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 of Invention VII, drawn to a method for treating LCAT deficiency (FLD), and the species of AAV8, V114M, and hLCAT-V114M-v1 in the reply filed on 06 January 2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). Furthermore, Claims 1-17 and 46 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention and species, respectively, there being no allowable generic or linking claim.
Application Status
The amendments and remarks filed 06 January 2026 have been entered. Claims 1 and 30 are amended. Claims 18-29 and 31-41 are cancelled. Claims 42-55 are newly added. Claim 1-17, 30, and 42-55 are pending. Claims 1-17 and 46 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Claims 30, 42-45 and 47-55 are pending and being examined on the merits.
Priority
This application is a CON of application 16/320,350 filed 01/24/2019 which is a 371 PCT of application US2017/043535 filed 07/24/2017 that claims priority to application 62/366,423 filed 07/25/2016.
Information Disclosure Statement
The information disclosure statement filed 6/20/2024 has been considered.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code on pages 20 and 30. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
The disclosure is objected to because of the following informalities: Merk is misspelled.
Appropriate correction is required
The use of the term American Type Culture Collection, Penn Vector Core, ThermoFisher, Freestyle 293 Expression Medium, Avanti Lipids, Wako, GE Healthcare, Applied Biosystems, SYBR Green, QuantStudio 7 Flex Real Time PCR System, QuikChange II XL Site Directed Mutagenesis, Agilent Technologies, Lipofectamine 2000, Biovendor, Superdex 200, Sigma-Aldrich, Maestro, Amicon Ultra 4, Millipore, and GraphPad Prism which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore, the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
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 30, 42-45 and 47-55 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.
Regarding claims 30 and 55 the SEQ ID NOs in the parenthesis and brackets renders the claim indefinite because it is unclear whether the limitations in the parenthesis or brackets are part of the claimed invention. See MPEP § 2173.05(d). A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 30 recites the broad recitation wild-type (WT) human LCAT, and the claim also recites SEQ ID NO: 1 which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Those claims identified in the statement of rejection but not explicitly referenced in the rejection are also rejected for depending from a rejected claim but failing to remedy the indefiniteness therein
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.
Claims 30, 44-45, 47 and 54-55 are rejected under 35 U.S.C. 103 as being unpatentable over Thigpen (WO 01/05943, published 1/25/2001) in view of Rader (WO2004108922, published 12/16/2004), Cohen (Cohen et al. 2004. Science 305: 869-871) and NM_000229 (NCBI Reference Sequence: NM_000229.1, 2014, Homo
sapiens lecithin-cholesterol acyltransferase (LCAT), mRNA).
Regrading claim 30, Thigpen teaches a method for treating or preventing a condition associated with LCAT deficiency comprising administering a therapeutically or prophylactically effective amount of a first exogenous nucleic acid segment that expresses lecithin-cholesterol acyltransferase (LCAT) wherein the cell express sufficient LCAT levels and wherein the first exogenous nucleic acid segment is operatively positioned under the control of at least a first exogenous promoter or regulatory sequences [claims 1, 11, 14, 58; pg. 21, lines 24-31; pg. 31, lines 16-18]. Thigpen teaches that Adeno-associated virus (AAV) is an attractive vector system for expressing LCAT (i.e., a recombinant AAV (rAAV) vector) in human cells as it has a high frequency of integration and it can transduce and infect nondividing cells, thus making it useful for delivery of genes into mammalian cells in tissue culture [pg. 62, lines 1-13]. Thigpen also teaches methods for making rAAV comprising an expression cassette. Thigpen teaches that the amounts of LCAT or LCAT-expressing cells necessary to generate a therapeutic response, or "therapeutically effective amounts", are exemplified by amounts of LCAT or LCAT-expressing cells effective to increase the HDL/LDL ratio upon contact with a sample comprising HDL (high density lipoproteins) and LDL (low density lipoproteins) [pg. 7, lines 4-7]. Thigpen teaches that the exogenous LCAT nucleic acid or gene is provided to the target cells simply by administering a suitable LCAT genetic construct to an animal or human in a manner effective to allow uptake and expression of the genetic construct. Viral vectors and recombinant viruses are generally preferred for such embodiments, whereas many viral vectors readily achieve expression in the liver, which is the normal site of LCAT expression, which is thus an advantage of the invention [pg. 19, lines 8-14]. Thigpen teaches that LCAT nucleic acids from non-human species may be used and engineered to improve expression by using at least a first codon optimized for expression in human cells [pg. 12, lines 21-23].
Thigpen do not teach that the LCAT is an LCAT enzyme having an V114M substitution based on the residue numbering of wild-type (WT) human LCAT [SEO ID NO: 1]. Thigpen is silent in regards to the rAAV being packaged in an AAV capsid. Thigpen do not teach the wild-type (WT) human LCAT of SEO ID NO: 1.
Regarding claim 30 and 47, Rader teaches compositions for lowering total cholesterol levels, reducing total very low-density lipoprotein (VLDL) levels, and/or raising high density lipoprotein (HDL) levels [pg.1, lines 30-34]. Rader teaches that these compositions are useful in treating atherosclerosis and heart disease, regulating elevated cholesterol levels and/or inappropriate lipoprotein metabolism [pg.1, lines 30-34]. Rader teaches these compositions contain an adeno-associated viral vector carrying expression cassettes comprising a capsid protein selected from an AAV serotype (such as serotype 7 or serotype 8) which expresses sufficiently high levels of transgene [pg. 2, lines 15-22; pg. 14, lines 8-22]. Rader teaches that the invention may include AAV delivery of transgenes useful for lipid modulation such as LCAT [pg. 13, line 29-pg. 14, line 13]. Rader teaches regulatory components operatively linked to transgenes in a manner that permits transgene transcription, translation, and/or expression in a host cell [pg. 13, lines 20-24].
Regarding claim 30, 47 and 54, Cohen teaches that the LCAT variant V114M is associated with high levels of high-density lipoproteins (HDL) [table 2]. The instant specification teaches that LCAT deficiency is characterized by low HDL levels.
NM_000229 teaches a sequence (residues 20 to 1342) that is 100% identical to SEQ ID NO:2 and encodes an amino acid sequence that is 100% identical to SEQ ID NO: 1. NM_000229 teaches that this gene encodes the extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase (see summary).
Regrading claim 30 and 47, it would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention to substitute the LCAT in the rAAV of Thigpen with the LCAT V114M of Cohen, based on the residue numbering of wild-type (WT) human LCAT of NM_000229, or obvious to try the codon-optimized LCAT V114M variant of SEQ ID NO: 63, and package them in an AAV capsid as taught by Rader. One of ordinary skill would be motivated to make the modification for the advantage of treating LCAT deficiency. One of ordinary skill would have a reasonable expectation of success given Cohen’s teaching that the LCAT variant V114M is associated with high levels of high-density lipoproteins (HDL) and the specification’s disclosure that LCAT deficiency is characterized by low HDL levels.
Regarding claim 45, it would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention to use the sequence disclosed in NM_000229 as the starting point when making the V114M variant. A skilled artisan would be motivated to make the modification with a reasonable expectation of success given that NM_000229 is 100% identical to SEQ ID NO: 2 and produces a functional protein with an amino acid sequence that is 100% identical to SEQ ID NO:1.
Regarding claims 44 and 55, it would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention that the AAV viral vector capsid comprising the LCAT V114M variant as taught and suggested by Thigpen, Rader and Cohen could be designed to have liver tropism given Thigpen’s teaching that administering suitable LCAT genetic constructs in a manner effective to allow uptake and expression of the genetic construct via viral vectors are, whereas many viral vectors readily achieve expression in the liver, which is the normal site of LCAT expression.
Claim 42 is rejected under 35 U.S.C. 103 as being unpatentable over Thigpen (WO 01/05943, published 1/25/2001) in view of Rader (WO2004108922, published 12/16/2004), Cohen (Cohen et al. 2004. Science 305: 869-871) and NM_000229 (NCBI Reference Sequence: NM_000229.1, 2014, Homo sapiens lecithin-cholesterol acyltransferase (LCAT), mRNA) as applied to claim 30, and further in view of
Lee (Lee et al. Biochimica et Biophysica Acta 1344 1997. 250–261).
The teachings of Thigpen, Rader, Cohen, and NM_000229 are discussed above as applied to claim 30 and similarly apply claim 42.
Thigpen, Rader, Cohen, and NM_000229 do not teach where the LCAT variant is truncated at the N-terminus or C-terminus.
Lee teaches LCAT mutants with C-terminal truncations at different positions [abstract; Fig. 2]. Lee teaches that mutants lacking the proline-rich region at the C-terminus were secreted at levels comparable to wild type, and have similar activities as well [abstract]. Lee teaches that the proline-deletion mutants were similar to wild-type LCAT in terms of phospholipase or transferase activities with various interfacial substrates, including reconstituted HDL, proteoliposomes, LDL, and micelles of platelet activating factor, and the binding of LCAT to the diverse interfaces [abstract]. Lee teaches that the mutants actually resulted in an 8-fold increase in the specific activity of LCAT towards the water-soluble p-nitrophenylbutyrate [abstract].
It would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention to modify the method as taught and suggested by Thigpen, Rader, Cohen, and NM_000229 by substituting the LCAT variant for a LCAT variant comprising mutants lacking the proline-rich region at the C-terminus. A skilled artisan would have been motivated to make the modification for the advantage of increasing the LCAT activity, which in turn would lead to the production of more HDL as taught by Cohen, in water soluble substrates.
Claim 43 is rejected under 35 U.S.C. 103 as being unpatentable over Thigpen (WO 01/05943, published 1/25/2001) in view of Rader (WO2004108922, published 12/16/2004), Cohen (Cohen et al. 2004. Science 305: 869-871) and NM_000229 (NCBI Reference Sequence: NM_000229.1, 2014, Homo
sapiens lecithin-cholesterol acyltransferase (LCAT), mRNA) as applied to claim 30 and further in view of Spahr (Spahr et al. Protein Science 2013 VOL 22:1739—1753).
The teachings of Thigpen, Rader, Cohen, and NM_000229 are discussed above as applied to claim 30 and similarly apply claim 43.
Thigpen, Rader, Cohen, and NM_000229 do not teach wherein the LCAT variant is delivered as a part of a fusion protein.
Spahr teaches that therapeutic proteins or peptides, such as human LCAT, often exhibit poor PK properties, including a short serum half-life, in humans and or research animals [pg. 1740, col. 2, para 2]. Spahr teaches that to extend the serum half-life and in vivo efficacy for preclinical and clinical studies, chimeric molecules with the Fc moiety fused to a protein or peptide can be engineered and produced. Spahr teaches that the fusion of an antibody Fc domain to a therapeutic protein or peptide to create a dimeric fusion molecule has proven to be highly successful for marketed products including protein-Fc chimeras. Spahr teaches a construct consisting of human LCAT fused to FC via a linker [pg. 1740, col. 2, para 2].
It would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention to modify the method as taught and suggested by Thigpen, Rader, Cohen, and NM_000229 by fusing an Fc moiety to the LCAT variant. A skilled artisan would be motivated with a reasonable expectation of success given Spahr’s teaching that proteins with the Fc moiety fused to the end of the protein have extended serum half-lives and in vivo efficacy for preclinical and clinical studies.
Claims 48-50 and 53 are rejected under 35 U.S.C. 103 as being unpatentable over Thigpen (WO 01/05943, published 1/25/2001) in view of Rader (WO2004108922, published 12/16/2004), Cohen (Cohen et al. 2004. Science 305: 869-871) and NM_000229 (NCBI Reference Sequence: NM_000229.1, 2014, Homo
sapiens lecithin-cholesterol acyltransferase (LCAT), mRNA) as applied to claim 30 and further in view of Wilson (US 10,137,176 B2, PCT filed 3/13/2014)
The teachings of Thigpen, Rader, Cohen, and NM_000229 are discussed above as applied to claim 30 and similarly apply claims 48-50 and 53.
Thigpen, Rader, Cohen, and NM_000229 do not teach where the regulatory sequence operably linked to the LCAT variant comprises an alpha mic/bik enhancer, a TGB promoter, a chimeric intron and a SV40 polyA.
Wilson teaches regulatory sequences linked to expression systems in AAV vectors. Wilson teaches that these control sequences can include a liver-specific TBG promoter, alpha mic/bic enhancers, a Promega intron sequence, and a rabbit globulin poly A [col. 12, lines 40-48]. Wilson teaches alternative poly A signals to include SV40 [col. 6, lines 59-67] and that the intron sequence can be a chimeric intron sequence [Fig. 1A].
It would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention to modify the method as taught and suggested by Thigpen, Rader, Cohen, and NM_000229 to use the liver-specific TBG promoter, alpha mic/bic enhancers, a chimeric intron sequence, and a SV40 poly A as regulatory sequences for the LCAT variant. One of ordinary skill would be motivated to make that modification for the advantage of expressing LCAT in liver specific tissues. One of ordinary skill would have a reasonable expectation of success given Wilson’s teaching that these regulatory sequences could be used to express genes in the liver, which is the normal site of LCAT expression.
Claims 51 and 52 are rejected under 35 U.S.C. 103 as being unpatentable over Thigpen (WO 01/05943, published 1/25/2001) in view of Rader (WO2004108922, published 12/16/2004), Cohen (Cohen et al. 2004. Science 305: 869-871) and NM_000229 (NCBI Reference Sequence: NM_000229.1, 2014, Homo
sapiens lecithin-cholesterol acyltransferase (LCAT), mRNA), Wilson (US 10,137,176 B2, PCT filed 3/13/2014) as applied to claim 30 and 48 and further in view of Tao (US 2011/0136100 A1)
The teachings of Thigpen, Rader, Cohen, NM_000229, and Wilson are discussed above as applied to claim 30 and 48 and similarly apply claims 51-52
Thigpen, Rader, Cohen, NM_000229, and Wilson do not teach where the chimeric intron comprises a human beta globin and human immunoglobulin heavy chain.
Tao teaches a method of transducing a hepatitis B virus genome comprising a hepatitis B virus genomic DNA insert into liver cells [0007]. Tao teaches that the expression constructs comprising the virus genome comprises synthetic introns and that synthetic intron improves transduction efficiency of trans-splicing adeno-associated viral vectors [0040]. Tao teaches that intron is a chimeric intron comprising a first intron in the human beta globulin gene and that the intronic acceptor sequences from the human immunoglobulin heavy chain gene which were inserted by PCR primers [0040].
It would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention to modify the method as taught and suggested by Thigpen, Rader, Cohen, NM_000229, and Wilson by substituting the chimeric intron as taught by Wilson for the chimeric intron that comprises a human beta globin and human immunoglobulin heavy chain as taught by Tao. The combination of prior art elements according to known methods to yield predictable results supports can support a conclusion of obviousness. See MPEP 2143(I). One of ordinary skill in the art would have a reasonable expectation of success since both Wilson and Tao teach delivering expression constructs comprising regulatory sequences to liver tissues using an AAV vector.
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 30, 42-45 and 47-55 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 4-5, and 7-21 of U.S. Patent No. 1883470 B2 in view of Thigpen (WO 01/05943, published 1/25/2001) and Cohen (Cohen et al. 2004. Science 305: 869-871).
Claim 1 of the US Patent claims a recombinant viral vector which comprises an expression cassette comprising: (a) a nucleic acid sequence comprising SEQ ID NO: 26, SEQ ID NO: 63, or a sequence at least 95% identical to SEQ ID NO: 26 or 63 which encodes a functional human lecithin cholesterol acyltransferase (LCAT) variant comprising: an M amino acid substitution at amino acid residue position 114 based on the residue numbering of WT normal LCAT (V114M); and (b) regulatory sequences which direct expression of the LCAT V114M in a host cell, said regulatory sequences being operably linked to the LCAT V114M sequence. Claim 2 claims that the recombinant viral vector is an adeno-associated virus
The patent does not teach using the AAV vector in a method for treating human familial lecithin cholesterol acyltransferase (LCAT) deficiency (FLD).
The teachings of Thigpen and Cohen are discussed above.
It would have been obvious to one ordinary skilled in the art before the effective filing date of the claimed invention to use the LCAT variant of the patent in a a method for treating human familial lecithin cholesterol acyltransferase (LCAT) deficiency (FLD). One of ordinary skill would be motivated to make the modification for the advantage of treating LCAT deficiency. One of ordinary skill would have a reasonable expectation of success given Cohen’s teaching that the LCAT variant V114M is associated with high levels of high-density lipoproteins (HDL) and the specification’s disclosure that LCAT deficiency is characterized by low HDL levels.
For additional limitations of the instant claims, see the additional teachings of the patented claims.
Conclusion
No claims allowed.
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/TIFFANY NICOLE GROOMS/Examiner, Art Unit 1637