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 .
DETAILED ACTION
Claims 1-10, 45-46, 58-66 are under consideration.
Priority
This application is a 371 National Stage entry from PCT/US2022/081912 (12/19/2022). PCT/US2022/081912 claims benefit of provisional application, 63/291,565 (12/20/2021).
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 12/18/2024 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Objections
Claims 2, 3, 4, 6, 8, 9, 62, and 63 are objected to because of the following informalities:
Claim 2: For improved consistency with terms in the art, change “intereferon” to “interferon”, “interleukine-2” to “interleukin-2”; “interleukine-4” to “interleukin-4”; “interleukine-12” to “interleukin-12”. Add a comma after the corrected “interleukin-12”. Change “Infectious salmon anemia virus (ISAV)” to “Infectious Salmon Anemia Virus (ISAV); “viral hemorrhagic septicemia virus” to “Viral Hemorrhagic Septicemia Virus”. Add a period to the end of the claim.
Claim 3: Add a comma between claim 1 and wherein for consistency with other claims. For example, “claim 1, wherein” .
Claim 4: For improved consistency with terms in the art, change “viral hemorrhagic septicemia virus” to “Viral Hemorrhagic Septicemia Virus”.
Claim 6: Add a comma between claim 5 and wherein. For example, “claim 5, wherein”.
Claim 8: Add a comma between claim 7 and wherein. For example, “claim 7, wherein”. Also, change “Transmembrane” to “transmembrane” for consistency with the other claims, e.g., claims 1, 7.
Claim 9: For improved consistency with terms in the art, change “Piscine Myocarditis Syndrome Virus (PMCV)” to “Piscine Myocarditis Virus”.
Claim 62: Add a comma between claim 61 and wherein. For example, “claim 61, wherein”.
Claim 63: For consistency within the claim set, change “piscine myocarditis virus (PMCV)” to “Piscine Myocarditis Virus (PMCV)”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 5-8, 59 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 5: The language of claim 5 is unclear. It is unclear what the relationship is between SEQ ID NO: 7 or SEQ ID NO: 48 with respect to identity. It is also unclear if SEQ ID NO: 7 and SEQ ID NO: 48 represent alternative options.
Claim 6: The phrase “wherein at least half of differing amino acids in said N-terminal secretion signal are conservative substitutions” is unclear. It is unclear what is being compared.
Claim 7: Similar to claim 5, the language of claim 7 is unclear. It is unclear what the relationship is between SEQ ID NO: 8 or SEQ ID NO: 49 with respect to identity. It is also unclear if SEQ ID NO: 8 and SEQ ID NO: 49 represent alternative options.
Claim 8: Similar to claim 6, the phrase “wherein at least half of differing amino acids in said transmembrane domain are conservative substitutions” is unclear. It is unclear what is being compared.
Claim 59: Claim 59 recites the limitation “The vector of claim 57 which is a plasmid vector. However, claim 57 was cancelled. Thus, there is insufficient antecedent basis for this limitation in the claim.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Section 33(a) of the America Invents Act reads as follows:
Notwithstanding any other provision of law, no patent may issue on a claim directed to or encompassing a human organism.
Claim 60 is rejected under 35 U.S.C. 101 and section 33(a) of the America Invents Act as being directed to or encompassing a human organism. See also Animals - Patentability, 1077 Off. Gaz. Pat. Office 24 (April 21, 1987) (indicating that human organisms are excluded from the scope of patentable subject matter under 35 U.S.C. 101).
See claim 60 as submitted 06/19/2024.
Claim 60 recites “A host cell comprising the vector of claim 58”. “A host cell” can read on a human organism’s cell that has been infected by a viral vector via vaccination methodology.
To overcome the rejection, and if appropriate, change “host cell” to “isolated host cell”.
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.
Claims 1, 3, 9, 10, 45, 58, 60, 61, 62, 63, and 66 are rejected under 35 U.S.C. 103 as being unpatentable over Tsai et al. (Tsai)(See PTO-892 Notice of References Cited) in view of Nilsen et al. (Nilsen)(WO2018144412A1)(as cited in the IDS submitted 12/18/2024).
See claims 1, 3, 9, 10, 45, 58, 60, 61, 62, 63, and 66 as submitted 06/19/2024.
Regarding claims 1, 3, Tsai teaches “The baculovirus–insect cell system has long been deployed for a variety of applications including for use as biopesticides, for recombinant protein production, transient transgene expression, tissue therapy, and for vaccine production” (p. 231, Abstract). Tsai also teaches “Baculoviruses are typically used to display foreign proteins (reads on instant claim 1. b) antigen) either on the viral surface or on the infected cell surface through fusion with viral glycoprotein GP64. In these cases, the foreign proteins…are usually fused with the GP64 signal peptide (SP) (reads on instant claim 1. a) N-terminal secretion signal sequence of a secreted or a first membrane -bound protein) and either its transmembrane (TMD) (reads on instant claim 1. c) a transmembrane domain of a second membrane-bound protein; also reads on instant claim 3, wherein the first membrane-bound protein is identical to the second membrane-bound protein, in this case GP64), cytoplasmic tail (C-terminal domain, CTD), or both the TMD and CTD domains of GP64 (Figure. 11.1B; Figure 11.2 D.)…The resulting recombinant virus thus displays the foreign proteins on the envelope alongside wild-type (WT) GP64. WT GP64 allows the virus to propagate normally, so that recombinant viruses expressing foreign genes are readily amplified” (p. 233).
Regarding claim 60, Tsai teaches insect and mammalian cells as host cells comprising the baculovector.
Tsai does not teach specifically any antigen from a non-enveloped virus.
Regarding claims 1, 9, 10, 45, 58, Nilsen, however, teaches a recombinant baculoviral vector is used to introduce the gene of interest (in this case PMCV ORF1 (as recited in instant claims 9 and 10)) into insect cells under the control of a strong baculoviral promoter (reads on instant claim 45, a nucleic acid sequence that encodes the fusion protein of claim 1; reads on instant claim 58, “a vector comprising…”). Infection of the insect cells in this way results in replication of the recombinant baculovirus vector genome, thereby increasing the number of genetic templates that encode the gene of interest and increasing the level of recombinant protein expression. Baculovirus-mediated protein expression also provides correct folding of recombinant proteins and other important post-translational modifications that provide proper biological activity and function to the expressed proteins.
Regarding claims 61 and 62, Nilsen teaches reference claim 11: A vaccine comprising the PMCV VLP of claim 10 where claim 10 refers back to reference claims 1-5 which specify PMCV ORF1 protein. With broad reasonable interpretation, a VLP can function as a vector.
Regarding claim 63, Nilsen teaches claim 10: The PMCV VLP as in any one of claims 1-5 for the treatment or prevention of cardiomyopathy syndrome (CMS) infections in fish. The reference disclosure states “The term "immunogenic" refers to the property that, when administered to fish (preferably salmonids), optionally together with an effective amount of a suitable adjuvant, in an immunogenically effective amount, the VLP of the invention induce the production of PMCV-specific antibodies in the fish. The reference disclosure also states “In some embodiments the PMCV VLP is suitable for use in treating or preventing viral infections of fish”. The reference disclosure also states the “PMCV VLP of the invention may be used in the production of a vaccine. For the avoidance of doubt, the term "vaccine" refers to a material or composition that can produce an immune response that blocks the infectivity, either partially or fully, of an infectious agent, which in respect of the present invention is the virus PMCV which causes CMS, affecting fish such as Atlantic salmon. Thus, when the vaccines of the invention, comprising PMCV VLP consisting only of PMCV ORF1 protein, are administered to a fish, the fish is immunised against CMS caused by PMCV”(p. 10).
Regarding claim 66, Nilsen teaches “[v]accines comprising the PMCV VLP of the invention are preferably administered to fish, which may, for example, be any species of fish that is susceptible to CMS infection. Of particular note, the vaccine is suitable for administration to, and for treating, a fin fish, which may be a telostei, for example, of the order Salmoniformes. Preferably, the claimed formulation may be used to treat salmon such as Atlantic and Pacific salmon, such as Coho salmon, arctic char, and trout such as rainbow trout and brown trout”(p. 12).
One of ordinary skill in the art would have been motivated to combine the teachings of both Tsai (for baculovirus expression system, and the role of GP 64) with the more specific (PMCV ORF-1 antigen) as taught by Nilsen to arrive at the fusion-protein in order to develop a vector based vaccine, such as a VLP, to prevent PMCV infection and the cardiomyopathy syndrome (CMS) it causes in fish, particularly Atlantic salmon (See MPEP 2143, Rationale A. Combining prior art elements according to known methods to yield predictable results and Rationale G. Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention).
One of ordinary skill in the art would have had a reasonable expectation of success for combining the teachings of Tsai and Nilsen. There would have been a reasonable expectation of success given the underlying materials and methods are known, successfully demonstrated in the baculovirus vector technology, piscine virology, and therapeutics, commonly used as evidenced by the applied prior art.
Therefore, the invention as a whole would have been prima facie obvious to one of
ordinary skill in the art before the effective filing date of the claimed invention.
Claim 64 and 65 are rejected under 35 U.S.C. 103 as being unpatentable over Tsai in view of Nilsen as applied to claims 1, 3, 9, 10, 45, 58, 60, 61, 62, 63, and 66 above, and further in view of Barker et al. (Barker)(US20210061866A1)(See PTO-892 Notice of References Cited)
See claims 64 and 65 as submitted 06/19/2024.
Tsai and Nilsen teach claim 63 but do not teach wherein said salmonid weighs between 15 and 200 grams (as recited in claim 64) and wherein said salmonid weighs between 40 and 110 grams (as recited in claim 65).
Barker, however, teaches intramuscular vaccine administration for the treatment or prevention of caligid copepod infection in fish (i.e. “sea lice”). Barker teaches “In embodiments of the invention, the fish is a salmonid. In embodiments of the invention, the fish is a salmon or trout” [0036] and provides examples involving more specifically, “Atlantic Salmon” [0061], similar to as taught by Nilsen. Barker also teaches “Fish size ranged from 98 to 295 grams at prime vaccination (average size 180 g)”[0151](this range overlaps with 15-200g and 40-110g as noted in instant claims 64 and 65). In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists (See 2144.05 Obviousness of Similar and Overlapping Ranges, Amounts, and Proportions].
One of ordinary skill in the art would have been motivated to immunize the salmonids as taught by Tsai and Nilsen using the fish size ranges in grams as taught by Barker in order to ensure good body condition, minimize anesthesia risk, increase ease of handling/visualization of the injection site(s), possibly reduce fish stress/sudden death, and improve recovery times post handling and inoculation (See MPEP 2143, Rationale A. Combining prior art elements according to known methods to yield predictable results).
One of ordinary skill in the art would have had a reasonable expectation of success for using the weight ranges as taught by Barker. There would have been a reasonable expectation of success given the underlying materials and methods are known, successfully demonstrated in the context of piscine vaccinology, therapeutics and/or aquaculture management, and commonly used as evidenced by the applied prior art.
Therefore, the invention as a whole would have been prima facie obvious to one of
ordinary skill in the art before the effective filing date of the claimed invention.
Claims 1-4, 9, 10, 45, 58, 59, 60, 61, 62, 63, and 66 are rejected under 35 U.S.C. 103 as being unpatentable over Martinez-Lopez et al. (Martinez-Lopez)(See PTO-892 Notice of References Cited) in view of Nilsen (as cited in the IDS submitted 12/18/2024) as evidenced by Tsai (See PTO 892: Notice of References Cited).
See claims 1-4, 9, 10, 45, 58, 59, 60, 61, 62, 63, and 66 as submitted 06/19/2024.
Regarding claim 1, Martinez-Lopez teaches to generate cell membrane anchored adjuvants (reads on a fusion-protein; as well as an antigen), in all of the cases the peptide DNA sequences were flanked by that of the signal peptide (SP) and the transmembrane domain (TM) of the gpGVHSV (reads on 1 a) “N-terminal secretion signal and 1 c) a transmembrane domain”)(p. 6012).
Regarding claim 2, 3, 4, Martinez-Lopez teaches that of the signal peptide (SP) and the transmembrane domain (TM) of the gpGVHSV (reads on wherein the first protein is selected from the group consisting of…viral hemorrhagic septicemia virus G-protein as recited in claim 2; wherein the first membrane bound-protein is identical to the second membrane-bound protein as recited in claim 3; and wherein said membrane bound protein is viral hemorrhagic septicemia virus G-protein (VHSV-G).
Regarding claim 45, 58, and 59, Martinez-Lopez teaches the properties of these viral glycoprotein regions as DNA molecular adjuvants, their corresponding cDNA sequences were cloned into a plasmid (pMCV1.4) flanked by the signal peptide and transmembrane sequences of gpGVHSV (p. 6012, Abstract). This reads on a nucleic acid sequence that encodes the fusion protein of claim 1 as recited in claim 45 and “plasmid” reads on claim 58 and claim 59’s “vector” and “plasmid vector”, respectively.
Note: For the above, claim 59 is being interpreted as “The vector of claim 58” which is a plasmid vector since claim 57 was canceled. However, see 112b rejection below.
Regarding claims 60, 61, Martinez-Lopez’s Zebrafish DNA immunization protocol (p. 6014) reads on both vaccine and a host cell comprising the vector.
Regarding claim 66, Martinez-Lopez teaches immunization of rainbow trout (p. 6014, section 2.8).
Martinez-Lopez teaches peptides 31 and 33, which are antigens from the enveloped virus VHSV. Martinez does not teach an antigen from a non-enveloped virus.
Regarding claims 1, 9, 10, 45, 58, as stated previously Nilsen, however, teaches a recombinant baculoviral vector, is used to introduce the gene of interest (in this case PMCV ORF1 (as recited in instant claims 9 and 10)) into insect cells under the control of a strong baculoviral promoter (reads on instant claim 45, a nucleic acid sequence that encodes the fusion protein of claim 1; reads on instant claim 58, “a vector comprising…”). Infection of the insect cells in this way results in replication of the recombinant baculovirus vector genome, thereby increasing the number of genetic templates that encode the gene of interest and increasing the level of recombinant protein expression. Baculovirus-mediated protein expression also provides correct folding of recombinant proteins and other important post-translational modifications that provide proper biological activity and function to the expressed proteins.
Regarding claims 61 and 62, Nilsen teaches reference claim 11: A vaccine comprising the PMCV VLP of claim 10 where claim 10 refers back to reference claims 1-5 which specify PMCV ORF1 protein. With broad reasonable interpretation, a VLP can function as a vector.
Regarding claim 63, Nilsen teaches claim 10: The PMCV VLP as in any one of claims 1-5 for the treatment or prevention of cardiomyopathy syndrome (CMS) infections in fish. The reference disclosure states “The term "immunogenic" refers to the property that, when administered to fish (preferably salmonids), optionally together with an effective amount of a suitable adjuvant, in an immunogenically effective amount, the VLP of the invention induce the production of PMCV-specific antibodies in the fish. The reference disclosure also states “In some embodiments the PMCV VLP is suitable for use in treating or preventing viral infections of fish”. The reference disclosure also states the “PMCV VLP of the invention may be used in the production of a vaccine. For the avoidance of doubt, the term "vaccine" refers to a material or composition that can produce an immune response that blocks the infectivity, either partially or fully, of an infectious agent, which in respect of the present invention is the virus PMCV which causes CMS, affecting fish such as Atlantic salmon. Thus, when the vaccines of the invention, comprising PMCV VLP consisting only of PMCV ORF1 protein, are administered to a fish, the fish is immunised against CMS caused by PMCV”(p. 10).
Regarding claim 66, Nilsen teaches “[v]accines comprising the PMCV VLP of the invention are preferably administered to fish, which may, for example, be any species of fish that is susceptible to CMS infection. Of particular note, the vaccine is suitable for administration to, and for treating, a fin fish, which may be a telostei, for example, of the order Salmoniformes. Preferably, the claimed formulation may be used to treat salmon such as Atlantic and Pacific salmon, such as Coho salmon, arctic char, and trout such as rainbow trout and brown trout”(p. 12).
Nilsen does not specifically discuss the baculovirus glycoproteins for the signal peptides or transmembrane domains.
Tsai, however, evidences “Baculoviruses are typically used to display foreign proteins either on the viral surface or on the infected cell surface through fusion with viral glycoprotein GP64. In these cases, the foreign proteins…are usually fused with the GP64 signal peptide (SP) and either its transmembrane (TMD), cytoplasmic tail (C-terminal domain, CTD), or both the TMD and CTD domains of GP64 (Figure. 11.1B; Figure 11.2 D.)…The resulting recombinant virus thus displays the foreign proteins on the envelope alongside wild-type (WT) GP64. WT GP64 allows the virus to propagate normally, so that recombinant viruses expressing foreign genes are readily amplified” (p. 233).
While the glycoproteins are not identical in Tsai/Nilsen’s teachings and Martinez-Lopez’s teachings, the overall construct of a N-terminal secretion signal sequence, an antigen, and a transmembrane domain is whether in a bacculoexpression system or using a plasmid based system.
One of ordinary skill in the art would have been motivated to combine the teachings of Martinez-Lopez for the VHSV-G components (signal peptide and transmembrane domain) of the fusion protein with the more specific (PMCV ORF-1 antigen) as taught by Nilsen and evidenced by Tsai to arrive at the fusion-protein in order to develop a vector based/plasmid based vaccine to prevent not only VHSV-G infection but also PMCV infection and the cardiomyopathy syndrome (CMS) it causes in fish, particularly Atlantic salmon or Rainbow trout (See MPEP 2143, Rationale A. Combining prior art elements according to known methods to yield predictable results and Rationale G. Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention).
One of ordinary skill in the art would have had a reasonable expectation of success for combining the teachings of Martinez-Lopez, Nilsen, and Tsai. There would have been a reasonable expectation of success given the underlying materials and methods are known, successfully demonstrated in the molecular biology, piscine virology, and aquaculture therapeutics, commonly used as evidenced by the applied prior art.
Therefore, the invention as a whole would have been prima facie obvious to one of
ordinary skill in the art before the effective filing date of the claimed invention.
Claims 5, 6, 7, and 8 are rejected under 35 U.S.C. 103 as being unpatentable over Martinez-Lopez in view of Nilsen and as evidenced by Tsai, as applied to claims 1-4, 9, 10, 45, 58, 59, 60, 61, 62, 63, and 66 above, and further in view of Wawra et al. (Wawra)(WO2014191759A1)(See PTO-892: Notice of References Cited).
See claims 5-8 as submitted 06/19/2024.
See also the 35 U.S.C. 112(b) rejection above.
Martinez-Lopez, Nilsen and Tsai teach claims 1 and 3, but do not teach wherein said N-terminal secretion signal sequence is at least 90% identical to SEQ ID NO: 7 or 48; at least half of the differing amino acids in said N-terminal secretion signal or the transmembrane domain are conservative substitutions; or wherein said transmembrane domain is at least 90% identical to SEQ ID NO: 8 or 49.
Wawra teaches “A composition comprising a translocation sequence derived from a fish pathogen and a heterologous payload coupled to the translocation sequence is provided. The composition is able to translocate across the plasma membrane of a eukaryotic cell, for example a fish cell, and thus stimulate an immune response. Accordingly, nucleic acids, vectors, host cells, compositions and vaccines based thereon are also provided” (Abstract). Wawra also teaches “Fish may be vaccinated by oral administration, immersion (bath, dip or spray) or injection (intraperitoneal or intramuscular)” (p. 1-2). “In one aspect the invention provides a vaccine of the invention for inducing an immune response in a human or animal. In some embodiments the immune response is the generation of antibodies against one or more antigens comprised in the payload. In some embodiments the animal is a fish or other marine animal, such as salmonids…Atlantic salmon (Salmo salaf)…rainbow trout (Oncorhynchus mykiss), sea trout (Salmo trutta) and other trouts (p. 17). The method may reduce the likelihood of contracting a condition associated with infection by…Viral haemorrhagic septicaemia virus (VHSV)(p. 18).
Regarding claim 5, Wawra also teaches a viral hemorrhagic septicemia virus protein, reference SEQ ID NO: 31 with amino acids 1 through 19 having a local 94.7% match to instant SEQ ID NO: 7 (see Result #23, BBQ97526, us-18-271-713-7.minpct90.rag, 07/24/2026, see supplementary contents tab).
Regarding claim 6, Wawra teaches a SEQ ID NO: 31 which also contains 18/19 residue matches and 1 conservative substitution at position 14, where instead of the Isoleucine of instant SEQ ID NO: 7, there is a Leucine in reference SEQ ID NO: 31. This meets the limitation of claim 6.
Regarding claim 7, similarly Wawra teaches a viral hemorrhagic septicemia virus protein, reference SEQ ID NO: 31 with amino acids 472 through 492 having a local 100% match to instant SEQ ID NO: 8 (see Result #6, BBQ97526, us-18-271-713-8.minpct90.rag, 07/24/2026, see supplementary contents tab).
Regarding claim 8, Wawra teaches amino acids 472 through 492 (21 amino acids) with a local 100% match (no substitutions) to the instant SEQ ID NO: 8. This also meets the limitation of claim 8.
One of ordinary skill in the art would have been motivated to substitute the VHSV-G protein N-terminal secretion signal and the transmembrane domain of reference SEQ ID NO: 31 as taught by Wawra for both the N-terminal secretion signal and the transmembrane domain as taught by Martinez-Lopez because of its role in targeting the protein to the endoplasmic reticulum and secretion as well as its role in immunogenicity against the VHSV-G protein (See MPEP 2143, Rationale B. Simple substitution of one known element for another to obtain predictable results).
One of ordinary skill in the art would have had a reasonable expectation of success for substituting the N-terminal secretion signal and the transmembrane domain sequences (from SEQ ID NO: 31) as taught by Wawra. There would have been a reasonable expectation of success given the underlying materials and methods are known, successfully demonstrated in the context of protein biology, vaccinology, and/or immunity, and commonly used as evidenced by the applied prior art.
Therefore, the invention as a whole would have been prima facie obvious to one of
ordinary skill in the art before the effective filing date of the claimed invention.
Claim 64 and 65 are rejected under 35 U.S.C. 103 as being unpatentable over Martinez-Lopez in view of Nilsen and as evidenced by Tsai, as applied to claims 1-4, 9, 10, 45, 58, 59, 60, 61, 62, 63, and 66 above, and further in view of Barker et al. (Barker)(US20210061866A1)(See PTO-892 Notice of References Cited).
See claims 64 and 65 as submitted 06/19/2024.
Martinez-Lopez, Tsai and Nilsen teach claim 63 but do not teach wherein said salmonid weighs between 15 and 200 grams (as recited in claim 64) and wherein said salmonid weighs between 40 and 110 grams (as recited in claim 65).
Barker, however, teaches intramuscular vaccine administration for the treatment or prevention of caligid copepod infection in fish (i.e. “sea lice”). Barker teaches “In embodiments of the invention, the fish is a salmonid. In embodiments of the invention, the fish is a salmon or trout” [0036] and provides examples involving more specifically, “Atlantic Salmon” [0061], similar to as taught by Nilsen. Barker also teaches “Fish size ranged from 98 to 295 grams at prime vaccination (average size 180 g)”[0151](this range overlaps with 15-200g and 40-110g as noted in instant claims 64 and 65). In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists (See 2144.05 Obviousness of Similar and Overlapping Ranges, Amounts, and Proportions].
One of ordinary skill in the art would have been motivated to immunize the salmonids as taught by Martinez-Lopez, Nilsen and Tsai using the fish size ranges in grams as taught by Barker in order to ensure good body condition, minimize anesthesia risk, increase ease of handling/visualization of the injection site(s), possibly reduce fish stress/sudden death, and improve recovery times post handling and inoculation (See MPEP 2143, Rationale A. Combining prior art elements according to known methods to yield predictable results).
One of ordinary skill in the art would have had a reasonable expectation of success for using the weight ranges as taught by Barker. There would have been a reasonable expectation of success given the underlying materials and methods are known, successfully demonstrated in the context of piscine vaccinology, therapeutics and/or aquaculture management, and commonly used as evidenced by the applied prior art.
Therefore, the invention as a whole would have been prima facie obvious to one of
ordinary skill in the art before the effective filing date of the claimed invention.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-5, 9-10, 45-46, 58, 60-66 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 14, 16, 19, 21, 23, 25, 27, 29, 31, 33, 36, 40-42, 45-51 of copending Application No. 18721719 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because both applications disclose a fusion protein, with a VHSV G protein N-terminal secretion signal sequence of a secreted or a first membrane -bound protein, an antigen, e.g., PMCV ORF-1, and a VHSV G protein transmembrane domain of a second membrane-bound protein as well as a vaccine comprising a vector with the nucleic acid sequence of the fusion protein to be used as a method of preventing PMCV in different salmonids of varying weight ranges. While the instant application is written quite generally, the reference application 18721719 provides different sequence options for the fusion protein, that all meet the limitations of the aforementioned claims to be rejected. The instant application (see instant claims 5, 46) and reference application’s (reference claims 36, 41) SEQ ID Nos: 7, 48, and 16 are identical.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-5, 9-10, 45, 58, 61 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6-7, 9-13, 15, 20, 33-35, 38 of copending Application No. 18721723 (reference application) in view of Nilsen (for PMCV ORF-1 antigen). Although the claims at issue are not identical, they are not patentably distinct from each other because both applications disclose a fusion protein, with a VHSV G protein N-terminal secretion signal sequence of a secreted or a first membrane -bound protein, an antigen, e.g., PMCV ORF-1, and a VHSV G protein transmembrane domain of a second membrane-bound protein as well as a vaccine comprising a vector with an expression cassette with the nucleic acid sequence of the fusion protein to be used as a method of preventing PMCV in different salmonids. While the instant application is written quite generally, the reference application 18721723 provides different sequence options for the fusion protein in the context of an expression cassette (which reads on vector), that all meet the limitations of the aforementioned claims to be rejected. The instant application (see instant claims 5, 46) and reference application’s (reference claims 15) SEQ ID Nos: 7, 48 are identical. The reference application teaches an antigen comprising a structural protein of a non-enveloped virus or a portion of said structural protein, said portion capable of eliciting protective response (as recited in reference claim 10)…The expression cassette of claim 10 wherein said structural protein is a capsid protein (as recited in reference claim 20)…and a vaccine comprising the expression cassette according to claim 7, and further comprising an antigen (as recited in claim 34).
The reference application, however, does not specifically state wherein the antigen is PMCV ORF-1 antigen. However, as noted previously above, Nilsen teaches the PMCV ORF-1 antigen, which is a capsid protein, in their composition for the prevention of cardiomyopathy syndrome (CMS) infections in fish, particularly salmonids.
One of ordinary skill in the art would have been motivated to substitute or use the PMCV ORF-1 antigen as taught by Nilsen as the “antigen” in order to develop a vaccine, as recited in reference claim 34, against an infection, such as a PMCV infection, in salmonid (See MPEP 2143 Rationale B. Simple substitution of one known element for another to obtain predictable results).
One of ordinary skill in the art would have had a reasonable expectation of success for substituting PMCV ORF-1 antigen as taught by Nilsen. There would have been a reasonable expectation of success given the underlying materials and methods are known, successfully demonstrated in the context of vaccinology, therapeutics and/or immunity within aquaculture, and commonly used as evidenced by the applied prior art.
Therefore, the invention as a whole would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
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 below is considered pertinent to applicant's disclosure.
Nzonza et al. (Nzonza)(See PTO-892 Notice of References Cited) teaches “a WNV vectored vaccine based on a fish Novirhabdovirus, the Viral Hemorrhagic Septicemia virus (VHSV). Nzonza generated rVHSV vectors bearing the complete WNV envelope gene (EWNV) (rVHSV-EWNV) or fragments encoding E subdomains (either domain III alone or domain III fused to domain II) (rVHSV-DIIIWNV and rVHSV-DII-DIIIWNV, respectively) in the VHSV genome between the N and P cistrons. With the objective to enhance the targeting of the EWNV protein or EWNV-derived domains to the surface of VHSV virions, Novirhabdovirus G-derived signal peptide and transmembrane domain (SPG and TMG) were fused to EWNV at its amino and carboxy termini, respectively (p. 1, Abstract)…The G signal peptide (SPG) from IHNV and the transmembrane domain (TMG) from VHSV were genetically fused to the amino and carboxy termini of the EWNV protein and EWNV domains” (p. 2). Nzonza did not teach that the first membrane-bound protein and the second membrane bound protein were the same, e.g., VHSV G protein.
Rouxel et al. (Rouxel)(See PTO-892 Notice of References Cited) “evaluate the potential of the Novirhabdovirus platform as a vaccine against influenza virus. Recombinant Novirhabdoviruses, rVHSV-HA and rIHNV-HA, expressing at the viral surface the hemagglutinin HA ectodomain were generated and used to immunized mice…[they] showed that mice immunized with either, rVHSV-HA or rIHNV-HA, elicited a strong neutralizing antibody response against influenza virus. A complete protection was conferred to the immunized mice when challenged with a lethal dose of influenza H1N1 A/PR/8/34 virus” (p. 1, Abstract). Rouxel teaches “the expression cassettes contain successively the signal peptide (SP) sequence derived from the IHNV glycoprotein G gene, the coding sequence for the ectodomain and stalk from the influenza H1N1 A/PR/8/34 hemagglutinin (HA) and the transmembrane sequence (TM) from
either IHNV or VHSV G gene. The expression cassettes were flanked with the gene start and
gene end signals of IHNV or VHSV in order to be recognized by the viral polymerase and to
direct the efficient expression of heterologous genes” (p. 6).
Haughland et al. (Haughland)(WO2011131600A1) teaches Figure 8 which is the same as the instant application’s Fig. 1 B, which illustrates the genome organization of PMCV with three large ORFs (p. 6, Specification and drawings).
Brun et al. (Brun)(See PTO 892-Notice of References Cited) teaches DNA vaccination in a veterinary context, particularly, in Table 1, and as noted, “Those developed against fish rhabdoviruses are amongst the most efficient DNA vaccines tested to date: non-specific early and specific long-time protective responses against infectious haematopoietic necrosis virus (IHNV) and Viral Hemorrhagic Septicemia virus (VHSV) have been achieved under a variety of conditions with single injections of small amounts of DNA encoding the viral surface glycoprotein (G), which is the only protein capable of eliciting neutralizing antibody and the production of a protective immune response (p. 2).
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/C.C./Examiner, Art Unit 1672
/M FRANCO G SALVOZA/Primary Examiner, Art Unit 1672
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