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 Application, Amendments and/or Claims
The amendment of 27 April 2026 has been entered in full. Claims 24, 32-35, 38, and 39 are amended. Claims 1-23, 25-27, and 31 are cancelled. Claims 40-44 are added.
Claims 24, 28-30, and 32-44 are under consideration in the instant application.
Drawings
The replacement drawings were received on 29 April 2026. These drawings are acceptable.
Withdrawn Objections and/or Rejections
1. The objection to the drawings as set forth at pages 3-4 of the previous Office Action of 27 January 2026 is withdrawn in view of the replacement drawings filed on 29 April 2026.
2. The Sequence Listing Requirement deficiency set forth at pages 4-7 of the previous Office Action of 27 January 2026 is withdrawn in view of Applicant’s amendment to the instant specification (27 April 2026).
3. The objection to the specification as set forth page 7 of the previous Office Action of 27 January 2026 is withdrawn in view of Applicant’s persuasive argument (27 April 2026). Specifically, the Brief Description of the Drawings refers to Figure 16I in the originally specification at page 13, line 24 and page 14, line 10.
4. The objections to claims 30, 32, and 35-39 as set forth at pages 7-9 of the previous Office Action of 27 January 2026 are withdrawn in view of the amended claims and Applicant’s persuasive arguments (27 April 2026).
5. The rejection of claims 33-35 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph as set forth at page 9 of the previous Office Action of 27 January 2026 is withdrawn in view of the amended claims (27 April 2026).
Maintained 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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
Written Description
6. Claims 24, 28, 29, 32-35, and 40-44 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, 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. The basis for this rejection is set forth for claims 24, 28, 29, and 32-35 at pages 9-16 of the previous Office Action of 27 January 2026.
Amended claim 24 is directed to a fusion protein comprising interleukin-1 receptor antagonist (IL-1Ra) and an extracellular matrix (ECM) binding peptide which specifically binds to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate, wherein the ECM binding peptide comprises a peptide from amphiregulin (AREG) comprising the amino acid sequence provided as SEQ ID NO: 2 or conservative variant thereof, wherein the sequence of the conservative variant only differs from SEQ ID NO: 2 in at least one amino acid substitution selected from the group consisting of:
(a) substitution of an aliphatic amino acid G with another aliphatic amino acid selected from a group consisting of A, L, I, and V or with an aromatic amino acid selected from a group consisting of F, Y, and W;
(b) substitution of a basic amino acid selected from the group consisting of R and K with another basic amino acid selected from a group consisting of R, K, and H; and
(c) substitution of an acidic or amide amino acid N with another acidic or amide amino acid selected from a group consisting of D, E, N, and Q.
New claims 40 and 41 recite that the conservative variant has at least 80% amino acid sequence identity with SEQ ID NO: 2.
(i) At page 9 of the Response of 27 April 2026, Applicant states that without acquiescing to the sufficiency of the rejection, and solely to advance prosecution, claim 24 has been amended to specify the conservative variant (see underlined claim limitations above). Applicant submits that amended claim 24 now specifically defines the scope of the claimed variants by reciting particular conservative amino acid substitutions, each of which is described and supported in the specification. Applicant argues that one of ordinary skill in the art reasonably would have understood, based on the disclosure of the specification, that Applicant was in possession of the claimed invention.
Applicant’s amendment and arguments have been fully considered but are not found to be persuasive. At the outset, the amino acid sequence of SEQ ID NO: 2 (RKKKGGKNGKNRR) is 13 amino acids in length. Amended claim 24 now recites that the ECM binding peptide comprises a peptide from AREG “comprising the amino acid sequence provided as SEQ ID NO: 2 or a conservative variant thereof, wherein the sequence of the conservative variant only differs from SEQ ID NO: 2 in at least one amino acid substitution selected from the group consisting of…”. Thus, there is no limit as to how many amino acids are substituted in a conservative variant—one amino acid up to all thirteen amino acids could be substituted.
Second, the remainder of claim 24 recites that the least one amino acid substitution is selected from the group consisting of:
(a) substitution of an aliphatic amino acid G with another aliphatic amino acid selected from a group consisting of A, L, I, and V or with an aromatic amino acid selected from a group consisting of F, Y, and W;
(b) substitution of a basic amino acid selected from the group consisting of R and K with another basic amino acid selected from a group consisting of R, K, and H; and
(c) substitution of an acidic or amide amino acid N with another acidic or amide amino acid selected from a group consisting of D, E, N, and Q.
There is no requirement as to which specific amino acid positions are substituted (i.e., a specific G, R, K, or N). The amino acid sequence of SEQ ID NO: 2 is only composed of RKKKGGKNGKNRR, so the new limitations of claim 24(a)-(c) encompass that all possible amino acids within the peptide may be substituted with any combination of the recited conservative amino acids.
However, Applicant is reminded that the instant specification does not teach any peptide variants (conservative or otherwise) of the amphiregulin (AREG) amino acid sequence of SEQ ID NO: 2.
There is no identification of any particular sequence or structure of the AREG peptide comprising the amino acid sequence of SEQ ID NO: 2 that must be conserved in order to provide the required function of binding to one or more extracellular matrix proteins. Thus, the claims are still drawn to a genus of fusion proteins comprising a genus of conservative peptide variants of the AREG amino acid sequence of SEQ ID NO: 2.
The instant specification fails to disclose and there is no art-recognized correlation between the structure of peptide variants of the AREG amino acid sequence of SEQ ID NO: 2 and the function of binding to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate. In other words, the specification does not teach the structure which results in a peptide variant of the AREG amino acid sequence of SEQ ID NO: 2 with the required characteristics. The description of the AREG amino acid sequence of SEQ ID NO: 2 is not adequate written description of an entire genus of conservative variants of the amino acid sequence of SEQ ID NO: 2 (as recited in amended claim 24) that bind to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate. There is little guidance in the specification indicating which amino acids are considered essential for the required biological activity of the AREG peptide amino acid sequence of SEQ ID NO: 2 of the instant claims. Furthermore, as discussed in the previous Office Action of 27 January 2026, the state of the art recognizes that protein function cannot be predicted from structure alone (see Bork, Skolnick et al., Doerks et al., Smith et al., Brenner, Bork et al., Tokuriki et al., Fenton et al., Bhattacharya et al., Guo et al.).
Applicant is reminded that generally, in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus (Enzo Biochem, Inc. v. Gen-Probe Inc., 323 F.3d 956 (Fed. Cir. 2002); Noelle v. Lederman, 355 F.3d 1343 (Fed. Cir. 2004); Regents of the University of California v. Eli Lilly Co., 119 F.3d 1559 (Fed. Cir. 1997)). A patentee must disclose “a representative number of species within the scope of the genus of structural features common to the members of the genus so that one of skill in the art can visualize or recognize the member of the genus” (see Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017) at page 1358). An adequate written description must contain enough information about the actual makeup of the claimed products – “a precise definition, such as structure, formula, chemic name, physical properties of other properties, of species falling with the genus sufficient to distinguish the gene from other materials”, which may be present in “functional terminology when the art has established a correlation between structure and function” (Amgen page 1361). A “mere wish or plan” to obtain the claimed invention is not sufficient (Centocor Orth Biotech, Inc. v. Abbott Labs, 636 F.3d 1341 (Fed. Cir. 2011); Regents of the Univ. of California, 119 F.3d at 1566).
In the instant application, the skilled artisan cannot envision the detailed chemical structure of the conservative peptide variants of the AREG amino acid sequence of SEQ ID NO: 2 that are biologically active of the encompassed claims, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The specific protein or variant thereof is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
Therefore, only a peptide from AREG comprising the amino acid sequence of SEQ ID NO: 2, but not the full breadth of the claims meets the written description provision of 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115). See also Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1355 (Fed. Cir. 2010).
Scope of Enablement
7. Claims 24, 28, 29, 32-35, and 40-44 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a fusion protein comprising IL-1Ra and an ECM binding peptide which specifically binds to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate, wherein the ECM binding peptide comprises a peptide from amphiregulin (AREG) comprising the amino acid sequence provided as SEQ ID NO: 2, does not reasonably provide enablement for a fusion protein comprising IL-1Ra and an ECM binding peptide which specifically binds to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate, wherein the ECM binding peptide comprises a peptide from amphiregulin (AREG) comprising the amino acid sequence provided as SEQ ID NO: 2 or conservative variants thereof (as recited in amended claim 24). The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims. The basis for this rejection is set forth for claims 24, 28, 29, and 32-35 at pages 16-21 of the previous Office Action of 27 January 2026.
Amended claim 24 is directed to a fusion protein comprising interleukin-1 receptor antagonist (IL-1Ra) and an extracellular matrix (ECM) binding peptide which specifically binds to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate, wherein the ECM binding peptide comprises a peptide from amphiregulin (AREG) comprising the amino acid sequence provided as SEQ ID NO: 2 or conservative variant thereof, wherein the sequence of the conservative variant only differs from SEQ ID NO: 2 in at least one amino acid substitution selected from the group consisting:
(a) substitution of an aliphatic amino acid G with another aliphatic amino acid selected from a group consisting of A, L, I, and V or with an aromatic amino acid selected from a group consisting of F, Y, and W;
(b) substitution of a basic amino acid selected from the group consisting of R and K with another basic amino acid selected from a group consisting of R, K, and H; and
(c) substitution of an acidic or amide amino acid N with another acidic or amide amino acid selected from a group consisting of D, E, N, and Q.
New claims 40 and 41 recite that the conservative variant has at least 80% amino acid sequence identity with SEQ ID NO: 2.
(i) At page 10 of the Response of 27 April 2026, Applicant states that claim 24 now specifically defines the claimed variants by reciting particular conservative amino acid substitutions, each of which is described and supported in the specification (pages 24-26). Applicant argues that it was well within the knowledge of those of ordinary skill in the art to confirm that the conservative variants specifically bind to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate (including, e.g., by ELISA as disclosed in the examples in the specification). Applicant asserts that a person of ordinary skill in the art, in view of the disclosure, would have been able to make and use the claimed conservative variants without undue experimentation.
Applicant’s amendment and arguments have been fully considered but are not found to be persuasive. As discussed above under the Written Description rejection, the amino acid sequence of SEQ ID NO: 2 (RKKKGGKNGKNRR) is 13 amino acids in length. Amended claim 24 now recites that the ECM binding peptide comprises a peptide from AREG “comprising the amino acid sequence provided as SEQ ID NO: 2 or a conservative variant thereof, wherein the sequence of the conservative variant only differs from SEQ ID NO: 2 in at least one amino acid substitution selected from the group consisting of…”. Thus, there is no limit as to how many amino acids are substituted in a conservative variant—one amino acid up to all thirteen amino acids could be substituted.
Second, the remainder of claim 24 recites that the least one amino acid substitution is selected from the group consisting of:
(a) substitution of an aliphatic amino acid G with another aliphatic amino acid selected from a group consisting of A, L, I, and V or with an aromatic amino acid selected from a group consisting of F, Y, and W;
(b) substitution of a basic amino acid selected from the group consisting of R and K with another basic amino acid selected from a group consisting of R, K, and H; and
(c) substitution of an acidic or amide amino acid N with another acidic or amide amino acid selected from a group consisting of D, E, N, and Q.
There is no requirement as to which specific amino acid positions are substituted (i.e., a specific G, R, K, or N). The amino acid sequence of SEQ ID NO: 2 is only composed of RKKKGGKNGKNRR, so the new limitations of claim 24(a)-(c) encompass that all possible amino acids within the peptide may be substituted with any combination of the recited conservative amino acids.
However, Applicant is reminded that the instant specification does not teach any peptide variants (conservative or otherwise) of the amphiregulin (AREG) amino acid sequence of SEQ ID NO: 2.
Specifically, Applicant’s broad brush discussion of utilizing well-known techniques without undue experimentation to generate, screen, and use the claimed fusion protein comprising conservative peptide variants of the AREG amino acid sequence of SEQ ID NO: 2 does not constitute adequate guidance, but rather, constitutes an invitation to experiment. A single embodiment may provide broad enablement in cases involving predictable factors such as mechanical or electrical elements, but more will be required in cases that involve unpredictable factors such as most chemical reactions and physiological activity. See In re Vickers, 141 F.2d 522, 526-27, 61 USPQ 122, 127 (CCPA 1944); In re Cook, 439 F.2d 730, 734, 169 USPQ 298, 301 (CCPA 1971); In re Soll, 97 F.2d 623, 634, 38 USPQ 189, 191 (CCPA 1938; In re Fisher, 427 F.2d 833, 839, 166 USPQ 18, 24 (CCPA 1970); In re Wright, 999 F.2d 1557, 1562, 27 USPQ2d 1510, 1513 (Fed. Cir. 1993); In re Vaeck, 947 F.2d 488, 496, 20 USPQ2d 1438, 1445 (Fed. Cir. 1991). While the technology to generally produce and express proteins was available at the time the invention was made, the amount of experimentation required to generate fusion proteins comprising peptide variants of the AREG amino acid sequence of SEQ ID NO: 2 would not have been routine, much less could one of ordinary skill in the art predict that any combination of all the variants encompassed by the instant claims would result in a functional peptide (and overall functional fusion protein). Because of this lack of guidance in the instant specification, the extended experimentation that would be required to determine which amino acid sequences and modifications would be acceptable to retain occluding structural and functional activity, and the fact that the relationship between the sequence of a protein/peptide and its tertiary structure (i.e. its activity) are not well understood and are not predictable (see also Bork, Skolnick et al., Doerks et al., Smith et al., Brenner, Bork et al., Tokuriki et al., Fenton et al., Bhattacharya et al., Guo et al. cited at pages 19-20 of the previous Office Action), it would require an undue amount of experimentation for one of skill in the art to arrive at the large number of conservative peptide variants of the AREG amino acid sequence of SEQ ID NO: 2 of the encompassed claims. Applicant has not provided sufficient guidance to enable one of ordinary skill in the art to make and use the genus of peptide variants of the AREG amino acid sequence of SEQ ID NO: 2 in the claims in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement. See In re Fisher, 166 USPQ 19 24 (CCPA 1970).
Applicant is reminded that the courts have stated that patent protection is granted in return for an enabling disclosure, not for vague intimations of general ideas that may or may not be patentable. Tossing out the mere germ of an idea does not constitute an enabling disclosure. Reasonable detail must be provided in order to enable members of the public to understand and carry out the invention. See Genentech v. Novo Nordisk A/S (CAFC) 42 USPQ2d 1001 (1997).
Proper analysis of the Wands factors was provided in the previous Office Action. Due to the large quantity of experimentation necessary to generate conservative peptide variants of the AREG amino acid sequence of SEQ ID NO: 2 and screen such for the desired functional activity; the lack of direction/guidance presented in the specification regarding the same; the absence of working examples directed to the same; the complex nature of the invention; the state of the prior art which establishes the unpredictability of the effects of mutation on protein structure and function; and the breadth of the claims, undue experimentation would be required of the skilled artisan to make and/or use the claimed invention.
New Claim Rejections - 35 USC § 112(b)
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.
8. Claims 24, 28, 29, 32-35, and 40-44 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.
8a. Claims 24, 28, 29, 32-35, and 40-44 are rejected as being indefinite because claim 24, subpart (c) recites that the conservative variant differs in at least one amino acid “substitution of an acidic or amide amino acid N with another acidic or amide amino acid selected from the group consisting of D, E, N, and Q”. Claim 24, subpart (c) is confusing and unclear because in one alternative, amino acid N is to be substituted with the same exact amino acid N.
New Claim Rejections - 35 USC § 112(a)
9. Claims 24, 28-30, and 32-44 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, 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.
Amended claim 24 is directed to a fusion protein comprising interleukin-1 receptor antagonist (IL-1Ra) and an extracellular matrix (ECM) binding peptide which specifically binds to one or more extracellular matrix proteins selected from the group consisting of fibrinogen, fibronectin, vitronectin, tenascin C, and heparan sulfate, wherein the ECM binding peptide comprises a peptide from amphiregulin (AREG) comprising the amino acid sequence provided as SEQ ID NO: 2 or conservative variant thereof, wherein the sequence of the conservative variant only differs from SEQ ID NO: 2 in at least one amino acid substitution selected from the group consisting of:
(a) substitution of an aliphatic amino acid G with another aliphatic amino acid selected from a group consisting of A, L, I, and V or with an aromatic amino acid selected from a group consisting of F, Y, and W;
(b) substitution of a basic amino acid selected from the group consisting of R and K with another basic amino acid selected from a group consisting of R, K, and H; and
(c) substitution of an acidic or amide amino acid N with another acidic or amide amino acid selected from a group consisting of D, E, N, and Q.
The specification as originally filed does not provide adequate written description for “substitution of an aliphatic amino acid G… with an aromatic amino acid selected from a group consisting of F, Y, and W” (as recited in the alternative in claim 24, subpart (a)). The “substitution of an aliphatic amino acid G… with an aromatic amino acid selected from a group consisting of F, Y, and W” limitation as recited in claim 24, subpart (a) is not expressly asserted, nor does it flow naturally from the specification.
At the top of the Remarks section at page 7 of the Response of 27 April 2026, Applicant states that support for the amended claims may be found in the original claims, throughout the application as filed (Application No. PCT/AU2021/050598 (WO 2021/248203)), and at page 24, lines 5-9 and pages 25-26. However, upon the Examiner’s independent review of the specification, Figures, and originally filed claims, the originally filed specification of 12 December 2022 only teaches the following regarding conservative aliphatic/aromatic variant substitutions:
Conservative substitutions include those between the following classes of amino acid residues:
Aliphatic— G, A, L, I, V
Hydroxyl or sulfur containing— S, C, T, M
Aromatic— F, Y, W
Basic— R, K, H
Acidic and their amides— D, E, N, Q (see page 24, lines 5-7)
The specification clearly teaches that conservative substitutions are those between classes of amino acid residues. For example, glycine (G) is an aliphatic amino acid and according to the instant specification, can be substituted with other aliphatic amino acids A, L, I, and V. Similarly, the aromatic amino acids F, Y, and W, can be substituted with another aromatic.
However, glycine is not an aromatic amino acid. Therefore, the Examiner is unable to locate where the specification provides adequate written description for substitutions of amino acids across different classes as recited in amended claim 24, (i.e., “substitution of an aliphatic amino acid G… with an aromatic amino acid selected from a group consisting of F, Y, and W”).
Conclusion
Claims 24, 28-30, and 32-44 are rejected.
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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BEB
Art Unit 1647
25 June 2026
/BRIDGET E BUNNER/Primary Examiner, Art Unit 1647
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