DETAILED CORRESPONDENCE
Status of the Application
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 May 7, 2026 has been entered.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1, 4-6, 11-15, and 21-28 are pending in the application.
Applicant’s amendment to the claims, filed May 7, 2026, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s remarks, filed May 7, 2026 in response to the final rejection mailed November 7, 2025 are acknowledged and have been fully considered.
The text of those sections of Title 35 U.S. Code not included in the instant action can be found in a prior Office action.
Restriction/Election
In response to a requirement for restriction/election mailed November 9, 2022, applicant elected without traverse the invention of Group I, pending claims 1, 4-6, 11-15, and 21-28, drawn to an engineered peptide for mediated degradation of a target infectious microbe, species (A), the targeting domain comprises an sACE2-derived peptide consisting of SEQ ID NO: 1, and species (AA), the ubiquitin ligase recruiting domain is an Fc domain in the reply filed April 11, 2023 and in a telephone conversation with Paul Haun on April 20, 2023.
Claims 14, 15, and 21-28 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected species, there being no allowable generic or linking claim.
Claims 1, 4-6, and 11-13 are being examined on the merits to the extent the claims read on the elected subject matter.
Claim Rejections - 35 USC § 112(b)
Claims 1, 4-6, and 11-13 are newly rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Claim 1 (claims 4-6 and 11-13 dependent therefrom) is confusing in the recitation of “an endogenous human protein including a targeting domain…and a ubiquitin ligase recruitment domain, wherein the targeting domain comprise the amino acid sequence of SEQ ID NO: 1…and the ubiquitin ligase recruiting domain comprises an Fc domain.” According to the instant specification, the claimed engineered peptide is a man-made fusion of the peptide of SEQ ID NO: 1 and an Fc domain with SEQ ID NO: 1 being the sequence of a peptide fragment derived from soluble angiotensin converting enzyme 2 (paragraph [0044], Table 1), and the Fc domain being an antibody recognition domain (paragraph [0007]). Given that the targeting domain of SEQ ID NO: 1 and the Fc domain components of the fusion protein are derived from distinct proteins and are fused together by the hand of man, one of skill in the art would recognize that there is no “endogenous human protein” that includes the sequence of SEQ ID NO: 1 and an Fc domain. In the interest of advancing prosecution, applicant may consider an amendment to delete “an endogenous human protein.”
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 1, 4-6, and 11-13 are newly rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a new matter rejection.
MPEP § 2163.II.A.3.(b) states, “when filing an amendment an applicant should show support in the original disclosure for new or amended claims”. See also MPEP 714.02. MPEP § 2163.II.A.3.(b) further states, “[i]f the originally filed disclosure does not provide support for each claim limitation, or if an element which applicant describes as essential or critical is not claimed, a new or amended claim must be rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112, para. 1, as lacking adequate written description”. According to MPEP § 2163.I.B, “While there is no in haec verba requirement, newly added claim limitations must be supported in the specification through express, implicit, or inherent disclosure” and “The fundamental factual inquiry is whether the specification conveys with reasonable clarity to those skilled in the art that, as of the filing date sought, applicant was in possession of the invention as now claimed. See, e.g., Vas-Cath, Inc., 935 F.2d at 1563-64, 19 USPQ2d at 1117”.
Claim 1 (claims 4-6 and 11-13 dependent therefrom) has been amended to recite “an endogenous human protein including a targeting domain…and a ubiquitin ligase recruitment domain, wherein the targeting domain comprise the amino acid sequence of SEQ ID NO: 1…and the ubiquitin ligase recruiting domain comprises an Fc domain.” According to applicant’s remarks at p. 7, top, support for this amendment is at the paragraph corresponding to paragraph [0046] of the instant specification. However, while paragraph [0046] of the instant specification provides descriptive support for “both peptide and E3 ubiquitin ligase components can be engineered from endogenous human proteins,” there is no apparent descriptive support for “an endogenous human protein including a targeting domain…and a ubiquitin ligase recruitment domain, wherein the targeting domain comprise the amino acid sequence of SEQ ID NO: 1…and the ubiquitin ligase recruiting domain comprises an Fc domain” as recited in claim 1. In the interest of advancing prosecution, applicant may consider an amendment to delete “an endogenous human protein.”
Claim Rejections - 35 USC § 103
Claims 1, 4-6, 11, and 12 are rejected under 35 U.S.C. 103 as being unpatentable over Mourtada et al. (WO 2019/118893 A1; cited on Form PTO-892 mailed on June 2, 2023; hereafter “Mourtada”) in view of Walensky et al. (WO 2021/216845 A1 with priority to April 2020; cited on Form PTO-892 mailed on June 2, 2023; hereafter “Walensky”) and Clift et al. (Cell 172:1692-1706, 2017, e18, 34 pages; cited on Form PTO-892 mailed on June 2, 2023; hereafter “Clift”). This rejection is modified from its previous version in order to address the applicant’s amendment to the claims.
As amended, claims 1, 4-6, 11, and 12 are drawn to (in relevant part) an engineered peptide for mediated degradation of a target virus, comprising:
a fusion protein comprising an endogenous human protein including a targeting domain for binding to a spike protein receptor and a ubiquitin ligase recruitment domain, wherein the targeting domain comprises the amino acid sequence of SEQ ID NO: 1, and the ubiquitin ligase recruiting domain comprises an Fc domain.
Regarding instant claim 1, Mourtada teaches peptide degron chimeras that act as protein degradation-inducing moieties and teaches the peptide degron chimeras include combining a peptide that binds and recruits a degrader protein with a peptide, which is incorporated for targeting a disease-related protein (p. 19, first full paragraph). Mourtada teaches the degrader protein is an E3 ubiquitin ligase (p. 27, first full paragraph). Mourtada teaches the targeted proteins can be of viral origin and are involved in or that are causative of disease and the chimeras are useful for treating diseases driven by such pathologic proteins (p. 2, first full paragraph).
Mourtada does not teach or suggest the claim 1 limitation “the targeting domain comprise the amino acid sequence of SEQ ID NO: 1.”
Walensky teaches structurally stabilized peptides that target the receptor binding domain (RBD) of the spike (S) protein of SARS-CoV-2, the peptides being useful for treating coronavirus infection (Abstract; p. 37, lines 20-28). Walensky teaches an ACE2 α1 helix sequence (SEQ ID NO: 1 of Walensky) that targets the RBD of SARS-CoV-2 (paragraph bridging pp. 38-39; Table 1). SEQ ID NO: 1 of Walensky comprises the amino acid sequence of SEQ ID NO: 1 of this application.
In view of the combined teachings of Mourtada and Walensky, it would have been obvious to one of ordinary skill in the art before the effective filing date to use the ACE2 α1 helix sequence of Walensky as the targeting peptide of the peptide degron chimera of Mourtada. One would have been motivated and would have expected success to do so because Mourtada taught a peptide degron chimera including a peptide for targeting a viral disease-related protein and Walensky teaches a peptide that targets a viral disease-related protein.
Mourtada also does not teach or suggest the claim 1 limitation “the ubiquitin ligase recruiting domain comprises an Fc domain.”
Clift teaches that antibody-bound pathogens can be recognized by the E3 ubiquitin ligase TRIM21, which binds with high affinity to the Fc domain of antibodies (p. 1692, column 2, bottom). Clift teaches that during infection, TRIM21 recruits the ubiquitin-proteasome system to antibody-bound pathogens, leading to their destruction (p. 1692, column 2, bottom). Clift teaches a fusion protein comprising an Fc domain fused to the C-terminus of a nanobody (Figure 2(I); p. e5, top) for degradation of the protein targeted by the nanobody (paragraph bridging pp. 1692-1693; p. 1694, column 2, middle).
In view of the combined teachings of Mourtada and Clift, it would have been obvious to one of ordinary skill in the art before the effective filing date to use the Fc domain of Clift as the peptide that binds and recruits a degrader protein in the peptide degron chimera of Mourtada. One would have been motivated and would have expected success to do so because Mourtada taught a peptide degron chimera comprising a peptide that binds and recruits an E3 ubiquitin ligase for degradation of the targeted protein, and Clift taught an Fc domain fused to a peptide targeting domain (a nanobody) to recruit an E3 ubiquitin ligase (TRIM21) for degradation of the targeted protein.
The combination of Mourtada, Walensky, and Clift does not teach or suggest the peptide degron chimera of Mourtada modified according to Walensky and Clift as described above comprises “an endogenous human protein.” However, in view of the indefiniteness of “an endogenous human protein” in the context of claim 1 and because the structure of the peptide degron chimera of Mourtada modified according to Walensky and Clift is substantially identical to the structure recited in claim 1, the peptide degron chimera of Mourtada modified according to Walensky and Clift is considered to satisfy the limitation of “an endogenous human protein” in claim 1.
Regarding instant claims 4-6, the combination of Mourtada, Walensky, and Clift does not teach or suggest the S protein of SARS-CoV-2 is part of a SARS-CoV-2 viral envelope. However, given that the S protein of SARS-CoV-2 is inherently part of the viral envelope of SARS-CoV-2 and the ACE2 α1 helix sequence of Walensky targets the RBD of the S protein of SARS-CoV-2 (see Abstract and p. 37, lines 20-28 of Walensky), the ACE2 α1 helix sequence of Walensky necessarily targets the S protein of the viral envelope of SARS-CoV-2.
Regarding instant claim 11, Clift teaches the Fc domain is fused to the C-terminus of the nanobody (Figure 2(I); p. e5, top).
Regarding instant claim 12, Mourtada teaches the degrader protein that is recruited by the peptide degron chimera is an E3 ubiquitin ligase (p. 27, first full paragraph) and Clift teaches the Fc domain binds to the E3 ubiquitin ligase TRIM21 (p. 1692, column 2, bottom).
Therefore, the engineered peptide of claims 1, 4-6, 11, and 12 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claim 13 is rejected under 35 U.S.C. 103 as being unpatentable over Mourtada in view of Walensky and Clift as applied to claims 1, 4-6, 11, and 12 above, and further in view of GenBank Database Accession Number NP_003132 (May 2019, 3 pages; cited on Form PTO-892 mailed on June 2, 2023; hereafter “GenBank”).
The relevant teachings of Mourtada, Walensky, and Clift as applied to claims 1, 4-6, 11, and 12 are set forth above.
The combination of Mourtada, Walensky, and Clift does not teach or suggest the amino acid sequence of TRIM21 is SEQ ID NO: 4.
The reference of GenBank teaches the amino acid sequence of human TRIM21 (p. 3), which is identical to SEQ ID NO: 4 of this application.
In view of Mourtada, Walensky, Clift, and GenBank, it would have been obvious to one of ordinary skill in the art before the effective filing date for the Fc domain of the peptide degron chimera of Mourtada modified according to Walensky and Clift to recruit the human TRIM21 of GenBank. One would have been motivated and would have expected success because Mourtada taught the subject to be treated is a human (p. 4, bottom), Clift teaches the TRIM21 is human TRIM21 (p. e4, bottom), and GenBank teaches the amino acid sequence of human TRIM21, which is identical to instant SEQ ID NO: 4.
Therefore, the engineered peptide of claim 13 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claims 1, 4-6, 11, and 12 are rejected under 35 U.S.C. 103 as being unpatentable over Mourtada in view of Chatterjee et al. (US 2022/0002700 A1 with priority to April 3, 2020; cited on Form PTO-892 mailed on June 2, 2023; hereafter “Chatterjee-2”) and Clift.
Regarding instant claim 1, Mourtada teaches peptide degron chimeras that act as protein degradation-inducing moieties and teaches the peptide degron chimeras include combining a peptide that binds and recruits a degrader protein with a peptide, which is incorporated for targeting a disease-related protein (p. 19, first full paragraph). Mourtada teaches the degrader protein is an E3 ubiquitin ligase (p. 27, first full paragraph). Mourtada teaches the targeted proteins can be of viral origin and are involved in or that are causative of disease and the chimeras are useful for treating diseases driven by such pathologic proteins (p. 2, first full paragraph).
Mourtada does not teach or suggest the claim 1 limitation “the targeting domain comprise the amino acid sequence of SEQ ID NO: 1.”
Chatterjee-2 teaches sACE2-derived peptide variants that bind to the SARS-CoV-associated spike (S) protein (paragraph [0002]) including sACE2 peptide variant 2 (SEQ ID NO: 2 of Chatterjee-2). SEQ ID NO: 2 of Chatterjee-2 comprises the amino acid sequence of SEQ ID NO: 1 of this application.
In view of the combined teachings of Mourtada and Chatterjee-2, it would have been obvious to one of ordinary skill in the art before the effective filing date to use the sACE2 peptide variant 2 of Chatterjee-2 as the targeting peptide of the peptide degron chimera of Mourtada. One would have been motivated and would have expected success because Mourtada taught a peptide degron chimera including a peptide for targeting a viral disease-related protein and Chatterjee-2 teaches a peptide that targets a viral disease-related protein.
Mourtada also does not teach or suggest the claim 1 limitation “the ubiquitin ligase recruiting domain comprises an Fc domain.”
Clift teaches that antibody-bound pathogens can be recognized by the E3 ubiquitin ligase TRIM21, which binds with high affinity to the Fc domain of antibodies (p. 1692, column 2, bottom). Clift teaches that during infection, TRIM21 recruits the ubiquitin-proteasome system to antibody-bound pathogens, leading to their destruction (p. 1692, column 2, bottom). Clift teaches a fusion protein comprising an Fc domain fused to the C-terminus of a nanobody (Figure 2(I); p. e5, top) for degradation of the protein targeted by the nanobody (paragraph bridging pp. 1692-1693; p. 1694, column 2, middle).
In view of the combined teachings of Mourtada and Clift, it would have been obvious to one of ordinary skill in the art before the effective filing date to use the Fc domain of Clift as the peptide that binds and recruits a degrader protein in the peptide degron chimera of Mourtada. One would have been motivated and would have expected success to do so because Mourtada taught a peptide degron chimera comprising a peptide that binds and recruits an E3 ubiquitin ligase for degradation of the targeted protein, and Clift taught an Fc domain fused to a peptide targeting domain (a nanobody) to recruit an E3 ubiquitin ligase (TRIM21) for degradation of the targeted protein.
The combination of Mourtada, Chatterjee-2, and Clift does not teach or suggest the peptide degron chimera of Mourtada modified according to Chatterjee-2 and Clift as described above comprises “an endogenous human protein.” However, in view of the indefiniteness of “an endogenous human protein” in the context of claim 1 and because the structure of the peptide degron chimera of Mourtada modified according to Chatterjee-2 and Clift is substantially identical to the structure recited in claim 1, the peptide degron chimera of Mourtada modified according to Chatterjee-2 and Clift is considered to satisfy the limitation of “an endogenous human protein” in claim 1.
Regarding instant claims 4-6, the combination of Mourtada, Chatterjee-2, and Clift does not teach or suggest the S protein of SARS-CoV-2 is part of a SARS-CoV-2 viral envelope. However, given that the S protein of SARS-CoV-2 is inherently part of the viral envelope of SARS-CoV-2 and the sACE2 peptide variant 2 of Chatterjee-2 targets the S protein of SARS-CoV-2 A (paragraph [0002] of Chatterjee-2), the sACE2 peptide variant 2 of Chatterjee-2 necessarily targets the S protein of the viral envelope of SARS-CoV-2.
Regarding instant claim 11, Clift teaches the Fc domain is fused to the C-terminus of the nanobody (Figure 2(I); p. e5, top).
Regarding instant claim 12, Mourtada teaches the degrader protein that is recruited by the peptide degron chimera is an E3 ubiquitin ligase (p. 27, first full paragraph) and Clift teaches the Fc domain binds to the E3 ubiquitin ligase TRIM21 (p. 1692, column 2, bottom).
Therefore, the engineered peptide of claims 1, 4-6, 11, and 12 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claim 13 is rejected under 35 U.S.C. 103 as being unpatentable over Mourtada in view of Chatterjee-2 and Clift as applied to claims 1, 4-6, 11, and 12 above, and further in view of GenBank.
The relevant teachings of Mourtada, Chatterjee-2, and Clift as applied to claims 1, 4-6, 11, and 12 are set forth above.
The combination of Mourtada, Chatterjee-2, and Clift does not teach or suggest the amino acid sequence of TRIM21 is SEQ ID NO: 4.
The reference of GenBank teaches the amino acid sequence of human TRIM21 (p. 3), which is identical to SEQ ID NO: 4 of this application.
In view of Mourtada, Chatterjee-2, Clift, and GenBank, it would have been obvious to one of ordinary skill in the art before the effective filing date for the Fc domain of the peptide degron chimera of Mourtada modified according to Walensky and Clift to recruit the human TRIM21 of GenBank. One would have been motivated and would have expected success because Mourtada taught the subject to be treated is a human (p. 4, bottom), Clift teaches the TRIM21 is human TRIM21 (p. e4, bottom), and GenBank teaches the amino acid sequence of human TRIM21, which is identical to instant SEQ ID NO: 4.
Therefore, the engineered peptide of claim 13 would have been obvious to one of ordinary skill in the art before the effective filing date.
RESPONSE TO REMARKS: Applicant argues the rejections are obviated by amendment to claim 1 because Mourtada teaches stapled peptides and does not teach or suggest an “endogenous human protein.”
Applicant’s arguments are not found persuasive. There is no dispute that the combination of cited prior art does not teach or suggest the peptide degron chimera of the combination of Mourtada, Walensky and Clift or the combination of Mourtada, Chatterjee-2, and Clift comprises “an endogenous human protein.” However, as stated above, according to the instant specification, the claimed engineered peptide is a man-made fusion of the peptide of SEQ ID NO: 1, which is the sequence of a peptide fragment derived from soluble angiotensin converting enzyme 2 (paragraph [0044], Table 1) and an Fc domain, which is an antibody recognition domain (paragraph [0007]), and given that these components are derived from distinct proteins and are fused together by the hand of man, one of ordinary skill in the art would have recognized that there is no “endogenous human protein” that includes the sequence of SEQ ID NO: 1 and an Fc domain. In view of the indefiniteness of “an endogenous human protein” in the context of claim 1 and because the structure of the peptide degron chimera of Mourtada modified according to Chatterjee-2 and Clift is substantially identical to the structure recited in claim 1, the peptide degron chimera of Mourtada modified according to Chatterjee-2 and Clift is considered to satisfy the limitation of “an endogenous human protein” in claim 1.
For these reasons, it is the examiner’s position that the claimed invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date.
Conclusion
Status of the claims:
Claims 1, 4-6, 11-15, and 21-28 are pending.
Claims 14, 15, and 21-28 are withdrawn from consideration.
Claims 1, 4-6, and 11-13 are rejected.
No claim is in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
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/David Steadman/Primary Examiner, Art Unit 1656
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