DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 February 9, 2026 has been entered.
Claims 2, 3, 9, and 10 have been canceled.
Claims 1, 5, 8, and 12 have been amended.
Claims 1, 4-8, and 11-14 are pending in the instant application.
Claim Rejections - 35 USC § 112
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.
Claims 1, 4-8, and 11-14 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Applicant has broadly claimed methods of administering a genus of polypeptides comprising SEQ ID NO:2 or a variant containing only conservative amino acid substitutions of SEQ ID NO:2 for the purpose of treating thromboinflammation, with dependent claims defining disease species including atherosclerosis, myocardial infarction, stroke, and cerebral injuries as being among those present in the genus of thromboinflammation (see all pending claims, particularly 1, 5, 8, and 12). Notably, there is no limit placed upon the number of conservative substitutions relative to SEQ ID NO:2 that can be made, and since SEQ ID NO:2 is 67 residues in length, the claims reasonably encompass simultaneously mutating all 67 residues.
On page 20, the specification discloses that SEQ ID NO:2 is a mutated, non-naturally occurring variant of Ir-CPI/SEQ ID NO:1 wherein the asparagine at residue 54 of SEQ ID NO:1 is changed to glutamine to remove an N-linked glycosylation site. It should be noted that as per the exemplification found on page 10 of the instant specification, substituting a Q for an N is considered to be conservative in nature. The instant specification does not appear to disclose the synthesis of any sequence variants apart from the aforementioned SEQ ID NO:2 and thus the only disclosed members of the genus of polypeptides encompassed by the claimed administration methods appear to be those of SEQ ID NOs:1 and 2. Notably, all of the administrations performed as part of the working examples appear to use the Ir-CPI polypeptide, i.e. SEQ ID NO:1 of the instant application, and none of the working examples appear to pertain to the synthesis of “variants” (conservative or otherwise) of the polypeptide of SEQ ID NO:1.
As already stated, the claims encompass administering polypeptides that have 0% identity with SEQ ID NO:2 as every residue can be mutated via conservative substitution. However, such polypeptides are recited as comprising the function properties of treating thromboinflammation which arises due to the ability of Ir-CPI to bind to and inhibit the activity of coagulation factors XII, XI, and kallikrein (as is explicitly recited in dependent claims 4 and 11 for example). It is well known that many amino acid side chains can strongly alter the secondary structure of a polypeptide, such as prolines forming bends or kinks in a polypeptide backbone while cystines often form intra- and intermolecular disulfide bonds (Stryer, see entire document, of record). Notably, page 10 indicates that “nonpolar (hydrophobic)” amino acids include alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, and methionine while “polar neutral” amino acids include glycine, serine, threonine, cysteine, tyrosine, asparagine, and glutamine. Given the propensity of proline to bend secondary structure, it does not appear reasonable that artisans could substitute P for every A, L, I, V, F, W, and M residue and maintain activity, nor that every G, S, T, Y, N, and Q could be substituted to C and have activity maintained due to the ability for C to participate in disulfide bond formation. However, the claims encompass such scenarios as well as mixing and matching all sorts of conservative substitutions such that the amount of sequence identity with the reference sequence can be zero. Artisans would not reasonably accept that all such alterations can be made while maintaining functional activities including binding and inhibiting FXII, FXI, and kallikrein while also inhibiting thromboinflammation. Indeed, Attwood (Science 2000; 290:471-473, of record) teaches that “[i]t is presumptuous to make functional assignments merely on the basis of some degree of similarity between sequences”. Skolnick et al. teach that the skilled artisan is well aware that assigning functional activities for any particular protein or protein family based upon sequence homology is inaccurate, in part because of the multifunctional nature of proteins (e.g., "Abstract" and "Sequence based approaches to function prediction", page 34, of record). Even in situations where there is some confidence of a similar overall structure between two proteins, only experimental research can confirm the artisan's best guess as to the function of the structurally related protein (see in particular "Abstract" and Box 2).
Thus the genus of all variants of SEQ ID NO:2 which contain only conservative substitutions relative to SEQ ID NO:2 does not reasonably appear to be suitable for use in the claimed administration methods as all such members are not reasonably expected to have the necessary functional activities and determining which do and which do not forces the practitioner of the instant claimed methods to first engage in unpredictable basis science trial and error research and experimentation before even trying to perform the claimed therapeutic administration methods.
Therefore, in view of the breadth of the claimed invention, the teachings of the art and the guidance and direction of the instant specification, artisans would be unable to practice the full extent of the instant claimed methods as of the filing date of the instant claimed inventions.
Applicant's arguments filed February 9, 2026 have been fully considered but they are not persuasive. Applicant argues the claims have been narrowed such that the substitutions must be conservative in nature and that page 10 of the specification provides examples of what is encompassed by the term. Applicant further argues that the paragraph bridging pages 19 and 20 provides examples of how many mutations are present, specifically “Particularly preferred are variants in which several, 5-10, 1-5, or 1-2 amino acids are substituted, deleted, or added in any combination.” Applicant also asserts that any “variant” which does not have functional activity is simply not part of the claimed invention. As such applicant believes the rejection should be withdrawn.
These arguments are not persuasive. Applicant is reminded that it is inappropriate to add limitations form the specification to the claims unless such limitation are by way of definition. Page 10 states “Conservative amino acid substitution may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues involved.” (emphasis added by the examiner). May is not equivalent to “must” and 6 different criteria, alone or in unspecified combinations, can be used to decide what is or is not “conservative” based upon the guidance of the specification and thus it is clearly exemplification (and thus not limiting) as compared to a definition (which is limiting). Similarly a large number of mutations, including the unknown “several”, are set forth as being “particularly preferred” and thus again are examples of what is encompassed rather than limiting what actually is being claimed. Thus, such exemplification does not in any way preclude an artisan from conservatively substituting all 67 residues of SEQ ID NO:2, and as such the pending claims reasonably are broader in scope presently as compared to when blanket percent identity limitations were recited. Further, conservative substitutions can often alter function as can readily be seen in the studies of Gencic et al. who identified a valine to alanine mutation in PLP that strongly impacted myelin formation (see entire document). Applicant is reminded that the quid pro quo for the monopoly rights granted by a patent are teaching the world how to make and use that which is presently claimed. Claiming a vast genus of molecules and then simply stating that any which don’t work aren’t part of the invention does not reasonably indicate to artisans how to make and use what has been claimed without undue experimentation as there is no guidance or direction concerning where within the 67 residues of SEQ ID NO:2 change is reasonably possible apart from the single conservative point mutation that changes the naturally occurring tick polypeptide of SEQ ID NO:1 into SEQ ID NO:2. Therefore, the unlimited and untargeted “conservative” substitution mutagenesis as encompassed by the instant claims is not reasonably expected to yield polypeptide sequences which maintain physiological activity in the absence of conducting additional unpredictable basic science research and experimentation.
The rejection is maintained.
Claims 1, 4-8, and 11-14 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.
Methods of reducing thromboinflammation by administering a genus of polypeptides encompassing SEQ ID NO:2 as well as polypeptides consisting of conservative amino acid substitutions of SEQ ID NO:2. The claims do not place any limitation upon the number of such conservative substitutions that may be made, and thus the claim encompasses polypeptides in which all 67 residues of SEQ ID NO:2 are mutated to a conservative residue (i.e. 0% percent identity with the reference sequence, which in the present context is SEQ ID NO:2). Conservative mutations are exemplified, but not limitingly defined, on page 10 of the specification filed 6/6/2025. To support such a genus, applicant discloses that the naturally occurring tick protein Ir-CPI (aka SEQ ID NO:1) can be mutated such that the N at position 54 is substituted to Q so as to prevent N-linked glycosylation (see page 20 of the specification). No data or working examples concerning the synthesis of variants of Ir-CPI appear to be disclosed in the instant specification.
The guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, § 1 "Written Description" Requirement make clear that if a claimed genus does not show actual reduction to practice for a representative number of species, then the Requirement may be alternatively met by reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the genus. See MPEP 2163. In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted: “A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin [e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate."). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.” The court has further stated that “Adequate written description requires a precise definition, such as by structure, formula, chemical name or physical properties, not a mere wish or plan for obtaining the claimed chemical invention.” Id. at 1566, 43 USPQ2d at 1404 (quoting Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606). Also see Enzo-Biochem v. Gen-Probe 01-1230 (CAFC 2002). Further, courts have long ruled that “When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.” See Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005). Also, “A sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can "visualize or recognize" the members of the genus.” See AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69.
In the instant application, applicant is claiming methods of administering “variants” of SEQ ID NO:2, which itself is a conservative variant of the naturally occurring tick polypeptide of SEQ ID NO:1/Ir-CPI which lack N-linked glycosylation found in the natural product. None of the working examples disclose generation of such variants, and even the disclosed administrations of the working examples appear to use the polypeptide of SEQ ID NO:1 rather than that of SEQ ID NO:2. All claims recite that the administered “variants” have the function of treating thromboinflammation, and the specification discloses that the mechanism of action by which this occurs is through binding to activated coagulation factors FXIIa, FXIa, and kallikrein (see most particularly dependent claims 4 and 11). There is no data indicating that “variants” maintain these functional activities, even including SEQ ID NO:2 itself. As presently constructed, variants wherein all 67 residues of SEQ ID NO:2 are changed to a “conservative” substitution are encompassed by the claimed therapeutic administration methods.
Loss of functional activity subsequent to mutagenesis is common, and indeed the art has long taught that assigning functional activities for any particular protein or protein family based upon sequence homology is inaccurate, in part because of the multifunctional nature of proteins (Skolnick et al, see entire document, particularly the Abstract and the section titled Sequence-based approaches to function prediction on page 34, of record). Even in situations where there is some confidence of a similar overall structure between two sequences, only experimental research can confirm the artisan's best guess as to the function of the structurally related sequence (see in particular the Abstract and Box 2 on page 36). It is also known that the complexity of the problem of assigning function based on homology rises as the percent similarity or identity falls (see Whisstock et al., Quarterly Reviews of Biophysics, 2003, 36:307-340, particularly the sentence that spans pages 321 and 323). As already stated, the claims encompass administering polypeptides that have 0% identity with SEQ ID NO:2 as every residue can be mutated via conservative substitution. However, such polypeptides are recited as comprising the function properties of treating thromboinflammation which arises due to the ability of Ir-CPI to bind to and inhibit the activity of coagulation factors XII, XI, and kallikrein (as is explicitly recited in dependent claims 4 and 11 for example). It is well known that many amino acid side chains can strongly alter the secondary structure of a polypeptide, such as prolines forming bends or kinks in a polypeptide backbone while cystines often form intra- and intermolecular disulfide bonds (Stryer, see entire document, of record). Notably, page 10 indicates that “nonpolar (hydrophobic)” amino acids include alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, and methionine while “polar neutral” amino acids include glycine, serine, threonine, cysteine, tyrosine, asparagine, and glutamine. Given the propensity of proline to bend secondary structure, it does not appear reasonable substituting P for every A, L, I, V, F, W, and M residue will maintain sufficient structure to allow for functional activity, nor does it appear reasonable that every G, S, T, Y, N, and Q can be substituted to C and have activity maintained due to the ability for C to participate in disulfide bond formation which profoundly alters structure. Notably, the claims encompass just such scenarios wherein structure is strongly non-conserved even though functional activity must be maintained. Artisans would not reasonably accept that all such alterations can be made while maintaining functional activities including binding and inhibiting FXII, FXI, and kallikrein while also inhibiting thromboinflammation, and no members lying within the recited genus apart from SEQ ID NO:1 appear to have data disclosed demonstrating the presence of such activities. Indeed, Attwood (Science 2000; 290:471-473, of record) teaches that “[i]t is presumptuous to make functional assignments merely on the basis of some degree of similarity between sequences”. Skolnick et al. teach that the skilled artisan is well aware that assigning functional activities for any particular protein or protein family based upon sequence homology is inaccurate, in part because of the multifunctional nature of proteins (e.g., "Abstract" and "Sequence based approaches to function prediction", page 34, of record). Even in situations where there is some confidence of a similar overall structure between two proteins, only experimental research can confirm the artisan's best guess as to the function of the structurally related protein (see in particular "Abstract" and Box 2). Further, conservative substitutions can often alter function as can readily be seen in the studies of Gencic et al. who identified a single valine to alanine mutation in PLP that strongly impacted myelin formation (see entire document).
In view of all of the above, there does not appear to be reasonable correlation between the recited conservative “variants” and the functional activities of inhibiting thromboinflammation via binding to FXIIa, FXIa, and kallikrein. As such artisans would reasonably conclude that applicant was not is possession of the full breadth of the claimed administration methods ate the time of filing.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 4-8, and 11-14 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Godfroid et al. (EP2123670, of record).
Godfroid et al. disclose the administration of a polypeptide isolated from tick salivary glands that is a 100% match to instant SEQ ID NO:1, and differs from instant SEQ ID NO:2 by a single Q to N mutation at position 54 of instant SEQ ID NO:2 (see enclosed sequence alignment). As indicated on page 10 of the instant specification a Q (glutamine) to N (asparagine) substitution is considered to be “conservative”. Such administrations are disclosed as being performed to treat disorders including thromboembolism, stroke, myocardial infarction, cerebrovascular diseases, cerebral ischemia, pulmonary embolism, renal vein thrombosis and hepatic vein thrombosis (see entire document, particularly the abstract, claims, paragraphs [0015-0029]). Notably, the polypeptide of Godfroid et al. is characterized as binding to factors XII, XI, and kallikrein, is referred to as “Ir-CPI”, and is present in pharmaceutical compositions (see particularly paragraphs [0026], [0027], [0031] and examples 4-6). Therefore the prior art anticipates the instant claimed invention.
Applicant's arguments filed February 9, 2026 have been fully considered but they are not persuasive. Applicant argues that claims 2 and 9 in the prior claim set were limited to the polypeptide of SEQ ID NO:2 and that since those claims were not rejected applicant amended the instant independent claims to recite “SEQ ID NO:2 or conservative variations thereof”.
This argument is not persuasive. While Godfroid do not teach the exact polypeptide of instant SEQ ID NO:2 they very much teach a polypeptide which is a conservative substitution mutant of instant SEQ ID NO:2. The rejection is maintained.
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, 4-8, and 11-14 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 11,897,924 in view of Godfroid et al. (EP2123670, of record).
The issued claims recite pharmaceutical compositions comprising fusion proteins comprising polypeptides identical to SEQ ID NOs: 1 and 2 of the instant application and their administration to treat thrombi present in a subject (see all issued claims, and note that SEQ ID NOs:1 and 2 are identical when comparing the instant and issued claims while SEQ ID NOs: 31 and 37-39 for example from the issued claims comprise SEQ ID NO:2). Such claims differ from the instant claimed invention in that the issued claim do not recite any specific condition or disease that is associated with thrombus formation which is being treated by administration of the pharmaceutical compassions comprising Ir-CPI fusion proteins.
Godfroid et al. disclose the administration of a polypeptide isolated from tick salivary glands that is a 100% match to instant SEQ ID NO:1 (and thus is more than 85% identical to instant SEQ ID NO:2) for the purpose of treating disorders including thromboembolism, strike, myocardial infarction, cerebrovascular diseases, cerebral ischemia, pulmonary embolism, renal vein thrombosis and hepatic vein thrombosis (see entire document, particularly the abstract, claims, paragraphs [0015-0029] and the enclosed sequence alignments). Notably, the polypeptide of SEQ ID NO:1 is characterized as binding to factors XII, XI, and kallikrein, is referred to as “Ir-CPI”, and is present in pharmaceutical compositions (see particularly paragraphs [0026], [0027], [0031] and examples 4-6).
Therefore it would have been obvious to a person of ordinary skill in the art at the time of filling to practice the administration methods of the issued claims upon patient populations identified by Godfroid et al. which include thromboembolism, strike, myocardial infarction, cerebrovascular diseases, cerebral ischemia, pulmonary embolism, renal vein thrombosis and hepatic vein thrombosis. This is because all of the conditions taught by Godfroid et al. involve thrombi, and because the polypeptides disclosed by Godfroid ate subcomponents of the fusion proteins administered by the issued claims. Given such strong structural identify when comparing the “Ir-CPI” compositions of Godfroid and the issued claims, as well as all of the specific disorders disclosed by Godfroid et al. being members encompassed by the larger genus of “thrombus” as recited in the issued claims, artisans would enjoy a more than reasonable expectation of success in making such alterations.
Applicant's arguments filed February 9, 2026 have been fully considered but they are not persuasive. Applicant argues the claims have been narrowed and therefore the double patenting rejections should be withdrawn.
This argument is not persuasive. Previously claims limited to administering SEQ ID NO:2 were rejected and applicant’s amendments to recite that the administered polypeptide is SEQ ID NO:2 or a conservative substitution variant thereof makes all claims under consideration broader in scope than that which was previously rejected. Thus, applicant’s claim amendments fail to establish a line of patentable distinctiveness between that which is presently claimed and that which was previously issued.
Claims 1, 4-8, and 11-14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 19/194,323. Although the claims at issue are not identical, they are not patentably distinct from each other because the copending claims anticipate that which is presently claimed.
Specifically, the copending claims recite pharmaceutical compositions comprising a polypeptide identical to instant SEQ ID NO:2 in combination with pharmaceutically acceptable excipients as well as methods of administering such compositions to treat thromboinflammation and other conditions including atherosclerosis, ischemic stroke, and cerebral injuries (see all copending claims, most particularly 1, 13, and 17-20, as well as the enclosed sequence alignments). Note that the copending claims either structurally constrain and/or explicitly name the excipient preset in the administered pharmaceutical compositions and thus the copending claims necessarily are narrower in scope than that which is presently claimed.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Applicant's arguments filed February 9, 2026 have been fully considered but they are not persuasive. Applicant argues the claims have been narrowed and therefore the double patenting rejections should be withdrawn.
This argument is not persuasive. Previously claims limited to administering SEQ ID NO:2 were provisionally rejected and applicant’s amendments to recite that the administered polypeptide is SEQ ID NO:2 or a conservative substitution variant thereof makes all claims under consideration broader in scope than that which was previously rejected. Thus, applicant’s claim amendments fail to establish a line of patentable distinctiveness between the instant and copending inventions.
Claims 1, 4-8, and 11-14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14 of copending Application No. 18/394,080. Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are obvious variants of the copending claims
Specifically, the copending claims recite treating thromboinflammation by administering the polypeptides of SEQ ID NOs:1 and 2 (see all copending claims, particularly claims 2 and 3). Note that application 18/394,080 is the parent of the instant application and thus all of the sequences are identical among the applications. Copending claims 4-14 are identical to instant claims 4-14. Note that the copending claims explicitly recite administering the polypeptide of SEQ ID NO:2 which is narrower in scope than the presently recited SEQ ID NO:2 or conservative substitution variants thereof. Also, as discussed earlier in this office action SEQ ID NO:1 is a specifically defined conservative substitution variant of SEQ ID NO:2 (i.e. Q54N substitution). Thus the species recited in the copending application methods anticipate the breadth of polypeptides administered by the instant claimed methods.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Applicant's arguments filed February 9, 2026 have been fully considered but they are not persuasive. Applicant argues the claims have been narrowed and therefore the double patenting rejections should be withdrawn.
This argument is not persuasive. Previously claims limited to administering SEQ ID NO:2 were provisionally rejected and applicant’s amendments to recite that the administered polypeptide is SEQ ID NO:2 or a conservative substitution variant thereof makes all claims under consideration broader in scope than that which was previously rejected. Also note that the copending claims recite administering the polypeptide of SEQ ID NO:1 which is a conservative substitution variant of SEQ ID NO:2 Thus, applicant’s claim amendments fail to establish a line of patentable distinctiveness between the instant and copending inventions.
The provisional rejection of claims 2 and 3 rejected under 35 U.S.C. 101 as claiming the same invention as that of claims 2 and 3 of copending Application No. 18/394,080 has been withdrawn in view of the claim amendments in the instant application received as part of the February 9, 2026 response.
No claims are allowable.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Michael Szperka whose telephone number is (571)272-2934. The examiner can normally be reached Monday-Friday 8:30-5:00.
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Michael Szperka
Primary Examiner
Art Unit 1641
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641