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 .
Applicant’s response and amendments received January 28, 2026 are acknowledged.
Claims 1 and 2 have been amended.
Claims 1-12 are pending in the instant application.
Claims 9-12 stand withdrawn from consideration as being drawn to a nonelected invention. See 37 CFR 1.142(b) and MPEP § 821.03, for reasons of record set forth in the restriction requirement mailed May 14, 2025.
Claims 1-8 are under examination in this office action.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
The rejection of claims 1-8 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, has been withdrawn in view of applicant’s claim amendments received January 28, 2026.
Claims 1-8 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.
Claims 1-8 contain the trademark/trade name “NANOBODY”. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name is used to identify/describe a particular type of single domain VHH obtained from a camelid and, accordingly, the identification/description is indefinite. Note that the term "nanobody" is an active, registered trademark of Ablynx N.V. The term is registered as a standard character mark without any particular claim to font size, size, or color (see USPTO Trademark Status attached). In other words, the standard character mark protects the name regardless of how the words are displayed (e.g. lowercase) (see Riddle, Charles. "What are the Differences Between Standard Character Marks and Design Marks?" Esquire Trademarks, 27 May 2020, https://esquiretrademarks.com/standard-character-mark-design-mark/).
Appropriate correction is required.
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, 3, 5, and 7 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.
Applicant has claimed antibodies that have the functional property of binding to the activation peptide of blood coagulation factor X , such binding making factor X more susceptible to proteolysis by factor IXa, and of comprising at least 90% sequence identity to the nanobodies of SEQ ID NOs: 8 or 10. It should be pointed out that it well accepted in the art that in the coagulation pathway, activated FIX (i.e. FIXa) is an enzyme that cleaves FX to FXa. See also page 7 of the instant specification. Dependent claims add further functional limitations, such as how tightly it binds. To support such breadth, the specification discloses generating VHH from a llama and an alpaca immunized with factor X (see page 38 of the specification). No data concerning mutagenesis of lead antibody clones appears to be disclosed in the specification as filed.
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). Recent court cases have emphasized the need for correlation between a well-defined structure and recited functional limitations. For example, the courts have indicated that recitation of an antibody which has specific functional properties in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See for example AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014) as well as Amgen v. Sanofi, (Fed Cir, 2017-1480. 10/5/2017). Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e. the antigen, as knowledge of the chemical structure of an antigen does not give the required kind of structure-identifying information about the corresponding antibodies, with the antibody-antigen relationship be analogized as a search for a key on a ring with a million keys on it. As such, knowledge of where an antibody binds provides no information as to what such an antibody necessarily looks like (i.e. its primary amino acid structure). Applicant is reminded that the courts have long ruled that “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. As such, disclosure of a screening assay to test for functional properties of an antibody (such as the epitope to which a test antibody binds or the fact that it does or does not inhibit some enzymatic process) does not provide evidence of possession of the antibody itself.
It should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway et al., see entire selection). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff et al., see entire document, particularly the abstract and the middle of the left column of page 1982). Thus, based upon the prior art, skilled artisans would reasonably understand that it is the structure of the CDRs within an antibody which gives rise to the functional property of antigen binding, the epitope to which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves.
In Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017), relying upon Ariad Pharms., Inc. v. Eli Lily & Co., 94 USPQ2d 1161 (Fed Cir. 2010), the following is noted. To show invention, a patentee must convey in its disclosure that is “had possession of the claimed subject matter as of the filing date. Demonstrating possession “requires a precise definition” of the invention. To provide this precise definition” for a claim to a genus, 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 at page 1358). Further, 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). Indeed, the 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. It should also be noted that the USPTO has released a Memo on the Clarification of Written Description Guidance For Claims Drawn to Antibodies and Status of 2008 Training Materials, 02/22/2018. See https://www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf. This Memo clarifies the applicability of USPTO guidance regarding the written description requirement of 35 U.S.C. § 112(a) concerning the written description requirement for claims drawn to antibodies and states: “In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional”. Further, the courts have indicated that the enablement and written description requirements of 35 USC 112 are separable as can be seen in for example Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111.
The above is true because knowledge of a given antigen (such as human factor X) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well, see entire document). Similarly, Lloyd et al. teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (see entire document). As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen as there does not appear to be any common or core structure present within all antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound in a population of antibodies that bind to a given antigen no number of species appears to be reasonably representative of the breadth of the genus of antibodies that bind the given antigen.
The antibodies presently claimed are not conventional antibodies that have six CDRs, and instead read upon immunoglobulin single variable domains, a class of antibodies typically derived from camelid heavy chain antibodies (VHH) which are distinct in that they comprise only a single polypeptide chain, and thus only have 3 CDRs which are responsible for antigen binding (see for example pages 11-13 of the instant specification). However, the majority of antigen contacts for such VHH are still found within the CDRs (Ghahroudi et al., see entire document).
All claims presently under examination in some way require the claimed VHH to have at least 90% sequence identity to either SEQ ID NO:8 or SEQ ID NO:10, both of which are specific nanobodies isolated and described in the working examples. Independent claim 1 requires the VHH to be “at least 90%” identical to SEQ ID NO:8 or 10, and notably neither claim 1 nor any of its dependent claims indicate where such sequence changes can occur. As such the changes in sequence relative to the recited reference SEQ ID numbers reasonably can occur within the CDR sequences, the very structure recognized in the art as giving rise to the functional property of antigen binding. As previously mentioned, no mutagenesis data concerning the VHH isolated from immunized camelids appears to have been disclosed. It should be noted that the complete sequence of SEQ ID NO:10/Nb 702C12 is disclosed on page 5 wherein the three CDR sequences are underlined, and that CDR1 is 10 residues long whereas CDRs 2 and 3 are 11 residues in length. SEQ ID NO:8/Nb 701B09 is comparable in that page 5 also shows its sequence wherein the CDRs are underlined, with CDRs 1 and 2 being 10 residues in length while CDR3 is 11 residues in length. Both SEQ ID NOs:8 and 10 are 120 residues in length, so at least 90% identical allows for the presence of 12 random mutations. However, as discussed above the art, such as Rudikoff et al., indicates that changes even as small as a single CDR residue can abrogate binding. The specification does not appear to provide any specific guidance concerning what mutations can or cannot be made to the CDRs while maintaining function. As such, the amount of structure that minimally must be present in the claims does not reasonably appear to give rise to the recited functional properties, and the prototypic VHH of SEQ ID NOs 8 and 10 themselves are not a reasonably representative sampling of species lying within the claimed genera.
As such, the while the instant specification discloses the VHH of SEQ ID NOs:8 and 10 which have the recited functional properties, the breath of structures encompassed by the instant claims is much broader than those of the working examples. As discussed supra, identifying an antibody based upon what it binds rather than what it is (i.e. its sequence/structure, such as a full length VHH) has generally been found to be insufficient to provide written description of the antibody in question, and the percent identity limitations encompass changes to the very structures identified in the art as being responsible for the function of antigen binding, i.e. the CDRs.
Therefore, in view of the facts that the VHH constructs disclosed by applicant are not representative of the breadth of structures encompassed by the instant claims and the fact that identification of an epitope bound by a reference antibody does not provide a description of all possible antibody structure that bind said epitope, skilled artisans would reasonably conclude that applicants were not in possession of the full genus antibodies at the time the instant application was filed.
Applicant's arguments filed January 28, 2026 have been fully considered but they are not persuasive. Applicant argues that the partial structures recited in the claims, when combined with the recited functional properties is sufficient to convey possession of that which is presently claimed.
This argument has been considered and is not persuasive. The partial structure recited in the claims is insufficient to give rise to the recited functional property. Indeed, it is well established in the art that it is the structure of the CDRs which is correlated with the function of antigen binding, not some arbitrary percent identity to a full length antigen binding domain. Thus the claims encompass removal via mutation the very structure artisans reasonably would accept as providing for the recited functional properties. Thus as written the claims fail to set forth sufficient correlation between the required structural and functional properties and therefore the rejection is maintained.
Claims 1, 3, 5, and 7 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 claimed a genus of nanobodies (also referred to as a VHH, the variable domain of a type of single domain antibody isolated from Camelidae animals that has only a heavy chain (and thus only three CDRs)) that bind to factor X which are required to be at least 90% identical in sequence to either SEQ ID NO:8 or SEQ ID NO:10. All claims under examination allow for changes relative to the recited reference sequences to occur anywhere within the sequence, and thus CDR mutations are encompassed. The specification discloses that applicant generated VHH from a llama and an alpaca immunized with factor X (see page 38 of the specification). No data concerning mutagenesis of lead antibody clones appears to be disclosed in the specification as filed.
It is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway et al., see entire selection). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff et al., see entire document, particularly the abstract and the middle of the left column of page 1982). The antibodies presently claimed are not conventional antibodies that have six CDRs, and instead read upon immunoglobulin single variable domains, a class of antibodies typically derived from camelid heavy chain antibodies (VHH) which are distinct in that they comprise only a single polypeptide chain, and thus only have 3 CDRs which are responsible for antigen binding (see for example pages 11-13 of the instant specification). However, the majority of antigen contacts for such VHH are still found within the CDRs (Ghahroudi et al., see entire document).
As previously stated, applicant recovered the VHH sequences of SEQ ID NOs:8 and 10 subsequent to immunization of an animal with human factor X antigen. Replication of such an experiment is unlikely to yield the polypeptides of SEQ ID NO:8 or 10 as the art has long recognized that a vast diversity of sequences can bind the same target antigen. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well, see entire document). Similarly, Lloyd et al. teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (see entire document). As such, it is very improbable that artisans would recover the biological sequences of either SEQ ID NO:8 or 10 if they attempted to replicate applicant’s method of making as set forth in the working example even if such a replication absolutely would yield VHH that bind factor X; it is simply that the sequences of such antibodies are unlikely to look anything like SEQ ID NOs:8 or 10. Note that as presently recited the instant claimed antibodies must be at least 90% identical to the recited SEQ ID number, and the only reasonable way presently to make an antibody with defined biological sequences is via recombinant molecular biotechnology. Such techniques require starting with six fully defined CDRs to ensure the antibody products will have the required functional activities, including binding to the correct target antigen. All of the present claims permit these CDR sequences needed for binding antigen to be mutated. No mutagenesis data appears to be provided in the instant application. Thus artisans would need to engage in additional unpredictable basic science research and experimentation in order to make the full extent of the genus of nanobodies as presently claimed.
Applicant's arguments filed January 28, 2026 have been fully considered but they are not persuasive. Applicant argues that the specification discloses how to identify a minimal epitope and therefore artisans can make and use that which is claimed.
This argument has been considered and is not persuasive. The claimed invention requires the antibody product to have at least 90% identity with a recited reference sequence (i.e. SEQ ID NOs:8 or 10) and have specific functions including binding factor X at a particular location. Given the large number of unrelated sequences which are reasonably expected to be recovered following immunization of an animal the only reasonable way to make the recited genus of antibodies is by recombinant techniques with such techniques requiring fixed CDR sequences to ensure antigen binding activity, such as binding to a defined epitope. Given that as explained in the rejection of record even a single CDR change can eliminate binding, the genus of VHH comprising mutations in the CDRs are not reasonably enabled without extensive trial and error research and experimentation. Indeed, SEQ ID NOs:8 and 10 are 120 residues in length, so 90% identity allows for 12 changes, all of which could occur within the CDRs. Thus, applicant’s argued screening assay does not inform an artisan of how to make what has been claimed but only serves to identify if something already been made (i.e. preexisting) does nor does not meet the recited functional limitations as such an assay in no way alters the physical form of the thing being tested. 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 1-6 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 11,787,874. Although the claims at issue are not identical, they are not patentably distinct from each other because the issued claims anticipate that which is presently claimed.
Specifically, the issued claims recite anti-FX nanobodies that comprise SEQ ID NOs: 8 and 10 and their administration to treat hemophilia, and note the SEQ ID numbers are identical as the instant application is a continuation of the application which gave rise to the ‘874 patent. It is noted that the issued claims do not recite binding epitopes or affinities. However, the courts have long recognized that "Products of identical chemical composition can not 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. Given that the polypeptides of SEQ ID NOs:8 and 10 are the same, functional properties including epitope specificity and binding activity are necessarily present even if not disclosed in the issued claims as having been elucidated or measured. Also note that SEQ ID NOs:8 and 10 are exact sequences whereas the instant claims are drawn to sequences at least 90 percent identical to SEQ ID NOs:8 or 10, which is in reality a genus of sequences which includes SEQ ID NO:8 and SEQ ID NO:10 themselves.
Applicant's arguments filed January 28, 2026 have been fully considered but they are not persuasive. Applicant has acknowledged the rejection and indicates that the issue will be attended to once the claimed inventions are otherwise allowable.
This argument is not persuasive as applicant has not amended the pending claims to provide a clear line of demarcation relative to that which was issued in the parent, nor has applicant filed a terminal disclaimer. The rejection is maintained.
Claims 7 and 8 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 11,787,874 as discussed above and further in view of Silence et al. (WO 2004/041865).
The inventions anticipated by the issued claims have been discussed above and differ from what is presently claimed in that the issued claims do not recite the presence of bi- or multi-specific antibodies.
Silence et al. disclose VHH that bind to serum albumin and which can be used in constructs comprising more than one VHH in order to increase serum half-life (see entire document, particularly the abstract, claims, and page 3).
Therefore, artisans would have been motivated to attach and anti-albumin VHH to the anti-FX VHH constructs of the issued claims in order to increase their serum half-life when used in methods including the claimed methods of administration to treat hemophilia.
Applicant's arguments filed January 28, 2026 have been fully considered but they are not persuasive. Applicant has acknowledged the rejection and indicates that the issue will be attended to once the claimed inventions are otherwise allowable.
This argument is not persuasive as applicant has not amended the pending claims to provide a clear line of demarcation relative to that which was issued in the parent, nor has applicant filed a terminal disclaimer. The rejection is maintained.
No claims are allowable.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to 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