DETAILED ACTION
All objections and rejections raised in prior Office Actions are withdrawn unless restated below.
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 .
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 1, 3-9 and 16-22 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.
Claim 1 recites a genus of proteases defined as having “improved wash performance compared to the protease parent without the alterations or compared to the protease with SEQ ID NO: 3.”
"[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production.”
Since claim 1 recites a product and does not recite a method of producing a protease (as in, for example, claim 11) the parent protease is not a single protease but is rather an undefined genus of proteases and includes proteases other than SEQ ID NO: 3, since the claim further recites “or compared to the protease of SEQ ID NO: 3” such that the parent protease is not SEQ ID NO: 3.
“In Brummer, the Board held that a limitation in a claim to a bicycle that recited "said front and rear wheels so spaced as to give a wheelbase that is between 58 percent and 75 percent of the height of the rider that the bicycle was designed for" was indefinite because the relationship of parts was not based on any known standard for sizing a bicycle to a rider, but on a rider of unspecified build.” MPEP 2173.05(b).
In claim 1, the recitation of “the parent protease” is a base reference for measuring improvement of wash performance that is analogous the “rider” referenced in MPEP 2173.05(b), wherein “the parent protease” is of unspecified sequence to which there are some parent proteases to which a potential embodiment of claim 1 have improved wash performance and other parent proteases to which a potential embodiment does not have improved wash performance. A parent protease can be considered to be any protease not having at least 80% identity to SEQ ID NO: 3 and amino acid residue 199K plus an additional alteration as recited in claim 1 (i.e. not a potential embodiment of claim 1 not having all of the structural features of claim 1). For example, all of the following proteases identical to SEQ ID NO: 3 other than stated substitutions, and an unlimited number of additional proteases, are embodiments of “the parent protease” (none of below having substitution N199K):
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It is not sufficient for an embodiment of claim 1 to be a protease having at least 80% identity to SEQ ID NO: 3, a substitution N199K and one additional alteration as recited. Rather, any embodiment of claim 1 must also have improved wash performance relative to “the parent protease.” Since the parent protease is of unspecified identity (i.e. defined only by what it is not), an ordinarily skilled artisan at the time of filing is unable to determine if any potential embodiment of claim 1 “has improved wash performance compared to the protease parent from which the variant was derived” and is therefore unable to determine how to avoid infringement of claim 1. Further, it is noted that no embodiment of claim 1 is required to be made by any act of being “derived” from any parent protease. Embodiments of claim 1 are not limited by the performance of any active steps of a method nor by a method that would, for example, satisfy claim 11. For example, an embodiment of claim 1 can be made by solid phase peptide synthesis or by translation of an encoding nucleic acid wherein the nucleic acid is produced by sold-phase synthesis without any acts of “introducing into a parent protease” (e.g. modifying a codon on a preexisting nucleic acid to another codon).
Claim 1 does not recite any step of a method and protease embodiments of claim 1 are not required to be made nor derived from any particular “the parent protease.” As discussed, there is no single “the parent protease” since the claims recite a composition of matter and are not required to be made by any particular process. See MPEP 2113 ("[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production.”). For these reasons, an ordinarily skilled artisan is unable to determine how to avoid infringement.
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.
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 1, 3-9 and 11-23 (all pending claims) are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 11,518,987 B2 in view of Svendsen (U.S. 2004/0209343 A1).
The present application claims priority to U.S. Patent No. 11,518,987 (Ser. No. 15/535,858) and has the same disclosure.
Copending or patented claims are also referred to as “reference” claims.
Patented claims 3 recite a protease variant having at least 90% identity to SEQ ID NO: 3 having substitutions S27K, S171N, S173P, G174R, S175P, F180Y, G182A, L184F, Q198E, N199K, S274V, T297P. Patented claims 1 and 2 recite a protease variant having identity to SEQ ID NO: 3 (same as recited SEQ ID NO: 3) with substitution S27K that has improved wash performance such that the patented claims evidence that embodiments of patented claim have improved wash performance. SEQ ID NO: 3 is the mature polypeptide of SEQ ID NO: 2. Claims 1-5 are anticipated for this reason. Regarding claim 19, G17R and N199K is alteration of two or more alterations as to anticipate claim 19. Regarding claims 1-5 and 19-21, patented claim 15 recites a protease of recited SEQ ID NO: 19 with substitutions S27K, S4K, E127Q, G132H, and Y156R that anticipates claims 1-5 and 19-21. Regarding claim 22, patented claim 12 (depending from patented claim 1 reciting S27K) recites several substitutions including N199K, V2H, S4K, T5K, D17N and Q18K wherein in the absence of a showing of an unexpected result is not inventive to make several plural alterations as recited in patented claim 12 wherein patented claim 13 recites 1-20 alterations.
Svendsen, abstract, teaches “producing variants of a parent TY145 subtilase” wherein SEQ ID NO: 1 of Svendsen is a TY145 protease identical to recited SEQ ID NO: 3. A subtilase is a type of protease. Svendsen, paras. [0374] and [0355]-[0356], teach that such protease variants are formulated into a detergent composition including a bar and can include additional detergent additives including a protease and used in cleaning processes (hard surface cleaning). “Further the present invention comprises a method of producing a variant of a parent TY145 like subtilase, the variant having at least one altered property as compared to the parent TY145 like subtilase, the method comprising:
a) modelling the parent TY145 like subtilase on the three-dimensional structure of a TY145 like subtilase to produce a three-dimensional structure of the parent TY145 like subtilase;
b) comparing the three-dimensional structure obtained in step a) to the three-dimensional structure of a Subtilisin family subtilase;
c) identifying on the basis of the comparison in step b) at least one structural part of the parent TY145 like subtilase, wherein an alteration in said structural part is predicted to result in an altered property;
d) modifying the nucleic acid sequence encoding the parent TY145 like subtilase to produce a nucleic acid sequence encoding deletion or substitution of one or more amino acids at a position corresponding to said structural part, or an insertion of one or more amino acid residues in positions corresponding to said structural part;
e) expressing the modified nucleic acid sequence in a host cell to produce the variant TY145 like subtilase.
f) isolating the produced subtilase;
g) purifying the isolated subtilase; and
h) recovering the purified subtilase.” Svendsen, para. [0135]-[0140].
The preceding teachings of Svendsen is understood as teaching that an appropriate methodology for obtaining a protease variant, including variants of recited SEQ ID NO: 3 being a TY145 protease, is to introduce the desired alterations/substitutions into a parent protease, wherein such parent protease can be the protease of SEQ ID NO: 3 (SEQ ID NO: 1 of Svendsen), and then the variant recovered.
As such, at the time of filing, an ordinarily skilled artisan would have been motivated to formulate any TY145 protease including variants thereof as recited in the reference claims in a detergent composition as taught by Svendsen et al. and to produce any such variant by introducing alternations/substitutions, including such alterations/substitutions as recited in the reference claims, into a parent TY145 protease having recited SEQ ID NO: 3, since Svendsen teaches that the use of proteases in a detergent composition is desirable in the art as well as introduction of alterations/substitutions into a parent protease is an advantages method of obtaining protease variants as taught in the prior art or recited in the reference claims. Implementing embodiments of the reference claims as discussed meets all of the features of claims 1-15.
Regarding claims 16-18, Svendsen, para. [0261], teach that any protease enzyme consistent with the teachings is to be included in a detergent composition for laundry or dishwashing. The same is considered to be a disclosure or direct teaching or suggestion that such detergent composition to be used in a method of contacting or combining such a detergent composition containing a protease as discussed above with a laundry item or a dish (i.e. a hard surface) to be cleaned as recited in claims 16-18.
Regarding recitation in the claims of improved wash performance compared to the protease of SEQ ID NO: 3, the specification, page 15, asserts that a protease having any of the modifications taught therein has improved wash performance relative to recited SEQ ID NO: 3 due to increased net charge: “Changing the net charge of SEQ ID NO 3, SEQ ID NO 4 or SEQ ID NO 5 to become larger in model B detergent (pH 7.8) increases the wash performance of the molecule as measured in Example 2 in Materials and Methods herein.“ As such, the specification evidences that any protease having the substitution N199K as in the patented or copending claims (as appropriate) inherently has improved wash performance as described by the specification.
The present claims are not consonant with the species element requirement set forth in the file wrapper of U.S. Patent No. 11,518,987 (Ser. No. 15/535,858) since the patented claims are not limited to the elected species (i.e. alteration S27K) but further include other unelected alterations.
Claims 1, 3-9 and 11-23 (all pending claims) are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 11,001,786 B2 in view of Svendsen (U.S. 2004/0209343 A1).
Copending or patented claims are also referred to as “reference” claims. SEQ ID NO: 3 of the reference patent/claims is identical to recited SEQ ID NO: 3.
Patented claim 1 recite a protease variant having at least 75% identity to SEQ ID NO: 3 having substitutions/alterations S27K, N59L, T67V, Q70N, S171N, S173P, G174R, S175P, F180Y, Q198E, N199K, T297P. The specification (col. 13, line 1) of the reference patent directly indicates that the same species of variant inherently has improved wash performance relative to the protease with SEQ ID NO: 3. SEQ ID NO: 3 is the mature polypeptide of SEQ ID NO: 2. Claims 1-5 and 19 are anticipated for this reason.
Reference claim 7 states that the variants of reference claim 1 be formed in a detergent composition. Svendsen, abstract, teaches “producing variants of a parent TY145 subtilase” wherein SEQ ID NO: 1 of Svendsen is a TY145 protease identical to recited SEQ ID NO: 3. A subtilase is a type of protease. Svendsen, paras. [0374] and [0355]-[0356], teach that such protease variants are formulated into a detergent composition including a bar and can include additional detergent additives including an additional amylase and used in cleaning processes (hard surface cleaning). “Further the present invention comprises a method of producing a variant of a parent TY145 like subtilase, the variant having at least one altered property as compared to the parent TY145 like subtilase, the method comprising:
a) modelling the parent TY145 like subtilase on the three-dimensional structure of a TY145 like subtilase to produce a three-dimensional structure of the parent TY145 like subtilase;
b) comparing the three-dimensional structure obtained in step a) to the three-dimensional structure of a Subtilisin family subtilase;
c) identifying on the basis of the comparison in step b) at least one structural part of the parent TY145 like subtilase, wherein an alteration in said structural part is predicted to result in an altered property;
d) modifying the nucleic acid sequence encoding the parent TY145 like subtilase to produce a nucleic acid sequence encoding deletion or substitution of one or more amino acids at a position corresponding to said structural part, or an insertion of one or more amino acid residues in positions corresponding to said structural part;
e) expressing the modified nucleic acid sequence in a host cell to produce the variant TY145 like subtilase.” Svendsen, para. [0135]-[0140].
The preceding teachings of Svendsen is understood as teaching that an appropriate methodology for obtaining a protease variant, including variants of recited SEQ ID NO: 3 being a TY145 protease, is to introduce the desired alterations/substitutions into a parent protease, wherein such parent protease can be the protease of SEQ ID NO: 3 (SEQ ID NO: 1 of Svendsen).
As such, at the time of filing, an ordinarily skilled artisan would have been motivated to formulate any TY145 protease including variants thereof as recited in the reference claims in a detergent composition as taught by Svendsen et al. and to produce any such variant by introducing alternations/substitutions, including such alterations/substitutions as recited in the reference claims, into a parent TY145 protease having recited SEQ ID NO: 3, since Svendsen teaches that the use of proteases in a detergent composition is desirable in the art as well as introduction of alterations/substitutions into a parent protease is an advantages method of obtaining protease variants as taught in the prior art or recited in the reference claims. Implementing embodiments of the reference claims as discussed meets all of the features of claims 1-15.
Regarding claims 16-18, Svendsen, para. [0261], teach that any protease enzyme consistent with the teachings is to be included in a detergent composition for laundry or dishwashing. The same is considered to be a disclosure or direct teaching or suggestion that such detergent composition to be used in a method of contacting or combining such a detergent composition containing a protease as discussed above with a laundry item or a dish (i.e. a hard surface) to be cleaned as recited in claims 16-18.
Regarding recitation in the claims of improved wash performance compared to the protease of SEQ ID NO: 3, the specification, page 15, asserts that a protease having any of the modifications taught therein has improved wash performance relative to recited SEQ ID NO: 3 due to increased net charge: “Changing the net charge of SEQ ID NO 3, SEQ ID NO 4 or SEQ ID NO 5 to become larger in model B detergent (pH 7.8) increases the wash performance of the molecule as measured in Example 2 in Materials and Methods herein.“ As such, the specification evidences that any protease having the substitution N199K as in the patented or copending claims (as appropriate) inherently has improved wash performance as described by the specification.
Claims 1, 3-5, 11-15, 19 and 23 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of U.S. Patent No. 11,744,263 (Ser. No. 16/630,156) in view of Svendsen (U.S. 2004/0209343 A1).
Copending or patented claims are also referred to as “reference” claims.
SEQ ID NO: 2 of the reference claims are identical to recited SEQ ID NO: 3, wherein the same is the mature polypeptide of recited SEQ ID NO: 2.
The reference claims recite an animal feed containing a protease polypeptide having at least 95% identity to SEQ ID NO: 2 as recited therein, which is recited SEQ ID NO: 3 of the present claims.
Patented claim 21 recites that such protease is a variant with mutations/alterations including:
21. The animal feed of claim 1, wherein the polypeptide has at least 95% identity to SEQ ID NO:2 and is a variant comprising one or more substitutions selected from the group consisting of S27K, N109K, S111E, S171E, S173P, G174K, S175P, F180Y, G182A, L184F, Q198E, N199K and T297P, wherein the positions correspond to the amino acid sequence of SEQ ID NO: 2.
Reference claim 21 does not directly state S27K and N199K and/or S27K, N199K and N109K embodied into the same protease variant. However, since patented claim 21 directly recites one or more substitutions, at the time of filing an ordinarily skilled artisan would have been motivated to form an embodiment of reference claim 21 wherein S27K and N199K and/or S27K, N199K and N109K substitutions are embodied in the same protease variant, since the reference claim directly states that inclusion of plural substitutions is appropriate such that an ordinarily skilled artisan at the time of filing would have been motivated to select any two or three substitutions of those recited including S27K and N199K and/or S27K, N199K and N109K as recited in claims 1-5 and 19.
Svendsen, abstract, teaches “producing variants of a parent TY145 subtilase” wherein SEQ ID NO: 1 of Svendsen is a TY145 protease identical to recited SEQ ID NO: 3. A subtilase is a type of protease. “Further the present invention comprises a method of producing a variant of a parent TY145 like subtilase, the variant having at least one altered property as compared to the parent TY145 like subtilase, the method comprising:
a) modelling the parent TY145 like subtilase on the three-dimensional structure of a TY145 like subtilase to produce a three-dimensional structure of the parent TY145 like subtilase;
b) comparing the three-dimensional structure obtained in step a) to the three-dimensional structure of a Subtilisin family subtilase;
c) identifying on the basis of the comparison in step b) at least one structural part of the parent TY145 like subtilase, wherein an alteration in said structural part is predicted to result in an altered property;
d) modifying the nucleic acid sequence encoding the parent TY145 like subtilase to produce a nucleic acid sequence encoding deletion or substitution of one or more amino acids at a position corresponding to said structural part, or an insertion of one or more amino acid residues in positions corresponding to said structural part;
e) expressing the modified nucleic acid sequence in a host cell to produce the variant TY145 like subtilase;
f) isolating the produced subtilase;
g) purifying the isolated subtilase; and
h) recovering the purified subtilase.” Svendsen, para. [0135]-[0140].
The preceding teachings of Svendsen is understood as teaching that an appropriate methodology for obtaining a protease variant, including variants of recited SEQ ID NO: 3 being a TY145 protease, is to introduce the desired alterations/substitutions into a parent protease, wherein such parent protease can be the protease of SEQ ID NO: 3 (SEQ ID NO: 1 of Svendsen), and then the variant recovered.
As such, at the time of filing, an ordinarily skilled artisan would have been motivated to produce any TY145 protease including variants thereof as recited in the reference claims by introducing alternations/substitutions, including such alterations/substitutions as recited in the reference claims, into a parent TY145 protease having recited SEQ ID NO: 3, since Svendsen teaches that introduction of alterations/substitutions into a parent protease is an advantages method of obtaining protease variants as taught in the prior art or recited in the reference claims. Implementing embodiments of the reference claims as discussed meets all of the features of claims 1-5, 11-15 and 19.
Regarding recitation in the claims of improved wash performance compared to the protease of SEQ ID NO: 3, the specification, page 15, asserts that a protease having any of the modifications taught therein has improved wash performance relative to recited SEQ ID NO: 3 due to increased net charge: “Changing the net charge of SEQ ID NO 3, SEQ ID NO 4 or SEQ ID NO 5 to become larger in model B detergent (pH 7.8) increases the wash performance of the molecule as measured in Example 2 in Materials and Methods herein.“ As such, the specification evidences that any protease having the substitution N199K as in the patented or copending claims (as appropriate) inherently has improved wash performance as described by the specification.
Claims 1, 3-5, 11-15, 19 and 23 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 2, 10, 21-23, 26-28, 31-49 of copending Application No. 18/329,971 in view of Svendsen (U.S. 2004/0209343 A1).
Claims 1, 3-5, 11-15, 19 and 23 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-29 of U.S. Patent No. 12653209 B2 (Ser. No. 18/329,971) in view of Svendsen (U.S. 2004/0209343 A1).
Copending or patented claims are also referred to as “reference” claims.
SEQ ID NO: 2 of the reference claims are identical to recited SEQ ID NO: 3, wherein the same is the mature polypeptide of recited SEQ ID NO: 2.
The reference claims recite a method of administering a protease polypeptide to an animal, the polypeptide having at least 85% identity to SEQ ID NO: 2 as recited therein, which is recited SEQ ID NO: 3 of the present claims.
Reference claim 6 recites that such protease is a variant with mutations/alterations including:
34. . . said polypeptide has at least 90% sequence identity to SEQ ID NO: 2 and comprises one or more substitutions selected from the group consisting of S27K, N109K, S111E, S171E, S173P, G174K, S175P, F18OY, G182A, L184F, Q198E, N199K and T297P, wherein the positions correspond to the amino acid sequence of SEQ ID NO: 2.
Reference claim 6 does not directly state S27K and N199K and/or S27K, N199K and N109K embodied into the same protease variant. However, since reference claim 6 directly recites one or more substitutions, at the time of filing an ordinarily skilled artisan would have been motivated to form an embodiment of reference claim 8 wherein S27K and N199K and/or S27K, N199K and N109K substitutions are embodied in the same protease variant, since the reference claim directly states that inclusion of plural substitutions is appropriate such that an ordinarily skilled artisan at the time of filing would have been motivated to select any two or three substitutions of those recited including S27K and N199K and/or S27K, N199K and N109K as recited in claims 1, 3-5 and 19.
Svendsen, abstract, teaches “producing variants of a parent TY145 subtilase” wherein SEQ ID NO: 1 of Svendsen is a TY145 protease identical to recited SEQ ID NO: 3. A subtilase is a type of protease. “Further the present invention comprises a method of producing a variant of a parent TY145 like subtilase, the variant having at least one altered property as compared to the parent TY145 like subtilase, the method comprising:
a) modelling the parent TY145 like subtilase on the three-dimensional structure of a TY145 like subtilase to produce a three-dimensional structure of the parent TY145 like subtilase;
b) comparing the three-dimensional structure obtained in step a) to the three-dimensional structure of a Subtilisin family subtilase;
c) identifying on the basis of the comparison in step b) at least one structural part of the parent TY145 like subtilase, wherein an alteration in said structural part is predicted to result in an altered property;
d) modifying the nucleic acid sequence encoding the parent TY145 like subtilase to produce a nucleic acid sequence encoding deletion or substitution of one or more amino acids at a position corresponding to said structural part, or an insertion of one or more amino acid residues in positions corresponding to said structural part;
e) expressing the modified nucleic acid sequence in a host cell to produce the variant TY145 like subtilase;
f) isolating the produced subtilase;
g) purifying the isolated subtilase; and
h) recovering the purified subtilase.” Svendsen, para. [0135]-[0140].
The preceding teachings of Svendsen is understood as teaching that an appropriate methodology for obtaining a protease variant, including variants of recited SEQ ID NO: 3 being a TY145 protease, is to introduce the desired alterations/substitutions into a parent protease, wherein such parent protease can be the protease of SEQ ID NO: 3 (SEQ ID NO: 1 of Svendsen), and then the variant recovered.
As such, at the time of filing, an ordinarily skilled artisan would have been motivated to produce any TY145 protease including variants thereof as recited in the reference claims by introducing alternations/substitutions, including such alterations/substitutions as recited in the reference claims, into a parent TY145 protease having recited SEQ ID NO: 3, since Svendsen teaches that introduction of alterations/substitutions into a parent protease is an advantages method of obtaining protease variants as taught in the prior art or recited in the reference claims. Implementing embodiments of the reference claims as discussed meets all of the features of claims 1, 2-5, 11-15 and 19.
Regarding recitation in the claims of improved wash performance compared to the protease of SEQ ID NO: 3, the specification, page 15, asserts that a protease having any of the modifications taught therein has improved wash performance relative to recited SEQ ID NO: 3 due to increased net charge: “Changing the net charge of SEQ ID NO 3, SEQ ID NO 4 or SEQ ID NO 5 to become larger in model B detergent (pH 7.8) increases the wash performance of the molecule as measured in Example 2 in Materials and Methods herein.“ As such, the specification evidences that any protease having the substitution N199K as in the patented or copending claims (as appropriate) inherently has improved wash performance as described by the specification.
Claims 1, 3-9, 11-19 and 23 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 8 of copending Application No. 17/299,273 in view of Svendsen (U.S. 2004/0209343 A1).
Copending or patented claims are also referred to as “reference” claims. SEQ ID NO: 3 of the reference patent/claims is identical to recited SEQ ID NO: 3.
Reference claim 8 recites a powder detergent composition wherein reference claim 8 recites that such composition includes a protease variant with at least 80% identity with recited SEQ ID NO: 3 (also SEQ ID NO: 3 of reference claims) with one or more substitutions selected from a list including S27K and N199K. Since reference claim 8 states one or more, an ordinarily skilled artisan would have been motivated to produce proteases having two of the substitutions recited.
As such, reference claim anticipates at least claims 1, 3-5, 6, 9 and 19 wherein a powder detergent composition is considered to be within the scope of a regular or compact powder.
Svendsen, abstract, teaches “producing variants of a parent TY145 subtilase” wherein SEQ ID NO: 1 of Svendsen is a TY145 protease identical to recited SEQ ID NO: 3. A subtilase is a type of protease. Svendsen, paras. [0374] and [0355]-[0356], teach that such protease variants are formulated into a detergent composition including a powder and can include additional detergent additives including a protease and used in cleaning processes (hard surface cleaning). “Further the present invention comprises a method of producing a variant of a parent TY145 like subtilase, the variant having at least one altered property as compared to the parent TY145 like subtilase, the method comprising:
a) modelling the parent TY145 like subtilase on the three-dimensional structure of a TY145 like subtilase to produce a three-dimensional structure of the parent TY145 like subtilase;
b) comparing the three-dimensional structure obtained in step a) to the three-dimensional structure of a Subtilisin family subtilase;
c) identifying on the basis of the comparison in step b) at least one structural part of the parent TY145 like subtilase, wherein an alteration in said structural part is predicted to result in an altered property;
d) modifying the nucleic acid sequence encoding the parent TY145 like subtilase to produce a nucleic acid sequence encoding deletion or substitution of one or more amino acids at a position corresponding to said structural part, or an insertion of one or more amino acid residues in positions corresponding to said structural part;
e) expressing the modified nucleic acid sequence in a host cell to produce the variant TY145 like subtilase;
f) isolating the produced subtilase;
g) purifying the isolated subtilase; and
h) recovering the purified subtilase.” Svendsen, para. [0135]-[0140].
The preceding teachings of Svendsen is understood as teaching that an appropriate methodology for obtaining a protease variant, including variants of recited SEQ ID NO: 3 being a TY145 protease, is to introduce the desired alterations/substitutions into a parent protease, wherein such parent protease can be the protease of SEQ ID NO: 3 (SEQ ID NO: 1 of Svendsen), and then the variant recovered.
As such, at the time of filing, an ordinarily skilled artisan would have been motivated to formulate any TY145 protease including variants thereof as recited in the reference claims in a detergent composition as taught by Svendsen et al. and to produce any such variant by introducing alternations/substitutions, including such alterations/substitutions as recited in the reference claims, into a parent TY145 protease having recited SEQ ID NO: 3, since Svendsen teaches that the use of proteases in a detergent composition is desirable in the art as well as introduction of alterations/substitutions into a parent protease is an advantages method of obtaining protease variants as taught in the prior art or recited in the reference claims. Implementing embodiments of the reference claims as discussed meets all of the features of claims 1, 3-9, 11-15.
Regarding claims 16-18, Svendsen, para. [0261], teach that any protease enzyme consistent with the teachings is to be included in a detergent composition for laundry or dishwashing. The same is considered to be a disclosure or direct teaching or suggestion that such detergent composition to be used in a method of contacting or combining such a detergent composition containing a protease as discussed above with a laundry item or a dish (i.e. a hard surface) to be cleaned as recited in claims 16-18.
Regarding recitation in the claims of improved wash performance compared to the protease of SEQ ID NO: 3, the specification, page 15, asserts that a protease having any of the modifications taught therein has improved wash performance relative to recited SEQ ID NO: 3 due to increased net charge: “Changing the net charge of SEQ ID NO 3, SEQ ID NO 4 or SEQ ID NO 5 to become larger in model B detergent (pH 7.8) increases the wash performance of the molecule as measured in Example 2 in Materials and Methods herein.“ As such, the specification evidences that any protease having the substitution N199K as in the patented or copending claims (as appropriate) inherently has improved wash performance as described by the specification.
This is a provisional nonstatutory double patenting rejection.
Response to arguments
Applicant argues:
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The Examiner agrees with the meaning of parent protease. The applicant asserts that the claim is not a product-by-process. However, in remarks above applicant states that the parent protease is defined as “a starting sequence or a reference sequence from which a variant is generated.” Generated is a past participle verb. Generating a variant from a starting sequence is a process. As such, these arguments are contradictory.
Claim 1 does not recite a method of “generating” an embodiment protease from a parent protease. Further, embodiments of the claims are not required to be generated from a “parent protease.” See MPEP 2113(I).
For example, a protease identical to SEQ ID NO: 3 with the following substitutions from claim 3 is an embodiment of claims 1 and 3, including the recited increased wash performance property, regardless of how such polypeptide/protease is formed:
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Such a protease/polypeptide can be made by solid state peptide synthesis without the involvement of any “parent” enzyme.
Such a protease can be made by producing an encoding polynucleotide by solid-phase oligonucleotide synthesis, such polynucleotide cloned into a vector and the protease/polypeptide expressed in a host cell, such a process not involving a “parent” enzyme.
Or consider a case wherein a product protease that is identical to SEQ ID NO: 3 except having the 13 substitutions indicated above and having an additional 4% of amino acid residues substituted (herein product protease).
Such a product protease can be made starting from a preformed polynucleotide encoding a protease with about 95.8% identity to SEQ ID NO: 3, not having any of the substitutions recited in claim 1 and having protease activity that is 25% of the activity of the protease of SEQ ID NO: 3 (herein, starting protease A), performing site-directed mutagenesis such that a produced polynucleotide encodes the product protease cited above, and then such mutated polynucleotide cloned into a vector and expressed in a host cell to produce the product protease. Such a process does not involve a “parent” enzyme as far as one enzyme is not transformed into another enzyme wherein a starting nucleotide is not a parent enzyme. The same process can be repeated producing the same product protease except the staring polynucleotide has 96.3% identity to SEQ ID NO: 3, does not have any the substitutions recited in claim 1 and has protease activity that is 85% of the activity of the protease of SEQ ID NO: 3 (herein starting protease B). The product protease does not have improved wash performance relative to the protease of SEQ ID NO: 3 or starting protease B, but does have increased wash performance relative to starting protease A. In such a scenario, it is not clear if the product protease is an embodiment of the claims.
That is, the claims present a paradox wherein embodiments are required to have increased wash performance relative to a parent protease wherein embodiments of the claims can be made by methods that do not require any parent protease, or wherein the same protease can be made from a number of plural parent proteases. As such, an ordinarily skilled artisan is unable to understand how to avoid infringement wherein a particular parent protease cannot be definitively identified.
Applicant argues:
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Increased wash performance is an intrinsic property of a protease defined by its amino acid sequence which has several contributors including protease activity and stability. The rejected claims do not recite a method nor a detergent composition. Claim 1 recites a protease variant only. As such, the following are embodiments of claim 1:
An embodiment protease variant in a generic buffer in a plastic tube.
An animal feed (or any other composition) to which the contents of the above plastic tube has been combined with including then feeding the same to an animal.
As such, an animal feed having a protease that has improved wash performance as an intrinsic activity and meeting all of the features of claim 1 anticipates the claims.
Regarding claims of the ‘273 application, claim 1 is understood as being open to the inclusion of other components in addition to the protease variant. For example, claim 6 recites a detergent composition. The recitation of any composition including an embodiment protease variant, regardless of how many additional features may be recited, anticipates at least claim 1.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to TODD M EPSTEIN whose telephone number is (571)272-5141. The examiner can normally be reached Mon-Fri 9:00a-5:30p.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert Mondesi can be reached at (408) 918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/TODD M EPSTEIN/Primary Examiner, Art Unit 1652
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