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 .
Any objection or rejection from the previous office action, which is not restated here, is withdrawn.
Election/Restrictions
Applicant's election with traverse of Group I (i.e., claims 1-22 drawn to a polypeptide) in the reply filed on 10/16/24 is acknowledged. Applicant’s election with traverse of a single and specific polypeptide as SEQ ID NO: 6 in the reply filed on 10/16/24 is acknowledged.
Applicants’ arguments and the response to their arguments in the Action mailed on 11/15/24. The requirement is still deemed proper and is therefore made FINAL.
Please note that the species is expanded to include SEQ ID NOs: 2-5, 11-14, and 55-65. As such, claims 3 and 28 are hereby rejoined for examination.
Status of Claims
Claims 1-27 were originally filed on March 15, 2024.
The amendment received on February 25, 2025, canceled claim 2; amended claims 1 and 16; and added new claim 28. The amendment received on November 24, 2025, canceled claim 5; amended claims 1, 3-4, 6, and 8; and added new claim 29.
Claims 1, 3-4, and 6-29 are currently pending and claims 1, 3, 6-11, and 28-29 are under consideration as claims 3 and 12-22 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species, and claims 23-27 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 10/16/24.
Priority
The present application claims the benefit under 35 U.S.C. 119(e) to U.S. Provisional Application Nos. 63/472,634 filed June 13, 2023; and 63/452,773 filed March 17, 2023. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, or 365(c) is acknowledged.
Sequence Interpretation
For claim 1, please note that the Examiner is interpreting the scope as open-ended requiring 100% identity to SEQ ID NO: 5 with any N- and/or C-terminal additions where X12 must be Ala and X14 must be Leu, i.e., TXXXXXXXTASLXXWKKXG, but the remaining X’s can be any amino acid as long as the polypeptide sequence is not the sequence of SEQ ID NO: 1, i.e., TVTIFVAGVLTASLTIWKKMG.
For claim 3, please note that the Examiner is interpreting the scope as open-ended requiring 100% identity to one of the recited sequences with any N- and/or C-terminal additions where the variable residues are as described in the sequence listing except for X12 being Ala and X14 being Leu.
For claim 6, please note that the Examiner is interpreting the scope as open-ended requiring 100% identity to one of the recited sequences with any N- and/or C-terminal additions where one of X12, X14, X15, and X16 is Ala. However, as further discussed in the 112(d) rejection below, since claim 1 requires X12 to be Ala, each of the sequences already contains an X that is Ala. Therefore, as long as the limitations of claim 1 are met, the limitations of claim 6 are met.
For claim 28, please note that the Examiner is interpreting the scope as open-ended requiring 100% identity to SEQ ID NO: 5 with any N- and/or C-terminal additions, i.e., TXXXXXXXTXSXXXWKKXG, but the remaining X’s can be any amino acid as long as the polypeptide sequence is not the sequence of SEQ ID NO: 1, i.e., TVTIFVAGVLTASLTIWKKMG.
For claim 29, please note that the Examiner is interpreting the scope as open-ended requiring 100% identity to SEQ ID NO: 57 with any N- and/or C-terminal additions, i.e., TATIAVAGVLTASLTIWKKMG.
Response to Arguments
Applicant’s arguments, see Response, filed 11/24/25, with respect to the claim objection have been fully considered and are persuasive. The objection of claim 8 has been withdrawn.
Applicant’s arguments, see Response, filed 11/24/25, with respect to the 112(d) rejection have been fully considered and are persuasive. The rejection of claim 5 as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends has been withdrawn.
Applicant’s arguments, see Response, filed 11/24/25, with respect to the 112(d) rejection have been fully considered and are persuasive. The rejection of claim 5 as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends has been withdrawn.
Applicant’s arguments, see Response, filed 11/24/25, with respect to the 101 rejection have been fully considered and are persuasive. The rejection of claims 1 and 5 as being directed to a judicial exception (i.e., a natural product) without significantly more has been withdrawn.
Applicant’s arguments, see Response, filed 11/24/25, with respect to the 102(a)(1) rejection have been fully considered and are persuasive. The rejection of claims 1 and 5 as being anticipated by La Rosa et al. US Publication No. 2004/0214272 A1 published on October 28, 2004 has been withdrawn.
Applicant’s arguments, see Response, filed 11/24/25, with respect to the 103(a) rejection have been fully considered and are persuasive. The rejection of claims 1 and 7-11 as being unpatentable over La Rosa et al. US Publication No. 2004/0214272 A1 published on October 28, 2004 as applied to claim 1 above, and further in view of Adessi et al., Curr. Medicinal Chem. 9:963-978 (2002) has been withdrawn.
New Rejections Necessitated by Amendment
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 6 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 6 is directed to where an X comprised by one of SEQ ID NOs: 2-5, 7, 54, 55 or 65 is Ala. However, claim 6 is dependent upon claim 1, which that requires that X12 be Ala in SEQ ID NO: 5. As such, the scope of claim 6 does not further limit that of claim 1.
Additionally, SEQ ID NO: 65 has the sequence of: XXXVXXXLTXSXXXXKK where each X can be any amino acid. However, SEQ ID NO: 5 is in claim 1 requires the sequence: TXXXXXXXTASLXXWKKXG, where the bold residues in SEQ ID NO: 5 are not required in SEQ ID NO: 65. As such, SEQ ID NO: 65 in claim 6 broadens the scope of SEQ ID NO: 5 in claim 1. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Please note that the Examiner is interpreting the scope of claim 6 such that if the limitations of claim 1 are met, then the limitations of claim 6 are also met in order to advance prosecution.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 3, 6, and 28 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a natural product) without significantly more. Claim 1 recites a polypeptide comprising at least nucleophosmin-binding domain, each nucleophosmin-binding domain the sequence of SEQ ID NO: 5 (TX4X5X6X7X8X9X10TX12SX14X15X16WKKX20G) where X12 is Ala, X14 is leucine, and the remaining Xaa’s are any amino acid. Please see the “Sequence Interpretation” section above. Briefly, the polypeptide of claim 1 encompasses a polypeptide comprising at least one nucleophosmin-binding domain, each nucleophosmin-binding domain comprising an amino acid sequence having 100% identity to SEQ ID NO: 5 with any N- and/or C-terminal additions where X12 is Ala, X14 is leucine as long as the polypeptide sequence does not comprise SEQ ID NO: 1. Claim 3 is directed to where the polypeptide comprises SEQ ID NO: 59. Claim 6 is directed to where an X comprised by SEQ ID NO: 5 is Ala. Claim 28 is identical in scope to claim 1 except X12 is not limited to Ala and X14 is not limited to Leu.
Yamazaki et al. teaches the full length of feline bax, bcl-2, bcl-xL, and caspase 3 genes (Yamazaki et al., Vet. Microbiol. 101:1-8 (2004) at abstract). In Figure 1, Yamazaki et al. teaches the amino acid sequence of feline bax where residues 172-192 are TVTIFVAGVLTASLAIWKKMG (See Yamazaki, Figure 1) thereby constituting a polypeptide comprising at least one domain, each domain comprising the sequence of instant SEQ ID NO: 5 where X4 is Ile, X5 is Phe, X6 is Val, X7 is Ala, X8 is Gly, X9 is Val, X10 is Leu, X12 is Ala, X14 is Leu, X15 is Ala, X16 is Ile, and X20 is Met. As such, the feline bax amino acid sequence constitutes a polypeptide comprising instant SEQ ID NO: 5 and SEQ ID NO: 59. Moreover, the feline bax amino acid sequence does not comprise SEQ ID NO: 1 given that the bold residue is Ala (i.e., X15) in the feline bax amino acid sequence whereas the residue in SEQ ID NO: 1 is Thr. As such, claims 1, 3, 6, and 28 encompass a naturally occurring polypeptide, which is not markedly different from its naturally occurring counterpart because it conveys the same genetic information.
Moreover, it is noted that the only structural component recited in claim 1 is the polypeptide sequence. As such, without evidence to the contrary, the naturally occurring peptide disclosed by Yamazaki et al. would inherently function as a nucleophosmin-binding domain. Thus, claim 1 encompasses a naturally occurring peptide, which is not markedly different from its naturally occurring counterpart because it conveys the same genetic information.
This judicial exception is not integrated into a practical application because claims 1, 3, 6, and 28 fail to recite a practical application of the polypeptide. Further, as discussed above, claims 1 and 28 recite that the polypeptide comprises a domain that functions as a nucleophosmin-binding domain thereby constituting a practical application. However, such a recitation does not add a meaningful limitation as it merely recites an inherent function of the naturally occurring polypeptide and is nothing more than an attempt to generally link the product of nature to a particular technological environment.
The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the structure of the claimed polypeptide does not require a modification that is significantly more than the naturally occurring polypeptide in order to result in a markedly different polypeptide.
Accordingly, it is the Examiner’s position that the claimed polypeptide is directed to a “product of nature” exception without significantly more because it does not exhibit markedly different characteristics from its naturally occurring counterparts in their natural state. More specifically, the claimed nature-based product is derived from a naturally occurring polypeptide, and thus, the comparison is with the naturally occurring polypeptide. It is noted that the claimed polypeptide is identical in amino acid sequence and structure to the naturally occurring polypeptide. Thus, the claims 1, 3, 6, and 28 encompass patent ineligible subject matter.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1, 3, 6, and 28 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Yamazaki et al., Vet. Microbiol. 101:1-8 (2004).
For claims 1, 3, 6, and 28, with respect to a polypeptide comprising at least one domain, each domain comprises the sequence of SEQ ID NO: 5 (TX4X5X6X7X8X9X10TX12SX14X15X16WKKX20G) where X12 is Ala and X14 is Leu and where the polypeptide does not comprise SEQ ID NO: 1 as recited in instant claim 1; with respect to where the polypeptide comprises instant SEQ ID NOs: 2-5 or 59 as recited in instant claim 3; with respect to where an X comprised by SEQ ID NO: 5 or 65 is Ala as recited in instant claim 6; with respect to a polypeptide comprising at least one domain, each domain comprises the sequence of SEQ ID NO: 5 (TX4X5X6X7X8X9X10TX12SX14X15X16WKKX20G) where Xaa’s are any amino acid and where the polypeptide does not comprise SEQ ID NO: 1 as recited in instant claim 28:
Yamazaki et al. discloses the full length of feline bax, bcl-2, bcl-xL, and caspase 3 genes (Yamazaki et al., Vet. Microbiol. 101:1-8 (2004) at abstract). In Figure 1, Yamazaki et al. discloses the amino acid sequence of feline bax where residues 172-192 are WQTVTIFVAGVLTASLAIWKKMG (See Yamazaki, Figure 1). When comparing residues 170-192 of the feline bax amino acid sequence to instant SEQ ID NOs: 2-5, 59, and 65, there is 100% identity. As such, the feline bax amino acid sequence constitutes a polypeptide comprising at least one domain, each domain comprising the sequence of instant SEQ ID NO: 5 where X4 is Ile, X5 is Phe, X6 is Val, X7 is Ala, X8 is Gly, X9 is Val, X10 is Leu, X12 is Ala, X14 is Leu, X15 is Ala, X16 is Ile, and X20 is Met. Thus, the feline bax amino acid sequence constitutes a polypeptide comprising instant SEQ ID NO: 5 and SEQ ID NOs: 2-4, 59, or 65. Moreover, the feline bax amino acid sequence does not comprise SEQ ID NO: 1 given that the bold residue is Ala (i.e., X15) in the feline bax amino acid sequence whereas the residue in SEQ ID NO: 1 is Thr. Plus, the feline bax amino acid sequence contains an Ala at an X of SEQ ID NOs: 2-5 or 65. Therefore, the disclosure of Yamazaki et al. satisfies the claim limitations as recited in instant claims 1, 3, 6, and 28.
For claims 1 and 28, with respect to where the domain is a nucleophosmin-binding domain:
Although Yamazaki et al. does not expressly disclose that the feline amino acid sequence contains a nucleophosmin-binding domain, since Yamazaki et al. discloses a polypeptide comprising instant SEQ ID NO: 5 thereby constituting a well-known sequence, the functional property (i.e., domain that is nucleophosmin-binding) of the polypeptide as claimed and the known sequence are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new functional property (i.e., domain that is nucleophosmin-binding) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977).
Additionally and/or alternatively, pursuant to MPEP 2112.01(II), “[p]roducts of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id. Therefore, the feline bax amino acid sequence disclosed by Yamazaki et al. inherently exhibits the property of nucleophosmin-binding as recited in instant claim 1.
Accordingly, the disclosure of Yamazaki et al. anticipates instant claims 1, 3, 6, and 28.
Claims 1, 3, 6-11, and 28 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Boohaker et al., Mol. Pharm. 9:2080-2093 (2012).
For claims 1, 3, 6-11, and 28, with respect to a polypeptide comprising at least one domain, each domain comprises the sequence of SEQ ID NO: 5 (TX4X5X6X7X8X9X10TX12SX14X15X16WKKX20G) where X12 is Ala and X14 is Leu and where the polypeptide does not comprise SEQ ID NO: 1 as recited in instant claim 1; with respect to where the polypeptide comprises instant SEQ ID NOs: 2-5 or 59 as recited in instant claim 3; with respect to where an X comprised by SEQ ID NO: 5 or 65 is Ala as recited in instant claim 6; with respect to where the polypeptide further comprises at least one N-terminus modification such as acetylation and/or at least one C-terminus modification such as amidation as recited in instant claims 7-11; with respect to a polypeptide comprising at least one domain, each domain comprises the sequence of SEQ ID NO: 5 (TX4X5X6X7X8X9X10TX12SX14X15X16WKKX20G) where Xaa’s are any amino acid and where the polypeptide does not comprise SEQ ID NO: 1 as recited in instant claim 28:
Boohaker et al. discloses a CT20p (i.e., C-terminus of Bax) peptide with the amino acid sequence of Ac-VTIFVAGVLTASLTIWKKMG-NH2 (See Boohaker, pg. 3, 2nd paragraph). When comparing to instant SEQ ID NOs: 4-5, 59, and 65, there is 100% identity. As such, the CT20p peptide constitutes a polypeptide comprising at least one domain, each domain comprising the sequence of instant SEQ ID NO: 5 where X4 is Ile, X5 is Phe, X6 is Val, X7 is Ala, X8 is Gly, X9 is Val, X10 is Leu, X12 is Ala, X14 is Leu, X15 is Thr, X16 is Ile, and X20 is Met. Thus, the CT20p peptide constitutes a polypeptide comprising instant SEQ ID NO: 5 and SEQ ID NOs: 4 or 65. Moreover, the CT20p peptide does not comprise SEQ ID NO: 1 given the CT20p N-terminal residue is Val whereas the N-terminal residue in SEQ ID NO: 1 is Thr. Plus, the feline bax amino acid sequence contains an Ala at an X of SEQ ID NOs: 4 or 65. Furthermore, the CT20p peptide is acetylated at the N-terminus and amidated at the C-terminus thereby constituting a N-terminus modification and a C-terminus modification such as acetylation and amidation, respectively. Therefore, the disclosure of Boohaker et al. satisfies the claim limitations as recited in instant claims 1, 3, 6-11, and 28.
For claims 1 and 28, with respect to where the domain is a nucleophosmin-binding domain:
Although Boohaker et al. does not expressly disclose that the CT20p peptide contains a nucleophosmin-binding domain, since Boohaker et al. discloses a polypeptide comprising instant SEQ ID NO: 5 thereby constituting a well-known sequence, the functional property (i.e., domain that is nucleophosmin-binding) of the polypeptide as claimed and the known sequence are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new functional property (i.e., domain that is nucleophosmin-binding) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977).
Additionally and/or alternatively, pursuant to MPEP 2112.01(II), “[p]roducts of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id. Therefore, the CT20p peptide disclosed by Boohaker et al. inherently exhibits the property of nucleophosmin-binding as recited in instant claims 1 and 28.
Accordingly, the disclosure of Boohaker et al. anticipates instant claims 1, 3, 6-11, and 28.
Allowable Subject Matter
Claim 29 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims. It is noted that there is no teaching or suggestion in the art to arrive at a polypeptide having 100% identity with any N- and/or C-terminal additions to instant SEQ ID NO: 57. Furthermore, there is no indication that the polypeptide occurs naturally. Thus, when the polypeptide comprises instant SEQ ID NO: 57, it is free of the prior art.
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.
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/THEA D' AMBROSIO/Primary Examiner, Art Unit 1654