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 .
Response to Amendment
The Amendment filed 03/10/2026 in which claims 1, 19, 21 were amended, new claims 30-36 was added, and claims 20, 22, 23, 25, 28 were canceled, has been entered. Claims 2-18 were previously canceled.
Claims 1, 19, 21, 24, 26, 27, 29-36 are under examination on the merits.
Claim Rejections - 35 USC § 112 - Written Description
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.
(Previous rejection, withdrawn as to claims 20, 22, 23, 25, 28; maintained and modified as necessitated by amendment as to claims 1, 19, 21, 24, 26, 27, 29; expanded as to new claims 30-36) Claims 1, 19, 21, 24, 26, 27, 29, 30-36 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.
See claims 1, 19-36 as submitted on 03/10/2026.
The previous rejections of claims 20, 22, 23, 25, 28 are moot in view of Applicant’s cancelation of these claims.
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.
The Federal Circuit has clarified the application of the written description requirement to inventions in the field of biotechnology. See University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568,43 USPQ2d l398, 1406 (Fed. Cir. 1997). The Court stated that a written description of an invention requires a precise definition, one that defines the structural features of the chemical genus that distinguishes it from other chemical structures. A definition by function does not suffice to define the genus because it is only an indication of what the genus does, rather than what it is. Further, the Court held that to adequately describe a claimed genus, an applicant must describe a representative number of species of the claimed genus, and that one of skill in the art should be able to “visualize or recognize the identity of the members of the genus.”
The instant claims (amended claims 1, 19, 21, 24, 26, 27, 29, and new claims 30-36) require explicitly or inherently a CMV protein having an amino acid sequence of a coat protein of CMV or an amino acid sequence of SEQ ID NO: 62, and having the ability to coat a virus-like particle. The instant claims alternatively require explicitly or inherently a CMV protein wherein sequence alterations such as substitutions, additions, insertions, or deletions of one or more amino acids can be made anywhere in the amino acid sequence of SEQ ID NO: 62, including specific regions essential for coat assembly, provided that a CMV protein bears at least 90% sequence homology to SEQ ID NO: 62. Regarding the amendment filed on 03/10/2026, it is noted that the instant claims require a CMV protein bearing at least 90% sequence homology to SEQ ID NO: 62. However, the Specification has failed to sufficiently describe the structural features that must be retained by members of the claimed genus as to establish a structure-function relationship with respect to virus-like particle coating.
SEQ ID NO: 62, e.g., is 218 amino acids long. The amended claims encompass any sequence having at least 90% sequence identity to SEQ ID NO: 62. An amino acid sequence sharing only 90% identity relative to SEQ ID NO: 62 could have anywhere from 1 to 21 substitutions, deletions, or additions in any combination along any length of SEQ ID NO: 62, which still corresponds to a massive genus (2021 = 2.1 x 1027) comprising trillions upon trillions of sequences, with respect to SEQ ID NO: 62 alone.
However, while the claims are drawn to a genus that comprises innumerable sequences, the Specification has only adequately described and successfully reduced to practice the full-length of SEQ ID NO: 62. This is not representative of the extremely large genus of sequences claimed, since no variants, mutants, etc. of SEQ ID NO: 62 are demonstrated to have virus-like particle coating ability.
At best, the Specification contemplates the use of BLAST to identify functional homologs based on sequence homology. However, this is not sufficient to describe members of the claimed genus because such methods access online databases that are continually being updated as sequencing technology improves. As a result, they are not a static source of information. Thus, one of skill in the art would readily appreciate that relying on a non-patent source that is continuously subject to change as a means to identify members of the claimed genus does not sufficiently meet the written description requirement.
Moreover, Friedberg (“Automated protein function prediction--the genomic challenge”. Brief Bioinform. 2006;7(3):225-242.) teach that homology-based transfer is not reliable for functional annotation even with high alignment percentages (page 227, second column). Friedberg also teach that identification of functionally significant sub-regions is critical to functional annotation, and that often addition, deletion, or re-shuffling of domains can lead to errors in annotation (page 227, second column; page 228, first paragraph). Furthermore, Friedberg teach that sequence-based tools are just not sensitive enough to identify functional protein similarity as databases get larger, and diversity of sequences gets larger (page 228, first full paragraph).
Thorton (“Structural genomics takes off.” Trends Biochem Sci. 2001;26(2):88-89.) teach that the same protein structure is often seen in apparently different homologous families with different functions. Thorton further describes examples of little correlation between specific binding function and overall protein structure (page 992, right column, at lines 2-10). Thus, when taken with the teachings of Friedberg and Thorton, one of skill in the art would readily appreciate that sequence homology alone cannot serve as the basis to describe members of the genus that have the recited function.
In the absence of a representative number of examples, the Specification must at least describe the structural features that are required for the claimed function, in this case virus-like particle coating ability. However, as discussed above, the Specification fails to describe any substantive structural limitations as to establish a structure-function relationship with respect to virus-like particle coating ability.
Accordingly, the claims as currently written are not adequately described and one of skill in the art would readily appreciate that Applicant was not in possession of the claimed genus at the time of filing.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
(Previous rejection, withdrawn as to claims 19-26) Claims 19-26 were rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 1. In the Applicant may cancel the claims, amend the claims to place the claims in proper dependent form, rewrite the claims in independent form, or present a sufficient showing that the dependent claims complies with the statutory requirements.
See claims 19-26 as submitted on 03/10/2026.
The previous rejections of claims 20, 22, 23, 25, are moot in view of Applicant’s cancelation of these claims.
Applicant’s amendment to the instant claims filed on 03/10/2026 has overcome previous rejection to claims 19, 21, 24, 26.
Claim Rejections - 35 USC § 103
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.
(Previous rejection, withdrawn as to claims 20, 22, 23, 25, 28; maintained and modified as necessitated by amendment as to claims 1, 19, 21, 24, 26, 27, 29) Claims 1, 19, 21, 24, 26, 27, 29 are rejected under 35 U.S.C. 103 as being unpatentable over Bachmann et al., in view of Natilla et al., further in view of Kramer et al. (prior art of record).
See claims 1, 19-29 as submitted on 03/10/2026.
The previous rejections of claims 20, 22, 23, 25, 28 are moot in view of Applicant’s cancelation of these claims.
Regarding claim 1, the amended claim as filed on 03/10/2026 requires a modified virus-like particle (VLP) of mosaic cucumber virus (CMV) comprising two elements listed in clauses (a) and (b). The limitations of clauses (a) and (b) are addressed below in relation to the teachings of Bachmann et al., Natilla et al. and Kramer et al. which have been explained in detail previously.
First, in reference to claim 1 clause (a) as explained in detail previously, Bachmann et al. teach a modified virus-like particles (VLPs) of plant virus Cucumber Mosaic Virus (CMV) (¶ [0047]). The teachings of Bachmann et al. encompass virus-like particles comprising more than one species of polypeptides, often referred to as mosaic VLPs (¶ [0047]). In one embodiment the VLPs of Bachmann et al. comprise at least two different species of polypeptides (¶¶ [0047], [0014]). Bachmann et al. further teach one of said species of polypeptide is an inventive polypeptide and comprises a fusion protein comprising a CMV protein and an antigen wherein the antigen may be associated, bound, mixed with or linked to the virus-like particle (¶¶ [0074]-[0078], [0220]).
Claim 1 clause (a) requires SEQ ID NO:29 in instant application which is 398 amino acid residues long and it refers to the amino acid sequence for a chimeric VLP of CMV (CMV-Ntt830-Ara-h202) comprising the CMV-Ntt830 vector (SEQ ID NO: 5 of instant application) and the Ara-h202 gene as the antigen. The insertion of the Ara-h202 gene into the CMV-Ntt830 vector (instant SEQ ID NO: 5) is as follows:
A first GS linker (amino acid residues 89-103 of SEQ ID NO:29)
The Ara-h202 gene (amino acid residues 104-254 of SEQ ID NO:29)
A second GS linker (amino acid residues 255-103 of SEQ ID NO:29)
As previously explained, Bachmann et al. teach an amino acid sequence for the CMV-Ntt830 construct SEQ ID NO:6 (example 3) which has 100% sequence identity to the CMV-Ntt830 vector of instant application (instant SEQ ID NO:5) (file alignment of record). Bachmann et al. further teach a peanut allergen termed Ara-h202 as the antigenic polypeptide (¶ [0168]), and GS linkers for attachment to the antigenic polypeptide (¶ [0134 (g)-(o)]).
Natilla et al. teach the insertion of the antigenic polypeptide between amino acid positions 88 and 89 of the CMV-Ntt830 (page 143) as previously explained.
Neither Bachmann et al. nor Natilla et al. teach an amino acid sequence for the Ara-h202 gene.
However, Kramer et al. teach immunogenic vaccine compositions comprised of CMV VLPs for the prevention and treatment of peanut allergy in humans (abstract, page 2). Kramer et al. further teach an amino acid sequence for the peanut allergen Ara-h202 gene coupled with CMV-Ntt830 VLPs (example 13, 14, Fig. 13B). The amino acid sequence for the Ara-h202 protein in Kamer et al.’s teachings, SEQ ID NO:18, has 100% sequence identify to the amino acid sequence for the Ara-h202 protein SEQ ID NO:27 in instant application (see sequence alignment file of record: “US-17-414-730-27_pep__vs__US-16-097-182-18_pep__align.pdf.)
Therefore, the 398 amino acid long CMV-Ntt830-Arah202 sequence of SEQ ID NO:29 in claim 1 (a) is an obvious embodiment of the sequences of the cited prior art as illustrated by the following:
amino acid residues 1-88 in SEQ ID NO:29 have 100% sequence identity to amino acid residues 1-88 in SEQ ID NO:6 (CMV-Ntt830) vector from Bachmann et al. see sequence alignment file of record: “US-17-414-730-29-aa1-88_pep__vs__US-15-520-676-aa1-88_pep__align.pdf.”
amino acid residues 89-103 of SEQ ID NO:29 refer to a first GS linker, as previously indicated the N-terminal GS linker is taught by Bachmann et al.’s formula.
amino acid residues 104-254 in SEQ ID NO:29 refer to the Ara-h202 gene which has 100% sequence identity to the Ara-h202 protein in Kamer et al.’s teachings, SEQ ID NO:18. Alignment file of record.
amino acid residues 255-264 of SEQ ID NO:29 refer to a second GS linker, as previously indicated the C-terminal GS linker is taught by Bachmann et al.’s formula.
amino acid residues 265-398 in SEQ ID NO:29 have 100% sequence identity to amino acid residues 89-222 in SEQ ID NO:6 (CMV-Ntt830) vector from Bachmann et al. See sequence alignment file of record: “US-17-414-730-29-aa265-398_pep__vs__US-15-520-676-aa89-222_pep__align.pdf.”
The insertion point between amino acid positions 88 and 89 of the CMV-Ntt830 was taught by Natilla et al., as previously explained.
It would have been prima facie obvious to a person of ordinary skill in the art, at the time of filing, to have included the teachings of Kramer et al. in the CMV VLP construct as taught by Bachmann et al. in view of Natilla et al. given that Bachmann et al. teach a peanut allergen Ara-h202 as the antigenic polypeptide (¶ [0168]) and the incorporation of flanking GS linkers, and Natilla et al. teach the insertion site in the CMV coat protein. One of ordinary skill in the art would have been motivated to include the Ara-h202 gene in the CMV VLP of Bachmann et al. in view Natilla et al. for the benefit of expressing a peanut allergen on the surface of each chimeric CMV VLP particle for the advantage of formulating chimeric CMV VLP with potential for preventing and treating peanut allergy in humans as taught by Kramer et al. See MPEP 2144.07. The selection of a known material based on its suitability for its intended use supported a prima facie obviousness determination in Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945).
One of ordinary skill in the art would have had a reasonable expectation of success for introducing the Ara-h202 gene from Kramer et al. into the CMV VLP particles of Bachmann et al. in view of Natilla et al. There would have been a reasonable expectation of success given that the methods of VLP cloning and expression are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Second, in reference to claim 1 clause (b), the amendment submitted on 03/10/2026 recites “(b) at least one CMV protein, wherein said CMV protein consists of a coat protein of CMV or an amino acid sequence having a sequence identity of at least 90% with SEQ ID NO:62, and wherein said CMV protein is optionally modified by a T helper cell epitope”. It is noted that the term “consists of” in the above clause is being interpreted herein as excluding any element not specified in the above clause. As explained in detail previously, Bachmann et al. already teach this limitation. Specifically, Bachmann et al. teach:
A VLP of CMV comprising more than one species of polypeptides, often referred to as mosaic VLPs (¶ [0047]) wherein at least one of said species of polypeptides consists of a CMV coat protein modified by a T helper cell epitope (¶¶ [0047], [0014]). Bachmann et al. further teach SEQ ID NO:1 which discloses a sequence of the coat protein of CMV which shares 100% sequence identity to instant SEQ ID NO:62 and is of the same length as instant SEQ ID NO:62 (218 amino acid residues long); see sequence alignment file of record: “US-17-414-730-62_pep__vs__AASEQ2_US 15-520-676-1_pep__align.pdf”
A T helper cell epitope, wherein said T helper cell epitope replaces a N-terminal region of said CMV polypeptide (¶¶ [0058], [ 0112])
Accordingly, the teachings of Bachmann et al. meet the amended limitation in claim 1 clause (b).
Regarding claims 19, 21, 24, 26, the teachings of Bachmann et al. explained above teach the limitations of claims 19-26 because Bachmann et al. teach a CMV coat protein sequence of the same length (218 amino acid residues long) with 100% identity to instant SED ID NO: 62, see sequence alignment file of record: “US-17-414-730-62_pep__vs__AASEQ2_US 15-520-676-1_pep__align.pdf”
Regarding claim 27, it is noted that no amendments were introduced to claim 27 in the amendment filed on 03/10/2026. As previously explained, Bachmann et al. further teach a modified VLP of CMV, wherein the T helper cell epitope is derived from tetanus toxin (claim 21), wherein the T helper cell epitope comprises the amino acid sequence SEQ ID NO: 4 which has 100% sequence identity to SEQ ID NO:64 in instant application (¶ [0118]); see sequence alignment file of record: “AASEQ1_US 15-520-676-4__vs__US-17-414-730-64_pep__align.pdf”. Bachmann et al. further teach wherein said T helper cell epitope replaces the N-terminal region of said CMV polypeptide, and wherein said replaced N-terminal region of said CMV polypeptide consists of 11 to 13 consecutive amino acids, preferably of 11 consecutive amino acids, and wherein further preferably said N-terminal region of said CMV polypeptide corresponds to amino acids 2-12 of Bachmann et al.’s SEQ ID NO: 1 which has 100% identity to instant SEQ ID: 62 (see sequence alignment file of record cited above) (¶ [0119]).
Regarding claim 29, it is noted that no amendments were introduced to claim 29 in the amendment filed on 03/10/2026. As previously explained, Bachmann et al. teach a modified VLP of CMV, wherein the CMV protein consist of the amino acid sequence of SEQ ID NO: 6 (¶ [0120]), which has 100% sequence identity to SEQ ID NO: 5 in instant application (see sequence alignment file of record: “US-17-414-730-5_pep__vs__US-15-520-676-6_pep__align.pdf”). It is noted that both sequences are 666 amino acid residues long.
Accordingly, the limitations of claims 1, 19, 21, 24, 26, 27, 29 would have been prima facie obvious to one of ordinary skill in the art before the effective filing date especially in the absence of evidence to the contrary.
(New rejection, necessitated by addition of claims 30-36) Claims 30-36 are rejected under 35 U.S.C. 103 as being unpatentable over Bachmann et al., Natilla et al., and Kramer et al. (prior art of record) as applied to claims 1, 19, 21, 24, 26, 27, 29 above; further in view of Stothard P. The sequence manipulation suite: JavaScript programs for analyzing and formatting protein and DNA sequences. Biotechniques. 2000;28(6):1102-1104. ( See PTO-892: Notice of References Cited.)
See claims 30-36 as submitted on 03/10/2026.
Regarding new claims 30-36, it is noted that these claims require a chimeric CMV polypeptide encoded by instant SEQ ID NO: 32. The Specification at page 86 evidences that SEQ ID NO:32 is a nucleotide sequence corresponding to the preferred chimeric CMV polypeptide CMV-Ntt830-Arah202 of SEQ ID NO:29. As explained in detail above, the entire length of SEQ ID NO: 29 is already taught by the cited prior art.
Neither Bachmann et al., Natilla et al., nor Kramer et al. teach the sequence of SEQ ID NO: 32.
However, Stothard teaches digital tools free and readily available for molecular biologists to reverse translate an amino acid sequence into its corresponding nucleic acid sequence for applications in molecular biology (pages 1, 3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to have applied a reverse translation tool as taught by Stothard to arrive at instant SEQ ID NO: 32 from the amino acid sequence of SEQ ID NO: 29 as taught by Bachmann et al., Natilla et al., and Kramer et al. for the benefit of using such nucleic acid sequence in molecular biology applications such as vector cloning. See MPEP 2144.07. The selection of a known material based on its suitability for its intended use supported a prima facie obviousness determination in Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945).
One of ordinary skill in the art would have had reasonable expectation of success in reverse translating the amino acid sequence of SEQ ID NO: 29 to arrive at instant SEQ IF NO: 32 given that the methods of reverse translation well known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claims 31-36, as explained above in detail the limitations of these claims are already taught by Bachmann et al., who teach a CMV coat protein sequence of the same length (218 amino acid residues long) with 100% identity to instant SED ID NO: 62, see sequence alignment file of record: “US-17-414-730-62_pep__vs__AASEQ2_US 15-520-676-1_pep__align.pdf” (relevant to new claims 31-34). Bachmann et al. further teach a modified VLP of CMV, wherein the T helper cell epitope is derived from tetanus toxin (claim 21), wherein the T helper cell epitope comprises the amino acid sequence SEQ ID NO: 4 which has 100% sequence identity to SEQ ID NO:64 in instant application (¶ [0118]); see sequence alignment file of record: “AASEQ1_US 15-520-676-4__vs__US-17-414-730-64_pep__align.pdf”. Bachmann et al. further teach wherein said T helper cell epitope replaces the N-terminal region of said CMV polypeptide, and wherein said replaced N-terminal region of said CMV polypeptide consists of 11 to 13 consecutive amino acids, preferably of 11 consecutive amino acids, and wherein further preferably said N-terminal region of said CMV polypeptide corresponds to amino acids 2-12 of Bachmann et al.’s SEQ ID NO: 1 which has 100% identity to instant SEQ ID: 62 (see sequence alignment file of record cited above) (¶ [0119]) (relevant to claim 35). Bachmann et al. teach a modified VLP of CMV, wherein the CMV protein consist of the amino acid sequence of SEQ ID NO: 6 (¶ [0120]), which has 100% sequence identity to SEQ ID NO: 5 in instant application (see sequence alignment file of record: “US-17-414-730-5_pep__vs__US-15-520-676-6_pep__align.pdf”) (relevant to claim 35).
Accordingly, the limitations of claims 30-36 would have been prima facie obvious to one of ordinary skill in the art before the effective filing date 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.
(Previous rejection, withdrawn as to claims 20, 22, 23, 25, 28; maintained and modified as necessitated by amendment as to claims 1, 19, 21, 24, 26, 27, 29; expanded as to claims 30-36) Claims 1, 19, 21, 24, 26, 27, 29-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 26, 27, 79, 80-85, 88, 90, 91 of copending application No.17/714307 in view of Natilla et al. and Stothard. It is noted that a Notice of Allowance was issues for the copending claims on 12/23/2025 in copending application No.17/714307. However, as of the present date of this Office Action, a Patent number has not been assigned. Although the claims at issue are not identical, they are not patentably distinct from each other because both sets of claims are directed to a modified VLP of CMV, wherein the VLP comprises a modified CMV polypeptide bearing a T helper cell epitope comprising the tetanus toxin, and an antigen that is linked to the VLP particles. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
See claims 1, 19, 21, 24, 26, 27, 29-36 as submitted on 03/10/2026.
The previous rejections of claims 20, 22, 23, 25, are moot in view of Applicant’s cancelation of these claims.
As to claims 1, 19, 21, 24, 26, 27, 29-36 of instant application, the copending claims in application ’307 are directed to: (a) a modified virus-like particle (VLP) of cucumber mosaic virus (CMV), wherein said modified VLP of CMV comprises a modified CMV amino acid sequence of a coat protein of CMV, (b) a T helper cell epitope, and (c) an antigen with at least one first and one second attachment sites.
The copending claims do not recite the insertion position of the antigenic polypeptide, wherein said insertion of said antigenic polypeptide is between amino acid residues of said CMV polypeptide corresponding to amino acid residues of position 84 (Ser) and position 85 (Tyr) of instant SEQ ID NO: 62 which shares 100% sequence identity with SEQ ID NO: 1 of the copending application. It is also noted that instant SEQ ID NO: 5 shares 100% sequence identity with SEQ ID NO: 6 of the copending application.
However, Natilla et al. teach a chimeric CMV VLP comprising an antigenic peptide, wherein the antigenic peptide is a R9 mimotope which was inserted within the CMV coat protein (CP) after nucleotide position 252 (page 143). Nucleotide position 252 corresponds to amino acid position 84 of the CMV coat protein. Therefore the insertion point is between amino acid residues of position 84 (Ser) and position 85 (Tyr) of the CMV coat protein (or SEQ ID NO:62, as recited in claim 1), (as noted above, SEQ ID NO:62 discloses a sequence for the CMV coat protein as per instant application specification page 17), for the advantage of expressing high number of copies of a foreign peptide on the surface of chimeric CMV VLP particles (page 151).
Stothard is cited for teaching reverse translation tools to arrive at instant SEQ ID NO: 32 from the amino acid sequence of SEQ ID NO: 29 as taught by Bachmann et al., and Kramer et al.
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have included the teachings of Natilla et al. in the CMV VLP construct as recited by the copending claims in application ’307, for the benefit of expressing high number of copies of an antigenic peptides on the surface of each chimeric CMV VLP particle. Further, would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have included the teachings of Stothard to arrive at instant SEQ ID NO: 32 from the amino acid sequence of SEQ ID NO: 29 as taught by Bachmann et al., and Kramer et al.
(previous rejection, withdrawn as to claims 20, 22, 23, 25, 28; maintained and modified as necessitated by amendment as to claims 1, 19, 21, 24, 26, 27, 29; expanded as to claims 30-36) Claims 1, 19, 21, 24, 26, 27, 29-36 as submitted on 03/10/2026 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of U.S. patent 10,898,569 B2 to Kramer et al. dated 01/26/2021 in view of Natilla et al. and Stothard. Although the claims at issue are not identical, they are not patentably distinct from each other because both sets of claims are directed to a modified VLP of CMV, wherein the VLP comprises a modified CMV polypeptide bearing a T helper cell epitope comprising the tetanus toxin, and an antigen that is linked to the VLP particles.
See claims 1, 19, 21, 24, 26, 27, 29-36 as submitted on 03/10/2026.
The previous rejections of claims 20, 22, 23, 25, are moot in view of Applicant’s cancelation of these claims.
As to claims 1, 19, 21, 24, 26, 27, 29-36 of the instant application, the patented claims are directed to: (a) a modified virus-like particle (VLP) of cucumber mosaic virus (CMV), wherein said modified VLP of CMV comprises a modified CMV amino acid sequence of a coat protein of CMV, (b) a T helper cell epitope derived from tetanus toxin, and (c) an antigen with at least one first and one second attachment sites, wherein the allergen is a peanut allergy consisting of SEQ ID NO:18 (which has 100% sequence identity to amino acid residues 104-254 of SEQ ID NO:29 of instant application. Alignment file of record).
The patented claims do not recite the insertion position of the antigenic polypeptide, wherein said insertion of said antigenic polypeptide is between amino acid residues of said CMV polypeptide corresponding to amino acid residues of position 84 (Ser) and position 85 (Tyr) of SEQ ID NO:62 which shares 100% sequence identity with SEQ ID NO: 1 of the patent.
However, as indicated above, Natilla et al. teach a chimeric CMV VLP comprising an antigenic peptide, wherein the antigenic peptide is a R9 mimotope which was inserted within the CMV coat protein (CP) after nucleotide position 252 (page 143). Nucleotide position 252 corresponds to amino acid position 84 of the CMV coat protein. Therefore the insertion point is between amino acid residues of position 84 (Ser) and position 85 (Tyr) of the CMV coat protein (or SEQ ID NO:62, as recited in claim 1), (as noted above, SEQ ID NO:62 discloses a sequence for the CMV coat protein as per instant application specification page 17), for the advantage of expressing high number of copies of a foreign peptide on the surface of chimeric CMV VLP particles (page 151).
Stothard is cited for teaching reverse translation tools to arrive at instant SEQ ID NO: 32 from the amino acid sequence of SEQ ID NO: 29 as taught by Bachmann et al., and Kramer et al.
It would have been prima facie obvious to a person of ordinary skill in the art, at the time of filing, to have included the teachings of Natilla et al. in the CMV VLP construct as recited by the patented claims for the benefit of expressing high number of copies of an antigenic peptides on the surface of each chimeric CMV VLP particle.
The sets of claims differ in scope; the claims in instant application indicated above refer to a product (modified CMV VLPs), while the patented claims indicated above refer to a composition.
(previous rejection, withdrawn as to claims 20, 22, 23, 25, 28; maintained and modified as necessitated by amendment as to claims 1, 19, 21, 24, 26, 27, 29; expanded as to claims 30-36) Claims 1, 19, 21, 24, 26, 27, 29-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 8, 9, 13, 15 of U.S. patent 11,324, 836 B2 to Bachmann et al. dated 05/10/2022 in view of Natilla et al. and Stothard. Although the claims at issue are not identical, they are not patentably distinct from each other because both sets of claims are directed to a modified VLP of CMV, wherein the VLP comprises a modified CMV polypeptide bearing a T helper cell epitope comprising the tetanus toxin, and an antigen that is linked to the VLP particles.
See claims 1, 19, 21, 24, 26, 27, 29-36 as submitted on 03/10/2026.
As to claims 1, 19, 21, 24, 26, 27, 29-36 of the instant application, the patented claims are directed to: (a) a modified virus-like particle (VLP) of cucumber mosaic virus (CMV), wherein said modified VLP of CMV comprises a modified CMV amino acid sequence of a coat protein of CMV, (b) a T helper cell epitope derived from tetanus toxin, and (c) an antigen. It is noted that instant SEQ ID NO: 62 shares 100% sequence identity with SEQ ID NO: 1 of the patent.
The patented claims do not recite the insertion position of the antigenic polypeptide, wherein said insertion of said antigenic polypeptide is between amino acid residues of said CMV polypeptide corresponding to amino acid residues of position 84 (Ser) and position 85 (Tyr) of SEQ ID NO:62.
However, as indicated above, Natilla et al. teach a chimeric CMV VLP comprising an antigenic peptide, wherein the antigenic peptide is a R9 mimotope which was inserted within the CMV coat protein (CP) after nucleotide position 252 (page 143). Nucleotide position 252 corresponds to amino acid position 84 of the CMV coat protein. Therefore the insertion point is between amino acid residues of position 84 (Ser) and position 85 (Tyr) of the CMV coat protein (or SEQ ID NO:62, as recited in claim 1), (as noted above, SEQ ID NO:62 discloses a sequence for the CMV coat protein as per instant application specification page 17), for the advantage of expressing high number of copies of a foreign peptide on the surface of chimeric CMV VLP particles (page 151).
Stothard is cited for teaching reverse translation tools to arrive at instant SEQ ID NO: 32 from the amino acid sequence of SEQ ID NO: 29 as taught by Bachmann et al., and Kramer et al.
It would have been prima facie obvious to a person of ordinary skill in the art, at the time of filing, to have included the teachings of Natilla et al. in the CMV VLP construct as recited by the patented claims for the benefit of expressing high number of copies of an antigenic peptides on the surface of each chimeric CMV VLP particle.
The sets of claims differ in scope; the claims in instant application indicated above refer to the genus of antigens while the patented claims refer to the species of antigens recited in patented claim 1. Therefore, the patented claims anticipate the instantly claimed genus in claims 1, 19, 21, 24, 26, 27, 29-36 of instant application.
Response to Arguments
Applicant's arguments filed 03/10/2026 have been fully considered but they are not persuasive.
Applicant contends on page 8 of the Remarks submitted on 03/10/2026:
Bachmann does not teach or even provide a reason to select the claimed VLP of CMV comprising CMV proteins with no fused antigenic polypeptides. Indeed, Bachmann is directed to improving vaccine development, see, e.g., Bachmann at [0012], which states "vaccines inducing good Th cell responses in essentially all subjects and individuals are an important goal in the field of vaccine development.". One of skill in the art interested in improving vaccine response would not have a reason to modify Bachmann to arrive at a VLP containing polypeptides that do not contain antigen. Bachmann therefore would not have directed a skilled artisan to arrive at the claimed invention and as discussed below, neither Natilla nor Kramer, alone or combined, remedy Bachmann's deficiencies.
In response:
Applicant’s thorough explanation of the instantly claimed invention is acknowledged. The remarks indicated above are not persuasive because as indicated previously Bachmann et al. already teach modified virus-like particles of CMV comprising more than one species of polypeptides, often referred to as mosaic VLPs; quoting from ¶ [0047]: “Virus-like particles comprising more than one species of polypeptides, often referred to as mosaic VLPs are also encompassed by the invention. Thus, in one embodiment, the virus-like particle according to the invention comprises at least two different species of polypeptides, wherein at least one of said species of polypeptides is a CMV polypeptide.” In one specific embodiment the VLPs of Bachmann et al. comprise at least two different species of polypeptides wherein at least one of said species of polypeptides is a CMV coat protein modified by a T helper cell epitope without an antigenic insertion (¶¶ [0047], [0014]). As explained in detail above, Bachmann et al. further teach a second species of polypeptide, wherein a second species of polypeptide is an inventive polypeptide and comprises a fusion protein comprising an antigen wherein the antigen may be associated, bound, mixed with or genetically linked to the virus-like particle (¶¶ [0074]-[0078], [0220]). Accordingly, the teachings of Bachmann et al. regarding the inventive polypeptide are not limited to chemical coupling but instead they encompass genetic fusions of antigens (¶¶ [0074]-[0078], [0220]). Therefore, is herein maintained that teachings of Bachmann et al. encompass the claimed modified VLPs comprising at least two different species of CMV polypeptides wherein one species comprised a fusion protein with an in-fused or genetically linked antigenic polypeptide and further a second one comprising a CMV coat protein with no such in-fused or genetically linked antigenic polypeptide. It should be underscored that Bachmann et al. already teach the embodiment of two species of CMV polypeptides (one with an antigenic insertion and a second without an antigenic insertion), and thus, one of ordinary skill in the art would not need to modify the teachings of Bachmann et al. to arrive at the VLPs containing a CMV polypeptide without an antigenic insertion. Said CMV polypeptide without an antigenic insertion is already included in the teachings of Bachmann et al. The modification to the teachings on Bachmann et al. relied on the present rejections pertain to the identity of the antigenic peptide (the Ara-h202 gene taught by Kramer et al.) and the insertion point (taught by Natilla et al.). In other words, one of ordinary skill in the art would not need to modify the teachings of Bachmann et al. to include a second CMV polypeptide without an antigenic insertion because Bachmann et al. already include this CMV polypeptide.
Applicant contends on page 9 of the Remarks submitted on 03/10/2026:
Bachmann's statement of a mosaic VLP comprising more than one species of polypeptide is a disclosure of an extremely large number of species as it encompasses VLPs comprising an enormous number of polypeptides. The size of the prior art genus should be considered when for obviousness purposes in this context. MPEP 2144.08 ("Consider the size of the prior art genus, bearing in mind that size alone cannot support an obviousness rejection. There is no absolute correlation between the size of the prior art genus and a conclusion of obviousness.").
In response:
Applicant’s remarks in regards to MPEP 2144.08 (size of the prior art genus) are not persuasive because Bachmann et al. teach the exact embodiment instantly claimed, including a sequence with 100% sequence identity to instant SEQ ID NO: 62. Further, the rejections set forth in the present Office Action, do not rely on the size of the genus taught by Bachmann et al., but instead on the clear teaching of a mosaic VLP comprising a two species of CMV polypeptides (one with an antigenic insertion and a second without an antigenic insertion). Further, Applicant’s remark that a mosaic VLP “comprising more than one species of polypeptide is a disclosure of an extremely large number of species as it encompasses VLPs comprising an enormous number of polypeptides” is not supported by evidence. The arguments of counsel cannot take the place of evidence in the record. In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965). Bachmann et al. do not teach nor suggest “an enormous amount of polypeptides” further it would be unclear whether such an embodiment would even form a VLP given that Bachmann et al. teach that the interactions of the CMV capsid subunits lead to the formation of viral capsid or viral-capsid like structure with an inherent repetitive organization (¶ [0046]). On the contrary, Bachmann et al. make reference to an embodiment comprising exactly two species of CMV polypeptides (one with an antigenic insertion and a second without an antigenic insertion) (¶ [0047]).
Applicant contends on page 9 of the Remarks submitted on 03/10/2026:
Bachmann's preferred embodiments weigh against a determination of obviousness because these preferred embodiments are significantly different in structure than the claimed invention. Bachmann's preferred embodiments do not form VLPs with two different proteins, as claimed. Furthermore, Bachmann's Examples uniformly rely on chemical coupling of antigens to preassembled VLPs via heterobifunctional linkers (see Examples 8-23). The "fusion protein" referred to in Bachmann (OA, p. 6) is not a fusion protein as claimed but rather, two cat allergen Fel dls are fused (i.e., chain 1 of Fel dl is fused to chain 2 of Fel dl), and this 'fused" Fel dl allergen is itself chemically conjugated using the crosslinker SMPH to CMV VLPs and is not genetically fused to CMV VLPs ( [0081]-[0083], Example 17). Therefore, Bachmann's preferred embodiments are significantly different in structure than what is claimed because (a) Bachmann's exemplified VLPs are not formed from two different polypeptides, let alone one antigen-containing polypeptide, and one that does not contain antigen, and (b) the antigens in Bachmann are not part of a fusion protein, but rather are chemically coupled to an existing VLP.
In response:
Applicant's arguments against the references individually are not persuasive because one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). As explained above and previously, the combination of the teachings of Bachmann et al., Natilla et al., and Kramer et al. render the claim invention obvious. Bachmann's preferred embodiments or examples are not cited in the present rejections as evidence of obviousness. The cited prior art provides clear teachings, suggestions and motivation to arrive at the claimed invention. In view of the foregoing, when all of the evidence is considered, the totality of the rebuttal evidence of nonobviousness fails to outweigh the evidence of obviousness.
Applicant contends on page 11 of the Remarks submitted on 03/10/2026: Applicant requests that the double patenting rejections be held in abeyance until patentable subject matter has been agreed to in the captioned application.
In response:
Applicant’s requests that the double patenting rejections be held in abeyance is acknowledged. However, it is herein maintained that double patenting rejections cannot be held in abeyance.
Conclusion
No claims are allowed.
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 MARLENE V BUCKMASTER whose telephone number is (703)756-5371. The examiner can normally be reached M-F 8-5.
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/MARLENE V BUCKMASTER/Examiner, Art Unit 1672
/NICOLE KINSEY WHITE/Primary Examiner, Art Unit 1672
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