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 .
Claim Status and Formal Matters
This action is in response to papers filed 6/11/2026.
The instant response in non-compliant with respect to 37 CFR 1.121 as claim 3 provides language that is both underlined and in double brackets. However to promote compact prosecution and customer service the instant response will be examined. Future amendment which are not compliant may not be entered or examined.
Claims 1, 3, 15, 31-32, 39, 59, have been amended.
Claims 1, 3, 15, , 20, 27, 29-33, 35, 39, 59, 64-66 are pending and being examined.
The objection to the drawings has been withdrawn.
The previous objection to the specification has been withdrawn.
The previous objection to the claims has been withdrawn.
The 102 rejection has been withdrawn in view of the amendment to require SEQ ID NO in the independent claims.
Priority
The instant application was filed 03/15/2024 Claims Priority from Provisional Application 63452617, filed 03/16/2023.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 6/18/2024 is being considered by the examiner.
Specification
The specification is objected to as failing to provide proper antecedent basis for the claimed subject matter. See 37 CFR 1.75(d)(1) and MPEP § 608.01(o). Correction of the following is required:
Claim 1 has been amended to recite, “fragment crystallizable.” Review and searching of the specification did not reveal antecedent basis for the amendment.
Response to Arguments
This is a new ground of objection necessitated by amendment.
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, 3, 15, , 20, 27, 29-33, 35, 39, 59, 64-66 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.
As set forth in In re Alonso 88 USPQ2d 1849 (Fed. Cir. 2008), at 1851:
The written description requirement of 35 U.S.C. § 112, ¶ 1, is straightforward: “The specification shall contain a written description of the invention ….” To satisfy this requirement, the specification must describe the invention in sufficient detail so “that one skilled in the art can clearly conclude that the inventor invented the claimed invention as of the filing date sought.” Lockwood v. Am. Airlines, Inc., 107 F.3d 1565, 1572 [41 USPQ2d 1961] (Fed. Cir. 1997); see also LizardTech, Inc. v. Earth Res. Mapping, Inc., 424 F.3d 1336, 1345 [76 USPQ2d 1724] (Fed. Cir. 2005); Eiselstein v. Frank, 52 F.3d 1035, 1039 [34 USPQ2d 1467] (Fed. Cir. 1995).
Alonso at 1852:
A genus can be described by disclosing: (1) a representative number of species in that genus; or (2) its “relevant identifying characteristics,” such as “complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics.” Enzo, 323 F.3d at 964.
In applying the test as set forth in Alonso, it is noted that applicant is claiming A construct comprising a truncated poliovirus receptor (PVR) and a fragment crystallizable (Fc}domain, wherein the truncated PVR comprises a truncated murine immunoglobulin-like variable (IgV) extracellular domain (ECD) comprising or consisting of residues 29 to 147 of SEQ ID NO:1 and wherein the Fe domain is a human IgG1 Fc domain comprising or consisting of a polypeptide having at least 80% sequence identity to SEQ ID NO:3.. The independent claim provides the function of truncated poliovirus receptor (PVR) and Fc domain is a human IgG1 Fe domain. Dependent claims require at least one of:(a) the construct is soluble;(b) the construct can bind to cognate receptors with similar nanomolar affinities[[y]] as compared to a construct comprising a non-truncated PVR;(c) the construct binds to the cognate receptor at low nanomolar affinities oT cell immunoreceptor with Ig and ITIM domains (TIGIT) with an affinity of about 2.2 nM;(e) the construct binds to CD96 with an affinity of about 1.7 nM; (f) the construct binds to CD226 with an affinity of about 0.7 nM;(g) when administered in vitro or in vivo, the construct suppresses immune responses, wherein the immune response comprises a cytokine response or cells, as compared to a construct comprising a non-truncated PVR;(h) when administered to a subject, the construct reduces symptoms associated with an inflammatory disease or condition selected from Crohn's disease, ulcerative colitis, multiple sclerosis, asthma, rheumatoid arthritis, or psoriasis, as compared to a construct comprising a non-truncated PVR; and(i) when administered to a subject, the construct delays the onset of psoriasis, as compared to a construct comprising a non-truncated PVR.
Further claims 59, 64-65 encompass nucleic acids comprising or consisting of a polynucleotide having at least 80% of SEQ ID NO 9 or SEQ ID NO 10. The indefinite article prior to a polynucleotide encompasses a fragment of the polynucleotide.
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The specification in examples provides an assessment of PVFR-Fc binding affinity. Example 2 provides some commercially available antibodies, but does not provide amino acid or nucleotide sequences. The specification has not provided a representative number of species to demonstrate possession of the functional outcomes of dependent claims.
New Matter
MPEP 2163 IB New or amended claims section II
With respect to newly added or amended claims, applicant should show support in the original disclosure for the new or amended claims. See, e.g., Hyatt v. Dudas, 492 F.3d 1365, 1370, n.4 (Fed. Cir. 2007) (citing MPEP § 2163.04 which provides that a "simple statement such as ‘applicant has not pointed out where the new (or amended) claim is supported, nor does there appear to be a written description of the claim limitation ‘___’ in the application as filed’ may be sufficient where the claim is a new or amended claim, the support for the limitation is not apparent, and applicant has not pointed out where the limitation is supported."); see also MPEP §§ 714.02 and 2163.06 ("Applicant should ... specifically point out the support for any amendments made to the disclosure."); and MPEP § 2163.04
Claim 39 has been amended to recite, “as compared to a construct comprising a non-truncated PVR;” in (g), (h), (i). The response merely asserts the amendments to the claims can be found throughout the specification. Review and searching of the specification revealed “as compared to a construct comprising a non-truncated PVR;.” However, the portions which recite, “as compared to a construct comprising a non-truncated PVR” does not provide a nexus or blaze marks to “hen administered in vitro or in vivo, the construct suppresses immune responses, wherein the immune response comprises a cytokine response or cells, as compared to a construct comprising a non-truncated PVR;(h) when administered to a subject, the construct reduces symptoms associated with an inflammatory disease or selected from Crohn's disease, ulcerative colitis, multiple sclerosis, asthma, rheumatoid arthritis, or psoriasis, as compared to a construct comprising a non-truncated PVR; and(i) when administered to a subject, the construct delays the onset of psoriasis, as compared to a construct comprising a non-truncated PVR.” Thus the amendment appears to introduce new matter.
Response to Arguments
The response traverses the rejection by asserting, “Applicant submits that claim 1 as amended satisfies the written description requirement. Amended claim 1 is drawn to a relatively narrow group of truncated PVRs comprising IgV ECD and Fc domains with specific sequences. The relevant identifying characteristics, including the structure, physical/chemical properties, and functional characteristics of the claimed construct are encompassed in the sequences and are sufficiently described in the specification, including in the exemplified embodiments. For example, FIGS. 1-2 depict the structure of the claimed constructs according to some embodiments.” This argument has been thoroughly reviewed but is not considered persuasive as figures 1 and 2 provide cartoon or ribbon diagrams. This does not demonstrate written description for a construct comprising a truncated poliovirus receptor (PVR) and a fragment crystallizable (Fc}domain, wherein the truncated PVR comprises a truncated murine immunoglobulin-like variable (IgV) extracellular domain (ECD) comprising or consisting of residues 29 to 147 of SEQ ID NO:1 and wherein the Fe domain is a human IgG1 Fe domain comprising or consisting of a polypeptide having at least 80% sequence identity to SEQ ID NO:3 with the functional characteristics of a) the construct is soluble;(b) the construct can bind to cognate receptors with similar nanomolar affinities[[y]] as compared to a construct comprising a non-truncated PVR;(c) the construct binds to the cognate receptor at low nanomolar affinities of, such as, about 0.1 nM to about 10 nM;(d) the construct binds to T cell immunoreceptor with Ig and ITIM domains (TIGIT) with an affinity of about 2.2 nM;(e) the construct binds to CD96 with an affinity of about 1.7 nM;(f) the construct binds to CD226 with an affinity of about 0.7 nM;(g) when administered in vitro or in vivo, the construct suppresses immune responses, wherein the immune response comprises a cytokine response or wherein the immune response comprises proliferation of immune cells, as compared to a construct comprising a non-truncated PVR;(h) when administered to a subject, the construct reduces symptoms associated with an inflammatory disease or condition or for treating an inflammatory disease or condition selected from Crohn's disease, ulcerative colitis, multiple sclerosis, asthma, rheumatoid arthritis, or psoriasis, as compared to a construct comprising a non-truncated PVR; and(i) when administered to a subject, the construct delays the onset of psoriasis, as compared to a construct comprising a non-truncated PVR.
The response continues by asserting, “For example, FIGS. 3-6 and pages 9-10 of the specification provide data showing surface plasmon resonance (SPR) titration profiles of the constructs and further show and describe that the claimed constructs bind primary mouse T-cells and suppresses T-cell activity in mouse splenocyte cultures ex vivo. Meanwhile, FIG. 8 and pages 9-10 of the specification describe that the claimed constructs show cytotoxicity towards mouse splenocytes. And FIGS. 10-12 and pages 11-12 of the specification describe that the claimed constructs can attenuate, delay the onset of, or reduce symptoms of various diseases, such as DSS-induced colitis and psoriasis. Thus, the specification has sufficiently disclosed the correlation between the structure and function of the claimed constructs.” This argument has been thoroughly reviewed but is not considered persuasive as the cited portion provides no amino acid or nucleic acid sequences such as to provide a structure function relationship with 80% sequence identity with SEQ ID NO 3 and the required function of truncated polio virus receptor or functional requirement of dependent claims.
The response continues by asserting, “the specification provides a detailed description of the manner of making and using the claimed constructs. Example 1 provides a detailed description of the design and the method of producing the claimed constructs. Examples 2-4 describe in detail how to use the claimed constructs in binding and ex vivo assays and to suppress murine T-cell activity. Example 5 and FIG. 9 describe how to use the claimed constructs in clinical applications and show the experimental outline of a DSS-induced colitis model. Thus, the specification has provided ample description of the manner of making and using the constructs according to instant amended claim 1. For at least these reasons, the specification provides sufficient written description for claim 1 as amended.” This argument has been thoroughly reviewed but is not considered persuasive as the cited portion provides no amino acid or nucleic acid sequences such as to provide a structure function relationship with 80% sequence identity with SEQ ID NO 3 and the required function of truncated polio virus receptor or functional requirement of dependent claims.
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.
Claims 333, 35, 39 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.
Claim 3 recites, “wherein the truncated PVR is does not comprise [[th]]immunoglobulin-like constant (IgC} domains.” The claim is confusing and unclear in view of the recitation of “[[th]]immunoglobulin-like constant (IgC}.”
Claim 33 has been amended to recite, “comprising or consisting of a polypeptide having at least 80% sequence identity to SEQ ID NO:7: METDTLLLWVLLLWVPGSTGdirvlvpynstgvlggsttlhcsltsnenvtitgitwmkkdsggshalvavfhpkkgp nikepervkflaaqqdlrnaslaisnlsvedegiyecqiatfprgsrstnawlkVQARPKNIEGRMDPTHTCPPCPAPE LLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPR EEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTL PPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLT VDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK or a fragment thereof; or comprising or consisting of a polypeptide having at least 85, 90, 95, 96, 97, 98, or 99% identity to SEQ ID NO:7.” However claim 1 has been amended to require residues 29 to 147 of SEQ ID NO 1 and 80% sequence identity of SEQ ID NO 3. Thus it is unclear how at least 80% sequence identity to SEQ ID NO:7:relate to the sequences of the independent claim.
Claim 39 recites, “the construct can bind to cognate receptors with similar nanomolar affinities as compared to a construct comprising a non-truncated PVR.” The statement is confusing and unclear. The recitation of “similar nanomolar affinities” suggests there is non-similar nanomolar affinities. Further the claim and specification do not define what is required of cognate receptor. Thus the metes and bounds are unclear.
Response to Arguments
The previous grounds of rejection have been withdrawn. The amendment has introduced new issues as indicated in the rejection.
Claim Rejections - 35 USC § 103
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 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claim(s) 1, 3, 15, 20, 27, 29-33, 39, 59, 64-66 is/are rejected under 35 U.S.C. 103 as being unpatentable over Tahara-Hanaoka (.International Immunology, Vol. 16, No. 4, pp. 533±538), Swanson (US 20190175654), Levin (Wo2006124667), Shi (WO202020281), Cherpes (WO2021071979), Anderson (WO2001036637), Swanson (WO2018022946)
Tahara-Hanaoka teaches, “human poliovirus receptor-related (PRR) family
members CD155 [poliovirus receptor (PVR)].”
With regards to claim 1, 5, 66 Tahara-Hanaoka teaches, “CD155-Fc and CD112-Fc fusion proteins were also generated with chimeric cDNAs of the entire extracellular domain of CD155 or CD112 with the human IgG1 Fc.” (534, expression of the Fc fusion proteins)
While, Tahara-Hanaoka teaches CD155-Fc fusion, Tahara-Hanaoka does not teach sequences or specifics of how the construct is made.
However, Swanson (US2019) teaches, “[0005] Provided herein are variant CD155 polypeptides. In some embodiments, the variant CD155 polypeptides comprise an IgV domain or a specific binding fragment thereof, an IgC domain or a specific binding fragment thereof, or both, wherein the variant CD155 polypeptide comprises one or more amino acid modifications in an unmodified CD155 or a specific binding fragment thereof corresponding to position(s) selected from 7, 8, 9, 10, 11, 12, 13, 15, 16, 18, 19, 20, 21, 22, 23, 24, 25, 26, 29, 30, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 64, 65, 67, 68, 69, 70, 72, 73, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 87, 88, 89, 90, 91, 92, 94, 95, 96, 97, 98, 99, 100, 102, 104, 106, 107, 108, 110, 111, 112, 113, 114, 115, or 116 with reference to positions set forth in SEQ ID NO: 47. In some embodiments, the amino acid modifications comprise amino acid substitutions, deletions or insertions. In some embodiments, the unmodified CD155 is a mammalian CD155 or a specific binding fragment thereof. In some embodiments, the unmodified CD155 is a human CD155 or a specific binding fragment thereof.” Swanson teaches, “0017] In some embodiments of any one of the variant CD155 polypeptides, the variant CD155 polypeptide is linked to a moiety that increases biological half-life of the polypeptide. In some embodiments, the variant CD155 polypeptide is linked to an Fc domain or a variant thereof with reduced effector function. In some embodiments, the Fc domain is mammalian, optionally human; or the variant Fc domain comprises one or more amino acid modifications compared to an unmodified Fc domain that is mammalian, optionally human.”
Levin teaches, “[20] An illustrative nucleotide sequence that encodes human CD 155 (also interchangeably known as PVR) is provided by SEQ TD NO: 17; the encoded polypeptide is shown in SEQ ID NO:18. CD155 has been shown to bind to ZB7R1 and thus is a counter-receptor for this B7 family member. Analysis of a human cDNA clone encoding zB7Rl (SEQ ID NO: 17) revealed an open reading frame encoding 417 amino acids (SEQ TD NO: 18) comprising an extracellular domain of approximately 316 amino acid residues (residues 28-343 of SEQ ID NO:18; SEQ TD NO:19), a transmembrane domain of approximately 24 amino acid residues (residues 344-367 of SEQ ID NO: 18), and an intracellular domain of approximately 50 amino acid residues (residues 368-417 of SEQ ID NO: 18). [21] An illustrative nucleotide sequence that encodes a murine CD155 is provided by SEQ TD NO:20; the encoded polypeptide is shown in SEQ TD NO:21. The extracellular domain is shown in SEQ TD NO:22. Analysis of a cDNA clone encoding murine CD155 revealed an open reading frame encoding 408 amino acids (SEQ ID NO:21) comprising an extracellular domain of approximately 319 amino acid residues (residues 29-347 of SEQ DD NO:21; SEQ TD NO:22), a transmembrane domain of approximately 20 amino acid residues (residues 348-367 of SEQ ID NO:21), and an intracellular domain of approximately 40 amino acid residues (residues 368-408of SEQ ID NO:21)” Levin teaches a mouse poliovirus receptor CD155 extracellular domain (SEQ ID NO 22) which copies SEQ ID NO 1. (claims 5-6, 7)
Shi teaches HCDR1 SEQ ID NO 3 (table 3) which comprises SEQ ID NO 3 (111-440) of instant claims.
Cherpes teaches SEQ ID NO 7 (IEGRMDP) a linker for fusion proteins which comprises instant SEQ ID NO 5 and linker of fusion proteins SEQ ID NO 8 (IEGRMD).
Anderson teaches Immunoglobulin (Ig) kappa chain leader peptide SEQ ID NO 16 which consists of instant SEQ ID NO 6. (page 82, example 15)
Swanson (WO2018) teaches SEQ ID NO 1121, example 11 which comprises amino acids 301-371 of SEQ ID NO 7.
Therefore it would have been prima facie obvious to one of ordinary skill in the art prior to the effective filing date of the claims to use known sequences to construct a soluble CD155-FC fusion. The artisan would be motivated to produce a soluble CD155-FC fusion as Tahara-Hanaoka, Swanson (WO2018), Swanson (US2019) explicitly suggest the production of an CD155-FC fusion for immunomodulation and treatment of disease. The artisan would be motivated to provide linker sequences to keep the peptides in correct orientation. The artisan would be motivated to use a secretion sequence to provide for secretion of the proteins from cells. The artisan would be motivated to use mammalian Fc domains as Swanson suggest they may increase protein half-life. The artisan The artisan would have a reasonable expectation of success as the artisan is merely using known amino acid sequences with known properties to provide a CD155-FC fusion.
With regards to claim 3, Tahara-Hanaoka teaches CD155-Fc fusion, which is free of IgC.
With regards to claim 29, Swanson teaches, “In some embodiments, the variant CD155 polypeptide is linked to the multimerization domain or Fc indirectly via a linker, optionally a G4S linker.” (0017)
Claims 59, 64-65 encompass nucleic acids comprising at least 80% of SEQ ID NO 9 or SEQ ID NO 10 or fragments thereof. Thus they are obvious over the cited prior art in view of the fragment thereof.
Response to Arguments
The response begins traversing the rejection by providing the representatives interpretation of the art. This is noted.
The response traverse the rejection asserting they cited reference fail to provide any motivation to modify. In response to applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, one of skill in the art in view recognizes what is required to produce a secreted protein as demonstrated by Tahara-Hanaoka (.International Immunology, Vol. 16, No. 4, pp. 533±538), Swanson (US 20190175654), Levin (Wo2006124667), Shi (WO202020281), Cherpes (WO2021071979), Anderson (WO2001036637), Swanson (WO2018022946). Thus the rejection is maintained.
Summary
No claims are allowed.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to STEVEN C POHNERT PhD whose telephone number is (571)272-3803. The examiner can normally be reached Monday- Friday about 6:00 AM-5:00 PM, every second Friday off.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Anne Gussow can be reached at (571)272-6047. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Steven Pohnert/Primary Examiner, Art Unit 1683
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