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 .
Election/Restrictions
Applicant's election with traverse of Group I, claims 1-9, 12, 14, 16-19, and 21-23 and the species of SEQ ID NO: 19, Shiga toxin translocation peptide in the reply filed on 11/28/25 is acknowledged. The traversal is on the ground(s) that claim 1, amended to recite element (d) of claim 1 to be located immediately adjacent to the CD40-binding domain and translocation domain, is not a feature disclosed in the cited art and makes a contribution over the cited art. This is not found persuasive because the technical feature under consideration when the Restriction requirement was made was Xa fusion protein comprising a CD40L that is 95% identical to SEQ ID NO: 19 or a functional fragment, antigen of a pathogen, a translocation domain, and a furin or cathepsin L cleavage site, all which was disclosed by WO’266, Pieczykolan, and Uniprot P29965. Thus, the claim was found to lack a special technical feature distinguished over the prior art. Hence, the requirement is still deemed proper and is therefore made FINAL, as Applicant cannot amend the claim to overcome initial grounds upon which a lack of unity of invention was made and supported.
It is also noted that Applicant did not select a sequence of Stx translocation peptide for examination (see claim 17). For the purposes of compact patent prosecution, the examiner has searched SEQ ID NO:12, which is utilized in the rejections below.
It is further noted that claims 2, 3, 12 and 16 are drawn to non-elected species of translocation peptide and will not be examined under the restriction requirement. Claims 2-3, 15-16 and 20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention (15 and 20) and species (2-3, 12 and 16), there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 11/28/25.
Priority
The instant application claims benefit to PCT/US2022/078832, filed on 10/28/2022 and is acknowledged. The instant claims herein are examined using the effective filing date of 10/28/2022 for the basis of any prior art rejections.
Information Disclosure Statement
The information disclosure statement(s) (IDS) submitted on 07/04/2023 properly filed in compliance with 37 CFR 1.97. Accordingly, the information disclosure statement(s) was considered.
Nucleotide and/or Amino Acid Sequence Disclosures
Summary of Requirements for Patent Applications Filed On Or After July 1, 2022, That Have Sequence Disclosures
37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted:
1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying:
a. the name of the XML file
b. the date of creation; and
c. the size of the XML file in bytes; or
2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying:
a. the name of the XML file;
b. the date of creation; and
c. the size of the XML file in bytes.
SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS:
Specific deficiency - The incorporation by reference paragraph required by 37 CFR 1.834(c)(1), 1.835(a)(2), or 1.835(b)(2) recites the XML file size in KB, not bytes.
Required response - Applicant must:
• Provide a substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required incorporation by reference paragraph, consisting of:
• A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
• A copy of the amended specification without markings (clean version); and
• A statement that the substitute specification contains no new matter.
Claim Objections
Claim 4 objected to because of the following informalities: claim 4 recites, inter alia, “SEQ ID NOs: 12” (emphasis added). The claims should be amended to recite “SEQ ID NO: 12.” Appropriate correction is required.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 4-9, 14, 17-19 and 21-23 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, 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 inventor was in possession of the claimed genus. See, e.g., Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1340, 94 USPQ2d 1161, 1167 (Fed. Cir. 2010); University of California v. Eli Lilly & Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) at 1406; Juno Therapeutics, Inc. v. Kite Pharma, Inc., 10 F.4th 1330, 1337, 2021 USPQ2d 893 (Fed. Cir. 2021) ("[T]he written description must lead a person of ordinary skill in the art to understand that the inventor possessed the entire scope of the claimed invention. Ariad, 598 F.3d at 1353–54 ('[T]he purpose of the written description requirement is to ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor's contribution to the field of art as described in the patent specification.' (internal quotation marks omitted).").
A "representative number of species" means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). The issue is whether the skilled artisan would understand inventor to have invented, and been in possession of, the invention as claimed.
Independent claim 1 (and thus the dependent claims) require (a) a CD40-binding domain, which is a CD40 ligand (CD40L) or a functional fragment thereof comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 19, said CD40L or functional fragment thereof consisting of 154-261 amino acid residues in length; (b) an antigen of a pathogen; (c) a translocation domain, located between the CD40-binding domain and the antigen, said translocation domain being selected from the group consisting of: (c1) a Shiga toxin (Stx) translocation peptide; and (c2) a Pseudomonas Exotoxin A (PE) translocation peptide; and (d) a furin and/or cathepsin L cleavage site, located between immediately adjacent to the CD40-binding domain and the translocation domain, wherein the pathogen is at least one selected from the group consisting of Classical Swine Fever Virus (CSFV), African Swine Fever Virus (ASFV), Porcine Circovirus 2 (PCV2), Porcine Reproductive and Respiratory Syndrome Virus (PRRSV), Porcine Epidemic Diarrhea Virus (PEDV), Foot-and-Mouth Disease Virus (FMDV), Swine Vesicular Disease Virus (SVDV), Pseudorabies Virus (PRV), Transmissible Gastroenteritis Virus (TGEV), Mycoplasma hyopneumoniae, Newcastle Disease Virus (NDV), Infectious Bronchitis Virus (IBV), Infectious Bursal Disease Virus (IBDV), Parvovirus, Poxvirus, Rotavirus, and Influenza Virus; and further wherein when the translocation domain is the Stx translocation peptide, the antigen is located at the N-terminal of the fusion protein; and when the translocation domain is the PE translocation peptide, the CD40-binding domain is located at the N-terminal of the fusion protein.
The specification defines “CD-40 binding domain” (and functional fragment thereof) as a protein that can recognize and bind to CD40, and CD40L as being capable of binding to CD40 protein on antigen-presenting cells which leads to many effects depending on the target cell type, plays a significant role in co-stimulation and regulation of immune response via T cell priming and activation of CD40-expressing immune cells (see pg. 3). Thus, the examiner has interpreted the claim to require a broad genus of fragments of CD40 binding domain (that is anywhere between 154-261 amino acids long) that must retain functional capacity to recognize and bind to CD40, and CD40L as being capable of binding to CD40 protein on antigen-presenting cells which leads to many effects depending on the target cell type. Furthermore, the specification defines “Shiga toxin translocation peptide” as a Stx translocating domain or a functional fragment thereof that has biological activity of translocation (see pg. 3 of the specification). Thus, the examiner has interpreted the claim to require a broad genus of Stx translocation peptides or functional fragments that retain the biological functional activity of translocation. This is problematic because the specification fails to teach an art-recognized correlation between structure and function.
In support of the claimed genus of CD40 ligands, the specification discloses 3 CD40 ligands for use in fusion proteins, namely, SEQ ID NOs: 17-19 (full length CD40L that is 261 AAs long, truncated CD40L retaining amino acids 47-261 that is 215 AAs long, and truncated CD40L retaining amino acids 108-261 that is 154 AAs long, respectively) (see Table 1; Example 1-2). Applicant further discloses that fusion proteins that contain SEQ ID NO: 19, (e.g., CD40L-TPE-CP204L-E183L and CP204L-E183L-TStx-CD40L) were expressed in E. coli cells and purified before subsequent immunogenicity analyses (see, e.g., Example 2). The specification also discloses 5 Stx translocation peptides, namely, SEQ ID NOs: 12-16 (minimal functional fragment, Stx 240-251, Stx 211-247, Stx 211-251, and Stx 168-251). The generation of the fusion proteins disclosed in Example 1 of the specification containing specific CD40Ls (full length and fragments) and Stx cannot reasonably be extrapolated and applied to support possession of the entire claimed genus of CD40L/functional fragments useful in a fusion protein, because no one species, combination, or variant accounts for the variability amongst the claimed genus. As in Ariad, merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing that one has invented a genus and not just a species. “A patent is not a hunting license. It is not a reward for the search, but compensation for its successful conclusion.” Brenner v. Manson, 383 U.S. 519, 536 (1966).
There is also no disclosure as to what structure(s) must be present or retained on the fragment of CD40L that would result in a functional fragment for use in the fusion protein. Applicant has not has not provided any information or steps as to how one of ordinary skill would obtain a functional fragment of CD40L or Stx, or any sufficient distinguishing structure-function relationship with respect to the broad genus as claimed. this data cannot be extrapolated to any and all possible fragments of the Stx translocation peptides. Even with knowledge in the art regarding modification of genes, one of ordinary skill would not reasonably know, based on the disclosure provided, what structures or functions are required for the outcome of creating a functional fragment of CD40L and Stx without a recognized correlation between structure and function.
There is no disclosure as to what structure(s) must be present or retained on the “functional fragment” or functional characteristics that would distinguish a functional fragment of a protein from a non-functional fragment. Applicant has provided no information as to how a fragment would be considered “functional”, distinguishing characteristics, or the amount of biological activity that is required for the fragment to work. There is no sufficient structure-function relationship with respect to the broad genus as claimed. The data in the specification cannot be extrapolated to any and all possible counterparts of CD40L and Stx translocation peptides. Even with knowledge in the art regarding the modification of proteins, one of ordinary skill would not reasonably know, based on the disclosure provided, what structures or functions are required for the outcome of creating a functional fragment of these proteins without a recognized correlation between structure and function.
The specification, then, is considered devoid of sufficiently detailed, relevant, identifying characteristics demonstrating that Applicant was in possession of the claimed genus of CD40L and Stx translocation peptides, i.e., additional complete or partial structures, other physical and/or chemical properties, functional characteristics coupled with a known or disclosed correlation between function and structure, or some combination thereof demonstrating possession of the claimed genus. Therefore, claims 1, 4-9, 14, 17-19 and 21-23 are rejected under 35 U.S.C. 112(a) for lack of written description.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 6 is 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 6 recites, inter alia, the furin and/or cathepsin L cleavage site comprises the amino acid sequence of SEQ ID NO: 1 or 2. SEQ ID NO: 1 and 2 are indefinite as the XML file does not list these sequences. Therefore, claim 6 fails to provide the metes and bounds of the claim by using SEQ ID NO: 1 and 2. For the purposes of compact patent prosecution, the examiner is interpreting the cleavage sites to comprise 4-20 amino acids (see pg. 6, lines 1-12 in the amended specification filed 11/28/2025).
It is noted any interpretation of the claims set forth above does not relieve Applicant of the responsibility of responding to this rejection. If the actual interpretation of the claims is different than that posited by the Examiner, additional rejections and art may be readily applied in a subsequent final Office action.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
First rejection
Claims 1, 4-9, 14, 17,-19, and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Wu et al (US9481714B2, see US 20140154285 A1; hereinafter “Wu”) in view of Raue et al (WO 2018213747 A1; hereinafter “Tykocinski”), and Poma et al (US10815469 B2; hereinafter “Poma”).
Wu teaches a fusion protein consisting of an antigen-presenting cell (APC) binding domain or a CD91 receptor-binding domain, an antigen of pathogen, and a translocation domain located between and immediately adjacent to the binding domain and the antigen (Abstract; see paragraph 0095). Wu teaches the binding domain is located at the N-terminus (abstract and paragraph 009). Wu teaches embodiments wherein a furin and/or L cathepsin L cleavage site is present in the fusion protein between the binding domain and the translocation domain (see paragraph 0055). Wu teaches the use of a translocation domain of Pseudomonas exotoxin A (see paragraph 0016). Wu also teaches the antigen of a pathogen can be Human Papillomavirus (HPV), PRRSV, HIV-1, flu virus, Dangue virus, Hepatitis C virus (HCV), Hepatitis B virus (HBV), Porcine Circovirus 2 (PCV2) (see paragraph 0102).
Wu does not teach that the CD binding domain is a CD40L that is 95% identical to SEQ ID NO: 19 and 154-261 amino acids in length and located at the C-terminal.
However, Raue teaches a bispecific molecule that is a fusion protein that comprises a CD40 agonist moiety, a 4-1BB agonist moiety, and a dendritic cell binding moiety. Raue also teaches the fusion molecule is for use in treatment of CD40 related disorders (abstract). Raue teaches the improved strategies for targeting diseases such as human immunodeficiency viruses (GIV), hepatitis viruses class A, B and C, human cytomegalovirus, human papilloma viruses, leishmaniasis, toxoplasmosis, cryptosporidiosis, sleeping sickness, malaria, herpes virus (e.g., VZV, HSV-1 , HAV-6, HSV-I I, and CMV, Epstein Barr virus), adenovirus, influenza virus, flaviviruses, echovirus, rhinovirus, coxsackie virus, coronavirus, respiratory syncytial virus, mumps virus, rotavirus, measles virus, rubella virus, parvovirus, vaccinia virus, HTLV virus, dengue virus, papillomavirus, molluscum virus, poliovirus, rabies virus, JC virus and arboviral encephalitis virus using CD40 activity are highly desirable (paragraph 0007; see paragraph 0127) and specifically that the CD40 is CD40L (see paragraph 0023). Raue teaches the CD40 agonist of the invention can result in increased efficacy, decreased toxicity, and an increased therapeutic window (paragraph 0034). Raue teaches the CD40 agonist moiety as attached to the C-terminus or the N-terminus of the dendritic cell binding moiety (paragraph 0096). Raue teaches the molecule comprises one or more CD40L domain wherein a CD40L domain is defined as residues 108-261 of SEQ ID NO: 32 (paragraph 0025-26). Raue’s SEQ ID NO: 32 is defined in Table 3 and in particular pages 40-41 and matches instant SEQ ID NO: 19 (pg. 41 second row of table).
Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the fusion protein of Wu with the CD40L of Raue to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Raue explicitly teaches a CD40L that can advantageously result in increased efficacy, decreased toxicity, and an increased therapeutic window to treat CD40 related disorders.
Neither Wu nor Raue explicitly teaches the translocation domain is Shiga toxin translocation peptide.
However, Poma teaches protease-cleavage resistant molecules comprising Shiga toxin effector polypeptides capable of exhibiting potent, Shiga toxin functions (e.g. subcellular routing and cytotoxicity) and capable of targeting specific cells for the treatment of a variety of diseases (see abstract). Poma also teaches the hydrophobic region around 224 to 241 in the carboxy-terminal region of the A1 fragment of StxA is believed to play a role in the retrotranslocation of the A1 fragment from the lumen of the endoplasmic reticulum to the cytosol (see col 4; see also col 6). Poma further teaches a Stx tanslocation domain with 100% identity to SEQ ID NO: 12.
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Therefore, it would have been prima facie obvious to one of ordinary skill to modify the fusion protein of Wu and Raue and include the Stx translocation peptide of Poma to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Poma explicitly teaches Stx translocation peptide capable of targeting specific cells for the treatment of a variety of diseases and plays a role in the retrotranslocation of the A1 fragment from the lumen of the endoplasmic reticulum to the cytosol.
Regarding claim 4-5, and 17 Poma teaches SEQ ID NO: 12 (see above).
Regarding claim 6, Wu further teaches the cathepsin linker sequence of RXRXKR in SEQ ID NO: 15 on page 5 in Table 1 and in paragraph 0114 (i.e., the linker is 4-20 amino acids long as interpreted above).
Regarding claim 7, Wu teaches the cleavage site is within a peptide linker and adjacent to the CD binding domain and translocation domain (paragraph 0095, 113-114).
Regarding claim 8-9, and 19, Raue teaches CD40L 100% identical to SEQ ID NO: 19.
Regarding claim 14, Wu teaches a vaccine composition (i.e., a pharmaceutical composition) comprising: (a) a therapeutically effective amount of a fusion protein; and (b) an adjuvant (paragraph 0048-49).
Regarding claim 18, the combination of Wu, Raue, and Poma teaches the fusion protein of claim 18.
Regarding claim 21, Wu teaches the antigen can be a fusion antigen of two antigenic polypeptides (see paragraph 0102).
Accordingly, the claimed invention was prima facie obvious to one of ordinary skill in the art the time of filing, especially in the absence of evidence to the contrary.
Second rejection
Claims 22 is rejected under 35 U.S.C. 103 as being unpatentable over Wu, Raue, and Poma as applied to claims 1, 4-9, 14, 17-19, and 21 above, and further in view of Keller et al (US 20200325182 A1).
As discussed above, claims 1, 4-9, 14, 17-19, and 21 were rendered prima facie obvious by the combined teachings of Wu, Raue, and Poma.
None of the references teach that the antigen of a pathogen is ASFV CP204L, ASFV E183L, fusion of the preceding antigens, or fusion antigen of CSFV E2 and NS3p.
However, Keller teaches various gD:antigen fusion proteins containing antigens of pathogens, including ASFV (see abstract, claim 1, paragraph 100-102) to for vaccines or to treat ASFV in pigs (paragraph 0137). Keller teaches that there can be one or more ASFV antigens included in the fusion protein (paragraph 0528), including E183L and CP204L (see paragraph 0925).
Therefore, it would have been prima facie obvious to one of ordinary skill to modify the fusion protein of Wu, Raue, and Poma by including the ASFV antigens as taught by Keller to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Keller teaches various ASFV antigens (including E183L and CP204L) capable of use in a therapeutic and advantageously treat ASFV or vaccinate against it.
Accordingly, the claimed invention was prima facie obvious to one of ordinary skill in the art the time of filing, especially in the absence of evidence to the contrary.
Third rejection
Claim 23 is rejected under 35 U.S.C. 103 as being unpatentable over Wu, Raue, and Poma as applied to claims 1, 4-9, 14, 17-19, and 21 above, and further in view of Ellmark et al (WO2013034904; hereinafter Ellmark).
As discussed above, claims 1, 4-9, 14, 17-19, and 21 were rendered prima facie obvious by the combined teachings of Wu, Raue, and Poma.
None of the references teach using CD40-specific antibody comprising VH (CDR1-3) and VL (CDR1-3) where the VH CDR1 comprises SEQ ID NO: 24, SEQ ID NO: 25 and 26, and the VL CDR1, 2, and 3 are SEQ ID NO: 27-29.
However, Ellmark teaches antibodies (and fragments, variants, fusions and derivatives thereof) with multivalent binding specificity for CD40, which have a potency for dendritic cell activation which is higher than, or is equal to, the potency for B cell activation (see abstract). Ellmark teaches variable heavy (VH) and variable light (VL) domains of the antibody are involved in antigen recognition (see pg. 8) and use of CDR1-3 for the VH and VL for vaccines involving CD40 stimulation (pg. 2-3, 6). Ellmark explicitly teaches VH CDR1 (SEQ ID NO: 28) that has 100% sequence identity to SEQ ID NO: 24, and VH CDR 2-3 with 100% sequence identity with SEQ ID NOs: 25-26 and VL CDR1, 2, and 3 that have 100% sequence identity with SEQ ID NO: 27-29:
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SEQ ID NO 25-26 v. Ellmark
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SEQ ID NO: 27 vs Ellmark
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SEQ ID NO 28 v. Ellmark
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SEQ ID NO 29 v. Ellmark
Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the fusion protein of Wu, Raue, Poma with the VH and VL components of Ellmark to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Ellmark explicitly teaches VH and VL CDR components capable of providing multivalent specificity for CD40 for the treatment of various diseases (see abstract, pg. 4).
Accordingly, the claimed invention was prima facie obvious to one of ordinary skill in the art the time of filing, especially in the absence of evidence to the contrary.
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.
First rejection
Claims 1, 4-9, 14, 17-19 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 8-16 of U.S. Patent No. US 12358996 B2. Although the claims at issue are not identical, they are not patentably distinct from each other. Please note the conflicting claim language is bolded below.
Regarding claim 1 and 18, patent claim 1 and 10 teaches a fusion protein comprising: (a) a CD40-binding domain, which is a CD40 ligand (CD40L) or a functional fragment thereof comprising an amino acid sequence that is at least 90% identical to SEQ ID NO: 19, said CD40L or functional fragment thereof consists of 154-261 amino acids in length; (b) an antigen, which is a tumor antigen or an antigen of a pathogen, being located at the N-terminal of the fusion protein; (c) a translocation domain, located between the CD40-binding domain and the antigen, said translocation domain being a Shiga toxin (Stx) translocation peptide; and (d) a furin and/or cathepsin L cleavage site, located between the CD40-binding domain and the translocation domain. Patent claim 8 teaches many of the same species of pathogens as instantly claimed.
Regarding claim 4-5, 17, and 18 patent claim 2-3, 9, 11 teaches the Stx translocation peptide comprises an amino acid sequence that is at least 90% identical to the amino acid sequence selected from the group consisting of SEQ ID NOs: 12, 13, 14, 15 and 16, with 8-84 amino acid residues in length.
Regarding claim 6, patent claim 4-5 teaches furin or cathepsin L, the furin and/or cathepsin L cleavage site comprises an amino acid sequence of RX1X2R.
Regarding claim 7, patent claim 6 teaches the fusion protein further comprising a peptide linker, said peptide linker comprising the furin and/or cathepsin L cleavage site located between the CD40-binding domain and the translocation domain.
Regarding claim 9 and 19, claims 12-14 teach the CD40L or the functional fragment thereof comprises the amino acid sequence of SEQ ID NO: 19 (same SEQ ID NO 19 as instantly claimed).
Thus, it is clear that the claims are obvious variants of each other.
Second rejection
Claims 21-22 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 8-16 of U.S. Patent No. US 12358996 B2 in view of Wu and Keller. Although the claims at issue are not identical, they are not patentably distinct from each other.
As discussed above, claim 1 of the patent and instant claim 1 are obvious variants.
None of the patent claims teach using a fusion antigen comprising at least 2 antigenic polypeptides.
However, Wu teaches a fusion protein consisting of an antigen-presenting cell (APC) binding domain or a CD91 receptor-binding domain, an antigen of pathogen, and a translocation domain located between and immediately adjacent to the binding domain and the antigen (Abstract; see paragraph 0095). Wu explicitly teaches the antigen can be a fusion antigen of two antigenic polypeptides (see paragraph 0102).
Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the ‘996 patent with Wu because Wu teaches successful creation of fusion proteins containing one or more antigens for the creation of pharmaceutical therapeutic compositions.
Keller teaches various gD:antigen fusion proteins containing antigens of pathogens, including ASFV (see abstract, claim 1, paragraph 100-102) to for vaccines or to treat ASFV in pigs (paragraph 0137). Keller teaches that there can be one or more ASFV antigens included in the fusion protein (paragraph 0528), including E183L and CP204L (see paragraph 0925).
Therefore, it would have been prima facie obvious to one of ordinary skill to modify the fusion protein of the patent claims by including the ASFV antigens as taught by Keller to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Keller teaches various ASFV antigens (including E183L and CP204L) capable of use in a therapeutic and advantageously treat ASFV or vaccinate against it.
Thus, it is clear that the claims are obvious variants of each other.
Third rejection
Claim 23 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 8-16 of U.S. Patent No. US 12358996 B2 in view of Ellmark. Although the claims at issue are not identical, they are not patentably distinct from each other.
As discussed above, claim 1 of the patent and instant claim 1 are obvious variants.
None of the patent claims teach the fusion protein contaiing CD40-specific antibodies incuding VH and VL CDRs 1-3.
None of the references teach using CD40-specific antibody comprising VH (CDR1-3) and VL (CDR1-3) where the VH CDR1 comprises SEQ ID NO: 24, SEQ ID NO: 25 and 26, and the VL CDR1, 2, and 3 are SEQ ID NO: 27-29.
However, Ellmark teaches antibodies (and fragments, variants, fusions and derivatives thereof) with multivalent binding specificity for CD40, which have a potency for dendritic cell activation which is higher than, or is equal to, the potency for B cell activation (see abstract). Ellmark teaches variable heavy (VH) and variable light (VL) domains of the antibody are involved in antigen recognition (see pg. 8) and use of CDR1-3 for the VH and VL for vaccines involving CD40 stimulation (pg. 2-3, 6). Ellmark explicitly teaches VH CDR1 (SEQ ID NO: 28) that has 100% sequence identity to SEQ ID NO: 24, and VH CDR 2-3 with 100% sequence identity with SEQ ID NOs: 25-26 and VL CDR1, 2, and 3 that have 100% sequence identity with SEQ ID NO: 27-29:
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Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the claimed fusion protein with the VH and VL components of Ellmark to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Ellmark explicitly teaches VH and VL CDR components capable of providing multivalent specificity for CD40 for the treatment of various diseases (see abstract, pg. 4).
Thus, it is clear that the claims are obvious variants of each other.
Fourth rejection
Claims 1, 4-9, 14, and 17-19 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 7, 14, 27, 30, 33, 35, 37 of copending Application No. 17/240160 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding instant claim 1 and 18, copending claim 1 teaches fusion protein comprising:(a) a CD40-binding domain, consisting of a CD40 ligand (CD40L) monomer or a functional fragment thereof comprising an amino acid sequence that is at least 90% identical to SEQ ID NO: 19, said CD40L monomer or functional fragment thereof consisting of 154-261 amino acid residues in length and being located at the N-terminal of the fusion protein;(b) an antigen, which is a tumor antigen or an antigen of a pathogen;(c) a translocation domain, located between the CD40-binding domain and the antigen, said translocation domain being a Pseudomonas Exotoxin A (PE) translocation peptide; and(d) a furin and/or cathepsin L cleavage site, located immediately adjacent to the CD40-binding domain and the PE translocation peptide (see also copending claim 35). Claim 14 teaches the claimed pathogens.
None of the claims teach Shiga toxin translocation peptide (instant claim 1, 4-5, 18.
However, Poma teaches protease-cleavage resistant molecules comprising Shiga toxin effector polypeptides capable of exhibiting potent, Shiga toxin functions (e.g. subcellular routing and cytotoxicity) and capable of targeting specific cells for the treatment of a variety of diseases (see abstract). Poma also teaches the hydrophobic region around 224 to 241 in the carboxy-terminal region of the A1 fragment of StxA is believed to play a role in the retrotranslocation of the A1 fragment from the lumen of the endoplasmic reticulum to the cytosol (see col 4; see also col 6). Poma further teaches a Stx tanslocation domain with 100% identity to SEQ ID NO: 12.
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Therefore, it would have been prima facie obvious to one of ordinary skill to modify the fusion protein of ‘160 and include the Stx translocation peptide of Poma to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Poma explicitly teaches Stx translocation peptide capable of targeting specific cells for the treatment of a variety of diseases and plays a role in the retrotranslocation of the A1 fragment from the lumen of the endoplasmic reticulum to the cytosol.
Regarding instant claim 6, claim 7 and 33 teaches wherein the furin and/or cathepsin L cleavage site comprises an amino acid sequence of SEQ ID NO: 1 or 2.
Regarding claims 8-9, and 19, copending claim 27 and 37 teaches the amino acid sequence of the CD40 ligand comprises SEQ ID NO: 19.
Thus, it is clear the claims are obvious variants of each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Fifth rejection
Claim 21-22 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 7, 14, 27, 30, 33, 35, 37 of copending Application No. 17/240160 (reference application) in view of Wu and Keller. Although the claims at issue are not identical, they are not patentably distinct from each other.
As discussed above, claim 1 of the copending application and instant claim 1 are obvious variants.
None of the patent claims teach using a fusion antigen comprising at least 2 antigenic polypeptides.
However, Wu teaches a fusion protein consisting of an antigen-presenting cell (APC) binding domain or a CD91 receptor-binding domain, an antigen of pathogen, and a translocation domain located between and immediately adjacent to the binding domain and the antigen (Abstract; see paragraph 0095). Wu explicitly teaches the antigen can be a fusion antigen of two antigenic polypeptides (see paragraph 0102).
Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify ‘160 with Wu because Wu teaches successful creation of fusion proteins containing one or more antigens for the creation of pharmaceutical therapeutic compositions.
Keller teaches various gD:antigen fusion proteins containing antigens of pathogens, including ASFV (see abstract, claim 1, paragraph 100-102) to for vaccines or to treat ASFV in pigs (paragraph 0137). Keller teaches that there can be one or more ASFV antigens included in the fusion protein (paragraph 0528), including E183L and CP204L (see paragraph 0925).
Therefore, it would have been prima facie obvious to one of ordinary skill to modify the fusion protein of ‘160 by including the ASFV antigens as taught by Keller to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Keller teaches various ASFV antigens (including E183L and CP204L) capable of use in a therapeutic and advantageously treat ASFV or vaccinate against it.
Thus, it is clear that the claims are obvious variants of each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Sixth rejection
Claim 23 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 7, 14, 27, 30, 33, 35, 37 of copending Application No. 17/240160 (reference application) in view of Ellmark.
As discussed above, claim 1 of ‘160 and instant claim 1 are obvious variants.
None of the claims teach the fusion protein contaiing CD40-specific antibodies incuding VH and VL CDRs 1-3.
None of the references teach using CD40-specific antibody comprising VH (CDR1-3) and VL (CDR1-3) where the VH CDR1 comprises SEQ ID NO: 24, SEQ ID NO: 25 and 26, and the VL CDR1, 2, and 3 are SEQ ID NO: 27-29.
However, Ellmark teaches antibodies (and fragments, variants, fusions and derivatives thereof) with multivalent binding specificity for CD40, which have a potency for dendritic cell activation which is higher than, or is equal to, the potency for B cell activation (see abstract). Ellmark teaches variable heavy (VH) and variable light (VL) domains of the antibody are involved in antigen recognition (see pg. 8) and use of CDR1-3 for the VH and VL for vaccines involving CD40 stimulation (pg. 2-3, 6). Ellmark explicitly teaches VH CDR1 (SEQ ID NO: 28) that has 100% sequence identity to SEQ ID NO: 24, and VH CDR 2-3 with 100% sequence identity with SEQ ID NOs: 25-26 and VL CDR1, 2, and 3 that have 100% sequence identity with SEQ ID NO: 27-29:
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Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the fusion protein of ‘160 with the VH and VL components of Ellmark to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Ellmark explicitly teaches VH and VL CDR components capable of providing multivalent specificity for CD40 for the treatment of various diseases (see abstract, pg. 4).
Seventh rejection
Claim 1, 4-9, 14, 17-18 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-8, 10, 12, 18-19 of copending Application No. 18/697859 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding claim 1, 7-9 and 18-19, copending claim 1 teaches a fusion protein, comprising: (i) a CD40-binding domain, which is a CD40 ligand (CD40L) or a functional fragment thereof comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 19, said CD40L or functional fragment thereof consisting of 154-261 amino acid residues in length; (ii) an antigen, which is a tumor antigen or an antigen of a pathogen; (iii) a translocation domain, located between the CD40-binding domain and the antigen, said translocation domain being selected from the group consisting of: (iii-1) a Shiga toxin (Stx) translocation peptide; and (iii-2) a Pseudomonas Exotoxin A (PE) translocation peptide; and (iv) a furin and/or cathepsin L cleavage site, located between the CD40-binding domain and the translocation domain, wherein when the translocation domain is the Stx translocation peptide, the antigen is located at the N-terminal of the fusion protein; and when the translocation domain is the PE translocation peptide, the CD40-binding domain is a CD40L monomer and located at the N-terminal of the fusion protein. Claim 12 teaches the species of pathogen antigens.
Regarding instant claim 4-5, 17, and 18, copending claim 4 and 5teaches the translocation domain is the Stx translocation peptide, the Stx translocation peptide consisting of 8-84 amino acid residues in length and comprising an amino acid sequence that is at least 95% identical to the amino acid sequence selected from the group consisting of SEQ ID NOs: 12, 13, 14, 15 and 16.
Regarding claim 6 and 7, copending claim 7 and 8 teach the furin and/or cathepsin L cleavage site comprises an amino acid sequence of SEQ ID NO: 1 or 2, and further comprising a peptide linker, wherein the furin and/or cathepsin L cleavage site is present in said peptide linker.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Eighth rejection
Claims 21-22 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-8, 10, 12, 18-19 of copending Application No. 18/697859 (reference application) in view of Wu and Keller. Although the claims at issue are not identical, they are not patentably distinct from each other.
As discussed above, claim 1 of the copending application and instant claim 1 are obvious variants.
None of the patent claims teach using a fusion antigen comprising at least 2 antigenic polypeptides.
However, Wu teaches a fusion protein consisting of an antigen-presenting cell (APC) binding domain or a CD91 receptor-binding domain, an antigen of pathogen, and a translocation domain located between and immediately adjacent to the binding domain and the antigen (Abstract; see paragraph 0095). Wu explicitly teaches the antigen can be a fusion antigen of two antigenic polypeptides (see paragraph 0102).
Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the ‘859 with Wu because Wu teaches successful creation of fusion proteins containing one or more antigens for the creation of pharmaceutical therapeutic compositions.
Keller teaches various gD:antigen fusion proteins containing antigens of pathogens, including ASFV (see abstract, claim 1, paragraph 100-102) to for vaccines or to treat ASFV in pigs (paragraph 0137). Keller teaches that there can be one or more ASFV antigens included in the fusion protein (paragraph 0528), including E183L and CP204L (see paragraph 0925).
Therefore, it would have been prima facie obvious to one of ordinary skill to modify the fusion protein of ‘859 claims by including the ASFV antigens as taught by Keller to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Keller teaches various ASFV antigens (including E183L and CP204L) capable of use in a therapeutic and advantageously treat ASFV or vaccinate against it.
Thus, it is clear that the claims are obvious variants of each other.
Ninth rejection
Claim 23 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-8, 10, 12, 18-19 of copending Application No. 18/697859 (reference application) in view of Ellmark. Although the claims at issue are not identical, they are not patentably distinct from each other.
As discussed above, claim 1 of the copending application and instant claim 1 are obvious variants.
None of the patent claims teach the fusion protein contaiing CD40-specific antibodies incuding VH and VL CDRs 1-3.
None of the references teach using CD40-specific antibody comprising VH (CDR1-3) and VL (CDR1-3) where the VH CDR1 comprises SEQ ID NO: 24, SEQ ID NO: 25 and 26, and the VL CDR1, 2, and 3 are SEQ ID NO: 27-29.
However, Ellmark teaches antibodies (and fragments, variants, fusions and derivatives thereof) with multivalent binding specificity for CD40, which have a potency for dendritic cell activation which is higher than, or is equal to, the potency for B cell activation (see abstract). Ellmark teaches variable heavy (VH) and variable light (VL) domains of the antibody are involved in antigen recognition (see pg. 8) and use of CDR1-3 for the VH and VL for vaccines involving CD40 stimulation (pg. 2-3, 6). Ellmark explicitly teaches VH CDR1 (SEQ ID NO: 28) that has 100% sequence identity to SEQ ID NO: 24, and VH CDR 2-3 with 100% sequence identity with SEQ ID NOs: 25-26 and VL CDR1, 2, and 3 that have 100% sequence identity with SEQ ID NO: 27-29:
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Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the fusion protein ‘859 with the VH and VL components of Ellmark to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Ellmark explicitly teaches VH and VL CDR components capable of providing multivalent specificity for CD40 for the treatment of various diseases (see abstract, pg. 4).
Tenth rejection
Claim 1, 4-9, 14, 17-19 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-3, 6-8, 14 of copending Application No. 18/698008 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding claim 1, 7-9 and 18-19, copending claim 1 teaches a fusion protein comprising: (a) a CD40-binding domain, which is a CD40 ligand (CD40L) or a functional fragment thereof comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 19, said CD40L or functional fragment thereof consisting of 154-261 amino acid residues in length; (b) an antigen of severe acute respiratory syndrome coronavirus 2 (SARS-CoV2); (c) a translocation domain, located between the CD40-binding domain and the antigen, said translocation domain being selected from the group consisting of: (c1) a Shiga toxin (Stx) translocation peptide; and (c2) a Pseudomonas Exotoxin A (PE) translocation peptide; and (d) a furin and/or cathepsin L cleavage site, located between the CD40-binding domain and the translocation domain, wherein when the translocation domain is the Stx translocation peptide, the antigen is located at the N-terminal of the fusion protein; and when the translocation domain is the PE translocation peptide, the CD40-binding domain is a CD40L monomer and located at the N-terminal of the fusion protein. Copending claim 7 teaches the CD40 ligand (CD40L) or the functional fragment thereof comprises the amino acid sequence of SEQ ID NO: 19 with 154-261 amino acid residues in length.
Regarding claim 4-5 and 17-18, copending claim 2 teaches the translocation domain is the Stx translocation peptide, the Stx translocation peptide consisting of 8-84 amino acid residues in length and comprising an amino acid sequence selected from the group consisting of SEQ ID NOs:12, 13, 14, 15 and 16.
Regarding claim 6, copending claim 6 teaches the furin and/or cathepsin L cleavage site comprises an amino acid sequence of SEQ ID NO: 1 or 2.
Regarding claim 14, copending claim 14 teaches the pharmaceutical composition.
Thus, the claims are clearly obvious variants of each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Eleventh rejection
Claim 21-22 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-3, 6-8, 14 of copending Application No. 18/698008 (reference application) in view of Wu and Keller.
As discussed above, claim 1 of the copending application and instant claim 1 are obvious variants.
None of the claims teach using a fusion antigen comprising at least 2 antigenic polypeptides.
However, Wu teaches a fusion protein consisting of an antigen-presenting cell (APC) binding domain or a CD91 receptor-binding domain, an antigen of pathogen, and a translocation domain located between and immediately adjacent to the binding domain and the antigen (Abstract; see paragraph 0095). Wu explicitly teaches the antigen can be a fusion antigen of two antigenic polypeptides (see paragraph 0102).
Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify ‘008 with Wu because Wu teaches successful creation of fusion proteins containing one or more antigens for the creation of pharmaceutical therapeutic compositions.
Keller teaches various gD:antigen fusion proteins containing antigens of pathogens, including ASFV (see abstract, claim 1, paragraph 100-102) to for vaccines or to treat ASFV in pigs (paragraph 0137). Keller teaches that there can be one or more ASFV antigens included in the fusion protein (paragraph 0528), including E183L and CP204L (see paragraph 0925).
Therefore, it would have been prima facie obvious to one of ordinary skill to modify the fusion protein of ‘008 by including the ASFV antigens as taught by Keller to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Keller teaches various ASFV antigens (including E183L and CP204L) capable of use in a therapeutic and advantageously treat ASFV or vaccinate against it.
Thus, it is clear that the claims are obvious variants of each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Twelvth rejection
Claim 23 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-3, 6-8, 14 of copending Application No. 18/698008 (reference application) in view of Ellmark.
As discussed above, claim 1 of the copending application and instant claim 1 are obvious variants.
None of the copending claims teach the fusion protein contaiing CD40-specific antibodies incuding VH and VL CDRs 1-3.
None of the references teach using CD40-specific antibody comprising VH (CDR1-3) and VL (CDR1-3) where the VH CDR1 comprises SEQ ID NO: 24, SEQ ID NO: 25 and 26, and the VL CDR1, 2, and 3 are SEQ ID NO: 27-29.
However, Ellmark teaches antibodies (and fragments, variants, fusions and derivatives thereof) with multivalent binding specificity for CD40, which have a potency for dendritic cell activation which is higher than, or is equal to, the potency for B cell activation (see abstract). Ellmark teaches variable heavy (VH) and variable light (VL) domains of the antibody are involved in antigen recognition (see pg. 8) and use of CDR1-3 for the VH and VL for vaccines involving CD40 stimulation (pg. 2-3, 6). Ellmark explicitly teaches VH CDR1 (SEQ ID NO: 28) that has 100% sequence identity to SEQ ID NO: 24, and VH CDR 2-3 with 100% sequence identity with SEQ ID NOs: 25-26 and VL CDR1, 2, and 3 that have 100% sequence identity with SEQ ID NO: 27-29:
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Therefore, it would have been prima facie obvious to one of ordinary skill at the time of filing to modify the fusion protein of ‘008 with the VH and VL components of Ellmark to arrive at the claimed invention. One of ordinary skill would have been motivated to make the modification because Ellmark explicitly teaches VH and VL CDR components capable of providing multivalent specificity for CD40 for the treatment of various diseases (see abstract, pg. 4).
Thus, it is clear that the claims are obvious variants of each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
NO CLAIMS ALLOWED.
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure:
Ahmed (WO 2012096994 A2)
Tang et al (WO 2007056266 A2)
Tykocinski et al (US 10533054 B2)
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/G.C.R./Examiner, Art Unit 1651
/THOMAS J. VISONE/Supervisory Patent Examiner, Art Unit 1672