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 without traverse of group I and the species of MOG in the reply filed on 4/23/26 is acknowledged.
Claims 55-57 and 71 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 4/23/26.
Claims 4, 6-8, 12 and 24-28 are also withdrawn since they require a non-elected species.
Claims 1-3, 11, 14-23, 31, 35, 36, 45-47, 49, 50, 69 and 70 are examined on the merits.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 5/18/2022 and 4/23/26 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
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.
Notwithstanding any other provision of law, no patent may issue on a claim directed to or encompassing a human organism.
Claims 69 and 70 are 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). The claimed invention is drawn to a cell comprising the expression cassette or that produces the rAAV particle of claim 45.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-3, 11, 15-23, 31, 35, 36, 69 and 70 are rejected under 35 U.S.C. 112, first paragraph, as containing subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Applicant broadly claims a host cell or expression vector or nucleic acid containing the nucleic acids of claims 1-3, 11, 15-23, 31, 35, 36, 69 and 70. The claims read on a cell within a transgenic animal or a transgene therein given that the term "isolated" is not denoted in describing the host cell, nucleic acid, or expression vector.
With respect to the unisolated host cells and transgenes as “nucleic acids” or “expression vectors “of the instant claims discussed above, the state of the art at the time of filing was such that one of skill could not predict the phenotype of transgenics. The art of transgenic animals has for many years stated that the unpredictability lies, in part, with the site or sites of transgene integration into the target genome and that "the position effect" as well as unidentified control elements are recognized to cause aberrant expression of a transgene (Wall et Al., Theriogenology, Vol. 45, Pg. 57-68, 1996).
The elements of the particular construct used to make transgenic animals are also held to be critical, and they must be designed case by case without general rules to obtain good expression of a transgene; e.g., specific promoters, presence or absence of introns, etc. (Houdebine et Al., Journal of Biotechnology, Vol. 34, Pg. 269- 287, 1994). Furthermore, transgenic animals are regarded to have within their cells, cellular mechanisms that prevent expression of the transgene, such as methylation or deletion from the genome (Kappell et Al., Current Opinions in Biotechnology, Vol. 3, Pg. 548-553, 1992). Houdebine (Comparative Immunology, Microbiology, and Infectious Diseases, Vol. 32, Pg. 107-121, 2009) teaches progress has been made in the field of transgenic animals for production of foreign proteins (Abstract); however, constructing an efficient expression vector to produce a therapeutic protein is not a standard operation (Pg. 116, Paragraph, second). Therefore, undue experimentation is required to make and use a transgene and transgenic animal to produce the antibody and antibody fragments of the instant claims.
Examples in the literature aptly demonstrate that even closely related species carrying the same transgene construct can exhibit widely varying phenotypes. Mullins (1993, Hypertension, Vol. 22, No. 4, pp. 630-633) states that not all animals express a transgene sufficiently to provide a model for a disease as the integration of a transgene into different species of animal has been reported to give divergent phenotypes. For example, several animal models of human diseases have relied on transgenic rats when the development of mouse models was not feasible. Mullins (1990, Nature, Vol. 344, 541-544) produced outbred Sprague-Dawley x WKY rats with hypertension caused by expression of a mouse Ren-2 renin transgene. Hammer (1990, Cell, Vol. 63, 1099- 1112) describes spontaneous inflammatory disease in inbred Fischer and Lewis rats expressing human class I major histocompatibility allele HLA-B27 and human 02- microglobulin transgenes. Both investigations were preceded by the failure to develop human disease-like symptoms in transgenic mice expressing the same transgenes that successfully caused the desired symptoms in transgenic rats (Mullins, 1989, EMBO J., Vol. 8, pages 183-191). Thus, the use of nonmurine species for transgenesis will continue to reflect the suitability of a particular species for the specific questions being addressed, bearing in mind that a given construct may react very differently from one species to another.
The examiner notes here, in addition to these issues, even assuming arguendo a person having ordinary skill in the art could make a host organism with functional transgene that encodes the instantly recited SEQ ID NO: 5, there is no predictability that the host will survive its expression. The transgene depends on the host for function and harm to the host, including death, renders the transgene nonfunctional and thus not enabled.
The art is well-aware of side effects caused by expressing proteins, such as therapeutic antibodies. In a transgenic cell or animal that expresses the same, the antibody will exert any possible side effect it can. It is not administered but chronically present and so such side effects are chronic and potentially more serious than any from an administered antibody. Hansel (Nature Reviews Drug Discovery, Vol. 9, Pg. 325-337, 2010) teaches in their table 1 on page 328 numerous exemplary side effects from licensed monoclonal antibodies to include: increased bleeding risk, infection, heart failure, cancer, thyroid disorder, autoimmune reactions, and cytokine release syndrome (CRS) to name only a few. One or more such effects, or similar, may occur with the therapeutic antibody instantly recited when administered and indeed be exacerbated by chronic exposure due to internal expression. The instantly encoded antibody binds a mammalian protein and so may very well target related or unrelated proteins in the transgenic host, leading to such side effects. For all these reasons, previously raised and new, transgenes are not enabled.
At the time of filing, the phenotype of a transgene and transgenic cell contained within any animal was unpredictable. The claims as written, encompassing a transgene and cell in a transgenic animal, is not adequately described in the specification as to prevent excessive experimentation by the public to generate and use the invention. Applicants can obviate the instant rejection by amending the claim to recite the term "isolated" before the recitation, "host cell" and by amending the vector and polynucleotide claims to specify they are not in a transgenic animal. Applicant may consider using purified in such claims if description is appropriate for such a term and it is not redefined away from standard meaning. Method claims using these products should also carry the appropriate adjectives above.
In view of the lack of the predictability of the art to which the invention pertains as evidenced by the art above, the lack of guidance and direction provided by Applicant, and the absence of working examples, undue experimentation would be required to make and use transgenic animals possessing the claimed host cells, nucleic acid, or expression vector, with a reasonable expectation of success, absent a specific and detailed description in Applicant’s specification of how to effectively practice this and absent working examples providing evidence which is reasonably predictive that the claimed host cell, nucleic acid, or expression vector, commensurate in scope with the claimed invention. The same can be said for the transgenes and transgenic animals encompassed by the instant claims. Thus, the claims are rejected here.
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 3, 19, 21, 22, 45-47, 49 and 70 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 3 recites the limitation "said self-antgien or said autoantigen" in line 2. There is insufficient antecedent basis for this limitation in the claim.
Claims 19, 21 and 22 recite, “said MOG comprises or consists of amino acids 1-117 of a mature MOG”; amino acids 35 - 55, 118 - 132, 181 - 195, or 186 - 200 of a mature MOG; amino acids 1 - 20, 11 - 30, 21-40, 31-50 of a mature MOG. However, mature MOG is not a specifically defined sequence and it is unclear if the amino acid positions of 1-117, 35 - 55, 118 - 132, 181 - 195, or 186 – 200, 1 - 20, 11 - 30, 21-40, and 31-50 are based on the N-terminal amino acid or C-terminal amino acid of a MOG. It is suggested that the claim be amended to require a corresponding SEQ ID NO: which would provide a specific reference sequence.
Claim 45 recites the limitation "expression cassette" in line 1. There is insufficient antecedent basis for this limitation in the claim. Claims 2-3 do not recite expression cassette.
Claim 46 recites the limitation "said nucleic acid" in line 2. There is insufficient antecedent basis for this limitation in the claim. Claims 2-3 do not recite expression cassette.
Claim 47 recites, “SPK1 (SEQ ID NO: 1), SPK2 (SEQ ID NO: 2) VP1”, however, it is unclear if the SPK1 and SPK2 is SEQ ID NO: 1 and SEQ ID NO: 2 or if they are optional limitations since the SEQ ID NO:s are in parenthesis.
Claim 49 recites the limitation "one or more of particles" in line 1. There is insufficient antecedent basis for this limitation in the claim.
Claim 49 recites, “A pharmaceutical composition” and “in a biological compatible carrier or excipient”. It is unclear if the composition is a biological composition or if it is a pharmaceutical composition since a pharmaceutically acceptable carrier or excipient is not required by the claim.
Claim 70 recites the limitation "the viral particle, lentiviral particle" in line 1. There is insufficient antecedent basis for this limitation in the claim.
Claims 2 and 3 are rejected on the basis that it contains an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class, and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 2117.
The Markush grouping of proteins is improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons: claims 2 and 3 require different proteins (i.e., a self-antigen or autoantigen or protein or peptide), which are different proteins based on in vivo use and function.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
Claims 16, 17 and 23 are rejected on the basis that it contains an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class, and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 2117.
The Markush grouping of distinct proteins and fragments thereof is improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons: the disclosed sequences include MOG, MBP and PLP and fragments thereof.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 1-3, 11, 15-23, 31 and 69 are rejected under 35 U.S.C. 102a1 as being anticipated by Mi et al. (US PGPub 20090175846).
The claimed invention is drawn to an expression cassette comprising an expression control element operably linked to a nucleic acid encoding a fusion protein, said fusion protein comprising an unwanted antigen and a leader sequence for cell secretion.
The expression control element is position 5’ of said nucleic acid
The unwanted antigen comprises a self- antigen, autoantigen or protein or peptide that has structural similarity or sequence identity to said self-antigen or said autoantigen; the unwanted antigen is truncated or is a subsequence of a full length native/wildtype unwanted antigen; the unwanted antigen comprises a human protein; the unwanted antigen being myelin oligodendrocyte glycoprotein (MOG); the unwanted antigen is a subsequence of SEQ ID NO: 5 and is capable of inducing an immune response in a subject when expressed.
The claimed invention also requires a cell comprises the expression cassette.
The MOG: lacks all or part of its transmembrane domain; comprises or consists of amino acids 1-117 of a mature MOG; is a subsequence of a MOG extracellular domain or a subsequence of a transmembrane domain; comprises or consists of amino acids 35-55, 118-132, 181-195, 186-200 of a mature MOG; comprises or consists of amino acids 1-20, 11-30, 21-40, 31-50 of a mature MOG.
“[0124] As used herein, the terms "subsequence," "fragment" or "portion" or the like refer to any portion of a larger sequence, up to and including the complete sequence. The minimum length of a subsequence is generally not limited, except that a minimum length of the subsequence of an unwanted antigen should be long enough to solicit an immune response (e.g., can act an immunogen)…” Therefore, limitations of “subsequence” will be interpreted as a fragment MOG that is capable of eliciting an immune response, such as a fragment of MOG that would be long enough to be considered an epitope (i.e., 10 amino acids).
Mi et al. teach at paragraph [0236] … “secretion cassette can be incorporated into a replicable expression vector. Useful vectors include linear nucleic acids, plasmids, phagemids, cosmids and the like. An exemplary expression vector is pdC, in which the transcription of the immunofusin DNA is placed under the control of the enhancer and promoter of the human cytomegalovirus. See, e.g., Lo et al., Biochim. Biophys. Acta 1088:712 (1991); and Lo et al., Protein Engineering 11:495-500 (1998). An appropriate host cell can be transformed or transfected with a DNA that encodes a soluble OMgp polypeptide and used for the expression and secretion of the soluble OMgp polypeptide. Host cells that are typically used include immortal hybridoma cells, myeloma cells, 293 cells, Chinese hamster ovary (CHO) cells, Hela cells, and COS cells.” OMgp is oligodendrocyte-myelin glycoprotein and Mi et al. teach that at paragraph [0094] “A non-limiting example of soluble OMgp polypeptides include polypeptides which comprise, consist essentially of, or consist of one or more of an LRR domain, CR domain or S/TR domain of the OMgp polypeptide. As one of skill in the art would appreciate, any described domain of OMgp may comprise additional or fewer amino acids on either the C-terminal or N-terminal end of the extracellular domain polypeptide. As such, soluble OMgp polypeptides for use in the methods of the present invention include, but are not limited to, an OMgp polypeptide comprising, consisting essentially of, or consisting of amino acids 1 to 54 of SEQ ID NO:2; amino acids 1 to 56 of SEQ ID NO:2; amino acids 1 to 75 of SEQ ID NO:2; amino acids 1 to 98 of SEQ ID NO:2; amino acids 1 to 166 of SEQ ID NO:2; amino acids 1 to 191 of SEQ ID NO:2; amino acids 1 to 215 of SEQ ID NO:2; amino acids 1 to 228 of SEQ ID NO:2; amino acids 1 to 425 of SEQ ID NO:2; amino acids 1 to 440 of SEQ ID NO:2; amino acids 25 to 54 of SEQ ID NO:2; amino acids 25 to 56 of SEQ ID NO:2; amino acids 25 to 75 of SEQ ID NO:2; amino acids 25 to 98 of SEQ ID NO:2; amino acids 25 to 166 of SEQ ID NO:2; amino acids 25 to 191 of SEQ ID NO:2; amino acids 25 to 215 of SEQ ID NO:2; amino acids 25 to 228 of SEQ ID NO:2; amino acids 25 to 425 of SEQ ID NO:2; and amino acids 25 to 440 of SEQ ID NO:2 or fragments, variants, or derivatives of such polypeptides.
Mi et al. also teach at paragraph [0019] “In certain embodiments, the OMgp antagonist a soluble OMgp polypeptide. Certain soluble OMgp polypeptides of the invention comprise or lack the following domains: an OMgp cysteine-rich domain, an OMgp LRR, an OMgp serine/threonine-rich domain, a fragment, variant, or derivative thereof of an OMgp cysteine rich domain, LRR domain or serine/threonine rich domain, or a combination of at least two of said OMgp domains, fragments, variants, or derivatives thereof. In some embodiments, the OMgp antagonist is administered by bolus injection or chronic infusion. In some embodiments, the soluble OMgp polypeptide is administered directly into the central nervous system. In some embodiments, the soluble OMgp polypeptide is administered directly into a chronic lesion of MS.
They also teach at paragraph [0304] “an OMgp antagonist can be produced in vivo in a mammal, e.g., a human patient, using a gene-therapy approach to treatment of a nervous-system disease, disorder or injury in which promoting survival, proliferation and differentiation of neurons and/or oligodendrocytes or promoting myelination of neurons would be therapeutically beneficial. This involves administration of a suitable OMgp antagonist-encoding nucleic acid operably linked to suitable expression control sequences. Generally, these sequences are incorporated into a viral vector. Suitable viral vectors for such gene therapy include an adenoviral vector, an alphavirus vector, an enterovirus vector, a pestivirus vector, a lentiviral vector, a baculoviral vector, a herpesvirus vector, an Epstein Barr viral vector, a papovaviral vector, a poxvirus vector, a vaccinia viral vector, adeno-associated viral vector and a herpes simplex viral vector. The viral vector can be a replication-defective viral vector. Adenoviral vectors that have a deletion in its E1 gene or E3 gene are typically used. When an adenoviral vector is used, the vector usually does not have a selectable marker gene.”
Therefore, Mi et al. teach subsequences of MOG, as defined by applicant, and they teach truncated versions of MOG, which can comprise the amino acids of claims 18-22 as well.
Therefore, Mi et al. anticipate the instant invention.
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.
Claim(s) 35, 36, 45-47, 49, 50 and 70 are rejected under 35 U.S.C. 103 as being unpatentable over Mi et al. as applied to claims 1-3, 11, 15-23, 31 and 69 above, and further in view of Hoffman (US PGPub 2017/0043036), as evidenced by Lochrie et al. (US PGPub 2003/0134404).
The claimed invention also requires that the expression cassette is positioned between one or more 5’ and/or 3’ adeno-associated virus (AAV) inverted terminal repeats and the ITRs are from AAV serotype 2. The claimed invention also requires a recombinant AAV particle comprising the expression cassette that comprises in 5’ to 3’ orientation a first AAV ITR, a promoter operable in mammalian cells, said nucleic acid, a polyadenylation signal and optionally a second AAV ITR. The rAAV comprises a VP1, VP2 or VP3 sequence 60% or more identical to VP1, VP2 OR VP3 of an AAV serotype.
The claimed invention also requires a pharmaceutical composition comprising one or more particles of rAAV in a biologically compatible carrier or excipient and the composition also comprises empty AAV capsids.
The claimed invention also requires cells that produce the rAAV particle.
The teachings of Mi et al. are summarized above, while they teach nucleic acid expression systems for a modified MOG, which can be secreted and that viral vectors, including AAV vectors can be employed in the expression of an MOG antagonist, which includes soluble MOG itself.
Hoffman et al. teach the generation of recombinant AAV8 which contain nucleic acid expression cassettes that encode for MOG. [see examples 2 and 3] specific examples of MOG are that of SEQ ID NO: 3, which is 98% identical to SEQ ID NO: 5 of claims 16 and 23, MOG 35-55 (SEQ ID NO: 6) and MOG 92-106 (SEQ ID NO: 7). Hoffman et al. further teach at paragraph [0015-16] “In some embodiments, the invention provides improved rAAV particles including those derived from one or more serotypes as known in the art (including, for example, those selected from the group consisting of AAV1, AAV2, AAV3, AAV4, AAV5, AAV6, AAV7, AAV8, AAV9, AAV10, AAV11, and AAV12). The present invention also concerns rAAV nucleic acid vectors, wherein the nucleic acid segment further comprises a promoter, an enhancer, a post-transcriptional regulatory sequence, a polyadenylation signal, or any combination thereof, operably linked to the nucleic acid segment that encodes the selected polynucleotide of interest.” And at paragraph [0066] “In some embodiments, a rAAV nucleic acid vector described herein comprises inverted terminal repeat sequences (ITRs), such as those derived from a wild-type AAV genome, such as the AAV2 genome. In some embodiments, the rAAV nucleic acid vector further comprises nucleic acid segment that includes a transgene (also referred to as a heterologous nucleic acid molecule) operably linked to a promoter and optionally, other regulatory elements, wherein the ITRs flank the nucleic acid segment.”
Hoffman et al. further teach at paragraph [0108] “If desired, rAAV particles described herein may be administered in combination with other agents as well, such as, e.g., proteins or polypeptides or various pharmaceutically-active agents, including one or more systemic or topical administrations of therapeutic polypeptides, biologically active fragments, or variants thereof. In fact, there is virtually no limit to other components that may also be included, given that the additional agents do not cause a significant adverse effect upon contact with the target cells or host tissues. The rAAV particles may thus be delivered along with various other agents as required in the particular instance. Such compositions may be purified from host cells or other biological sources, or alternatively may be chemically synthesized as described herein.” While Hoffman et al. do not specifically state that empty AAV capsids would be present with their rAAV pharmaceutical compositions, as evidenced by Lochrie et al., which teach that during the prodocution of rAAV, both loaded or full AAV virions and empty virions would be produced (see paragraph 0012 of Lochrie et al.). Therefore, the rAAV pharmaceutical compositions of Hoffman et al. would include empty AAV capsids.
It would have been obvious to one of ordinary skill in the art to modify the compositions taught by Mi et al. in order to generation a rAAV of serotype 8 that contains the expression cassette of encodes a MOG subsequence of fragment in addition to AAV ITRs and a polyadenylation sequence and an operably linked promoter. One would have been motivated to do so, given the suggestion by Mi et al. that the viral vectors, including AAV, can be used to express/deliver MOG (OMgp agonist). There would have been a reasonable expectation of success, given the knowledge that rAAV can be readily produced that contain expression cassettes encoding for MOG, including fragments of MOG, as taught by Hoffman et al. Thus the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art at the time the invention was made.
Conclusion
No claims are allowed.
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/BENJAMIN P BLUMEL/Primary Examiner, Art Unit 1671
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