemical is chosen from a polymer, a quaternary ammonium, a detergent, a chaotropic agent, an organic acid, a phenol, an alcohol, an aldehyde, an aldehyde releaser, a base, an oxidizer, and a paraben.
‘952 does not teach that the active transglutaminase has a sequence according to SEQ ID NO: 2 (claim 2), or that the zymogen has a sequence according to SEQ ID NO: 3 (claim 3).
The teachings of Pietszch regarding claims 2 and 3 are set forth above.
It would have been obvious for a skilled artisan to combine ‘952 with the teachings of Pietzsch, arriving at a method using a composition comprising a zymogen form of the transglutaminase with a sequence according to SEQ ID NO: 3 and an active form with a sequence according to SEQ ID NO: 2. ‘952 recites using a zymogen in a composition. A skilled artisan would have been motivated to use the zymogen form with the sequence according to SEQ ID NO: 3 given the higher thermostability and activity of the modified transglutaminase zymogen to confer these beneficial properties to the composition.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
In light of amendments to the claims, the rejections of claims 1-3, 6-7, 9-10, and 20 under 35 U.S.C. § 102; and the rejection of claims 4, 5, 8, 11, and 12 under 35 U.S.C. § 103 over Hogenhaug in view of Juettner have been withdrawn. However, upon further consideration, new grounds of rejection of claims 1-3, 6-11, and 20-22 are made under 35 U.S.C. § 103 as set forth above. Given these new grounds of rejection, the arguments presented regarding claims rejected under 35 U.S.C. § 102 and under 35 U.S.C. § 103 over Hogenhaug in view of Juettner are moot.
Double Patenting
Applicant argues that the cited claims are completely silent regarding a composition
comprising a transglutaminase zymogen, a TAMEP, and a TAP.
It is noted that the limitation “a transglutaminase activating metalloprotease
(TAMEP) and a tripeptidyl aminopeptidase (TAP)” is not required by claim 1 given the and/or language for options (b) and (c) as discussed above. The double patenting rejections have been updated in light of claim amendments and are maintained as set forth above.
Conclusion
Claims 1-3, 6-11, and 20-22 are rejected. No claims are allowed.
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.
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/EMILY F EIX/Examiner, Art Unit 1653
/JENNIFER M.H. TICHY/Primary Examiner, Art Unit 1653
