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 .
Claims 1 and 77-96 are pending in the present application.
Applicant’s election without traverse of Group IV (claims 84, 87-88, 91 and 96), drawn to in the reply filed on 08/11/2025 is acknowledged.
Applicant also elected the following species: An isolated capsid polypeptide comprising a substitution at an amino acid position corresponding to position 496 of the AAV2 capsid polypeptide set forth in SEQ ID NO: 1 (735-amino-acid sequence).
Accordingly, claims 1, 77-83, 85-86, 89-90 and 92-95 were withdrawn from further considerations because they are directed to non-elected inventions.
Claim 96 was also withdrawn from further considerations because it is directed to a non-elected species.
Therefore, claims 84, 87-88 and 91 are examined on the merits herein with the above elected species.
Claim Objections
Claim 84 is objected to because it is dependent on a non-elected claim 1.
Claim Rejections - 35 USC § 112 (Lack of Written Description)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 84 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP 2163 - 35 U.S.C. 112(a) and the first paragraph of pre-AIA 35 U.S.C. 112 require that the “specification shall contain a written description of the invention ....” This requirement is separate and distinct from the enablement requirement. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1340, 94 USPQ2d 1161, 1167 (Fed. Cir. 2010) (en banc). Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111 (Fed. Cir. 1991), clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” Vas-Cath Inc. v. Mahurkar, 19USPQ2d at 1117. The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed” Vas-Cath Inc. v. Mahurkar, 19USPQ2d at 1116.
Claim 84 encompasses an AAV vector that is produced by a method for producing a modified AAV vector for use in transducing human hepatocytes in vivo, or for enhancing the in vivo human hepatocyte transduction efficiency of an AAV vector, comprising the steps a)-c) as recited in independent claim 1, including the step of modifying the sequence of the reference capsid polypeptide to introduce one or more amino acid substitutions anywhere in the capsid polypeptide as long as such one or more amino acid substitutions alter the affinity of the capsid polypeptide for heparin; and wherein at least the modified AAV vector is characterized in that it elutes from a heparin affinity chromatography medium with a NaCl concentration of no more than 275 mM or with a conductivity of no more than 25 ms/cm; and has an in vivo transduction efficiency of human hepatocytes that is enhanced compared to a reference AAV vector having a capsid comprising the reference capsid polypeptide.
Apart from a disclosure of modifying the sequence of the AAV2 reference capsid polypeptide of SEQ ID NO: 1 (735-amino-acid sequence) with specific substitutions at one or more amino acid positions at 482, 484, 487, 496, 503, 532, 582, 585, 588, 589 and 596 listed in Table 5 (C482S, C482T, R484Q, R484N, R487Q, R487N, N496D, N496E, T503A, T503V, T503I, K532E, K532Q, N582S, N582D, N582Y, N582T, R585S, R585T, R585G, R585A, R585E, R588T, R588I, R588A, Q589D, Q589E, Q589A, N596D and N596E) (paragraph [00241] and Table 5 at page 81), the instant specification fails to provide sufficient written description for other substitutions at one or more of these positions, let alone at any other positions in the AAV2 reference capsid polypeptide of SEQ ID NO: 1, such that a modified AAV vector with the modified AAV2 capsid polypeptide at least elutes from a heparin affinity chromatography medium with a NaCl concentration of no more than 275 mM or with a conductivity of no more than 25 ms/cm, and has an in vivo transduction efficiency of human hepatocytes that is enhanced compared to a an AAV vector having an unmodified reference AAV2 capsid polypeptide as encompassed broadly by the instant claim. The instant claim encompasses an AAV vector comprising about 20735 different species of modified capsid polypeptides that endow the modified AAV vector with the recited characteristics. Lochrie et al (J. Virology 80:821-834, 2006) already disclosed mutations on the external surfaces of adeno-associated virus type 2 capsids that affect transduction and antibody neutralization; and they reported that N496A, T503A, T503S, K532A, R585K, R588K and Q589A AAV2 capsid mutants all have the same heparin binding as a wild type AAV2 capsid protein. Unlike the Q589A AAV2 capsid mutant listed in Table 5 of the present application, the Q589A AAV2 capsid mutant of Lochrie et al has also been reported to have the same heparin binding as a wild type AAV2 capsid protein. Thus, it is unclear which other essential element that this particular Q589A AAV2 capsid mutant of the present application possesses such that it endows the modified AAV vector with the recited properties; and the data of Lochrie et al demonstrate at least the unpredictability between the introduction of any amino acid substitution(s) at any position/residue in a wild-type AAV2 capsid protein with any of the desired properties encompassed by the instant claim. Please note that the physiological art is recognized as unpredictable (MPEP 2164.03). Since the prior art at the effective filing date of the present application (07/04/2019) did not provide sufficient guidance for the aforementioned issues as evidenced at least by the teachings of Lochrie et al (J. Virol. 80: 821-834, 2006), Linden (WO 2015/121501; IDS) and Asokan et al (WO 2017/058892), it is incumbent upon the present specification to do so. The present application also fails to provide a representative number of species for a broad genus an AAV vector comprising a modified capsid polypeptide with the recited properties i)-iii) as claimed broadly.
The claimed invention as a whole is not adequately described if the claims require essential or critical elements which are not adequately described in the specification and which are not conventional in the art as of Applicants’ filing date. Possession may be shown by actual reduction to practice, clear depiction of the invention in a detailed drawing, or by describing the invention with sufficient relevant identifying characteristics such that a person skilled in the art would recognize that the inventor had possession of the claimed invention. Pfaff v. Wells Electronics, Inc., 48 USPQ2d 1641, 1646 (1998). The skilled artisan cannot envision the complete detailed structure of a representative number of species for a broad genus an AAV vector comprising a modified capsid polypeptide with the recited properties i)-iii) as claimed broadly; and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method. Adequate written description requires more than a mere statement that it is part of the invention and reference to a method of isolating it. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (Fed. Cir. 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016 (Fed. Cir. 1991). One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481, 1483.
Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
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.
Claims 87-88 and 91 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Asokan et al (WO 2017/058892).
The instant claims are drawn to an isolated capsid polypeptide, comprising a sequence of amino acids comprising one or more amino acid substitutions relative to the AAV2 capsid polypeptide set forth in SEQ ID NO: 1, or a polypeptide having at least or about 90% sequence identity to the polypeptide set forth in SEQ ID NO: 1, wherein the one or more amino acid substitutions are at an amino acid position selected from among those corresponding to positions 482, 484, 487, 496 (elected species), 503, 532, 582, 585, 588, 589 and 596 of the AAV2 capsid polypeptide set forth in SEQ ID NO: 1; an AAV vector comprising the same capsid polypeptide and a host cell comprising the same AAV vector.
Asokan et al already disclosed at least modified capsid proteins from AAV and virus vectors comprising the same modified capsid proteins (Abstract; Summary of the Invention; section titled “Modified AAV capsid proteins and virus capsids and virus vectors comprising the same” at page 18). Specifically, Asokan et al taught an AAV capsid protein comprising a substitution at all positions or in any combination of fewer than all positions, resulting in the amino acid sequence: X1-X2-X3-X4-X5-X6-X7 at the amino acids corresponding to amino acid positions 492 to 498 (VP1 numbering) of the native AAV2 capsid protein, wherein X1 is any amino acid other than S; wherein X2 is any amino acid other than A; wherein X3 is any amino acid other than D; wherein X4 is any amino acid other than N; wherein X5 is any amino acid other than N; wherein X6 is any amino acid other than N and wherein X7 is any amino acid other than S; along with the native AAV2 capsid protein sequence of SEQ ID NO: 2 that is 100% identical to SEQ ID NO: 1 of the present application (page 23, lines 22-29; SEQ ID NO: 2 at page 110; and attached sequence search below). Asokan et al also taught methods of producing AAV vectors comprising the above disclosed modified capsid proteins in a host cell (e.g., a mammalian cell, 293 cells) (see at least page 65, line 19 continues to line 3 at page 66).
Accordingly, the teachings of Asokan et al meet every limitation of the instant claims. Therefore, the reference anticipates the instant claims.
Claim 84 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by Lochrie et al (J. Virol. 80: 821-834, 2006).
The claim is directed to an AAV vector that is produced by a method comprising the steps a)-c) as recited in independent claim 1. It is noted that this is a product-by-process claim.
Lochrie et al already prepared at least a rAAV2 vector with the mutated R585A or R588A capsid protein, wherein the mutated capsid protein has less than 1% heparin binding affinity compared to a wild-type AAV2 capsid protein (see at least Abstract; particularly page 825, right column, first two paragraphs; and Table 1). Lochrie et al also stated “Previous studies (25, 34) have identified five basic amino acids (R484, R487, K532, R585, R588) as being important for heparin binding by AAV-2” (page 825, right column, second paragraph). Since the rAAV2 vector with the mutated R585A or R588A capsid protein of Lochrie et al has the same structure as a modified AAV vector that is produced by the method of claim 1, the rAAV2 vector would at least elute from a heparin affinity chromatograph medium with a NaCl concentration of no more than 450 mM or with a conductivity of no more than 41 ms/cm, as well as having an enhanced in vivo transduction efficiency of human hepatocytes in comparison with a reference AAV2 vector having a non-modified capsid protein, particularly at least due to the nature of the substitution at residue 585 or 588 (the mutated capsid proteins have less positive charges to interact with the negative charge heparin).
Please, also note that where, as here, the claimed and prior art products are identical or substantially identical, or are produced by identical or substantially identical processes, the PTO can require an applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his claimed product. See In re Ludtke. Whether the rejection is based on "inherency" under 35 USC 102, or "prima facie obviousness" under 35 USC 103, jointly or alternatively, the burden of proof is the same, and its fairness is evidenced by the PTO's inability to manufacture products or to obtain and compare prior art products. In re Best, Bolton, and Shaw, 195 USPQ 430, 433 (CCPA 1977) citing In re Brown, 59 CCPA 1036, 459 F.2d 531, 173 USPQ 685 (1972).
Accordingly, the reference anticipates the instant claim.
Claims 84, 87-88 and 91 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Linden (WO 2015/121501; IDS).
Linden already disclosed at least a variant AAV2 capsid protein comprising one or more amino acid substitutions with respect to the wild type AAV capsid protein at positions 585 and 588 in the AAV2 capsid protein, preferably the variant AAV2 capsid protein comprising one or more of the amino acid substitutions R585S and R588T in the sequence of wild type AAV2 capsid protein VP1 of SEQ ID NO: 1 (100% identical to SEQ ID NO: 1 of the present application; see attached sequence search below); and a recombinant AAV vector comprising the same variant AAV2 capsid protein (Summary of the Invention; particularly page 1, last full paragraph; 5th and 6th paragraphs at page 4; section titled “Variant AAV2 capsid protein” at page 19; section titled “The heparin binding site (HBS)” at pages 49-50). Linden stated “S585 and/or T588; these residues may be associated with decreased heparin binding and increased spread of the virus in heparin sulphate proteoglycan-rich brain tissue” (page 20, lines 3-4); “In another embodiment, the recombinant AAV vector exhibits increased transduction of liver tissue compared to a corresponding wild type AAV capsid protein” (3rd last paragraph at page 7); and “In some embodiments, the rAAV vectors disclosed herein exhibit increased transduction of a tissue (e.g. hepatic, neuronal and/or retinal tissues), e.g. compared to a corresponding AAV vector (from the same serotype) comprising a wild type AAV capsid protein” (page 38, first sentence of second last paragraph). Linden also taught preparation of a recombinant AAV virion comprising the above disclosed variant AAV2 capsid protein in a suitable cell (e.g., 293 cells, HeLa cells, CHO cells) (paragraph bridging pages 39-40). Since the rAAV2 vector with the variant AAV2 capsid protein comprising one or more of the amino acid substitutions R585S and R588T in the sequence of wild type AAV2 capsid protein VP1 of SEQ ID NO: 1 of Linden has the same structure as a modified AAV vector that is produced by the method of claim 1, the rAAV2 vector would also possess the properties recited in the functional “wherein clause”.
Accordingly, the teachings of Linden meet every limitation of the instant claims. Therefore, the reference anticipates the instant claims.
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 87-88 and 91 are rejected under 35 U.S.C. 103 as being unpatentable over Lochrie et al (J. Virol. 80: 821-834, 2006) in view of Linden (WO 2015/121501; IDS).
The instant claims encompass an isolated capsid polypeptide, comprising a sequence of amino acids comprising one or more amino acid substitutions relative to the AAV2 capsid polypeptide set forth in SEQ ID NO: 1, or a polypeptide having at least or about 90% sequence identity to the polypeptide set forth in SEQ ID NO: 1, wherein the one or more amino acid substitutions are at an amino acid position selected from among those corresponding to positions 482, 484, 487, 496 (elected species), 503, 532, 582, 585, 588, 589 and 596 of the AAV2 capsid polypeptide set forth in SEQ ID NO: 1; an AAV vector comprising the same capsid polypeptide and a host cell comprising the same AAV vector. It is noted that the term “isolated” with reference to a polynucleotide or polypeptide is defined by the instant specification to be meant that the polynucleotide or polypeptide is substantially free of cellular material or other contaminating protein from the cells from which the polynucleotide or polypeptide is derived, or substantially free from chemical precursors or other chemicals when chemically synthesized (paragraph [0068]).
Lochrie et al already disclosed mutations on the external surfaces of an AAV2 capsid protein, that include at least AAV2 capsid mutants such as R487K, N496A, T503A, T503S, K532A, R585A, R585K, R588A, R588K among others (see at least Abstract; particularly page 825, right column, first two paragraphs; and Table 1). Lochrie et al also stated “Previous studies (25, 34) have identified five basic amino acids (R484, R487, K532, R585, R588) as being important for heparin binding by AAV-2” (page 825, right column, second paragraph). Lochrie et al also taught preparation of recombinant AAV2 virions comprising the mutated AAV capsid proteins in 293 cells; and they were assayed for the capsid synthesis, heparin binding and in vitro transduction properties (section titled “Materials and Methods” at pages 822-823; and Table 1).
Lochrie et al did not teach explicitly that the AAV2 capsid mutants were made on the wild type AAV2 capsid protein of SEQ ID NO: 1.
Before the effective filing date of the present application (07/04/2019), Linden already disclosed at least a variant AAV2 capsid protein comprising one or more amino acid substitutions with respect to the wild type AAV capsid protein at positions 585 and 588 in the AAV2 capsid protein, preferably the variant AAV2 capsid protein comprising one or more of the amino acid substitutions R585S and R588T in the sequence of wild type AAV2 capsid protein VP1 of SEQ ID NO: 1 (100% identical to SEQ ID NO: 1 of the present application; see attached sequence search below); and a recombinant AAV vector comprising the same variant AAV2 capsid protein (Summary of the Invention; particularly page 1, last full paragraph; 5th and 6th paragraphs at page 4; section titled “Variant AAV2 capsid protein” at page 19; section titled “The heparin binding site (HBS)” at pages 49-50). Linden also taught preparation of a recombinant AAV virion comprising the above disclosed variant AAV2 capsid protein in a suitable cell (e.g., 293 cells, HeLa cells, CHO cells) (paragraph bridging pages 39-40).
Accordingly, it would have been obvious for an ordinary skilled artisan to modify the teachings of Lochrie et al by also preparing mutations on the external surfaces of the wild-type AAV2 capsid protein of SEQ ID NO: 1 for characterization of the AAV2 capsid mutants on transduction and antibody neutralization; in light of the teachings of Linden as presented above.
An ordinary skilled artisan would have been motivated to carry out the above modification because Linden already disclosed the variant AAV2 capsid protein comprising one or more of the amino acid substitutions R585S and R588T in the sequence of wild type AAV2 capsid protein VP1 of SEQ ID NO: 1 that is 100% identical to SEQ ID NO: 1 of the present application.
An ordinary skilled artisan would have a reasonable expectation of success in light of the teachings of Lochrie et al and Linden; coupled with a high level of skill for an ordinary skilled artisan in the relevant art.
The modified compositions resulting from the combined teachings of Lochrie et al and Linden as set forth above are indistinguishable and encompassed by the compositions of the presently claimed invention.
Therefore, the claimed invention as a whole was prima facie obvious in the absence of evidence to the contrary.
Conclusions
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Quang Nguyen, Ph.D., whose telephone number is (571) 272-0776.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s SPE, James D. Schultz, Ph.D. may be reached at (571) 272-0763.
To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Group Art Unit 1631; Central Fax No. (571) 273-8300.
Any inquiry of a general nature or relating to the status of this application or proceeding should be directed to (571) 272-0547.
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/QUANG NGUYEN/Primary Examiner, Art Unit 1631
Adeno-associated virus-2 wild-type capsid protein VP1 SEQ ID NO: l.
WO2015121501-A1.
Query Match 100.0%; Score 3994; Length 735;
Best Local Similarity 100.0%;
Matches 735; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MAADGYLPDWLEDTLSEGIRQWWKLKPGPPPPKPAERHKDDSRGLVLPGYKYLGPFNGLD 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MAADGYLPDWLEDTLSEGIRQWWKLKPGPPPPKPAERHKDDSRGLVLPGYKYLGPFNGLD 60
Qy 61 KGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHADAEFQERLKEDTSFGGNLGRAVFQ 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 KGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHADAEFQERLKEDTSFGGNLGRAVFQ 120
Qy 121 AKKRVLEPLGLVEEPVKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDAD 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 AKKRVLEPLGLVEEPVKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDAD 180
Qy 181 SVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNSSGNWHCDSTWMGDRVI 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNSSGNWHCDSTWMGDRVI 240
Qy 241 TTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLI 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 TTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLI 300
Qy 301 NNNWGFRPKRLNFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 NNNWGFRPKRLNFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQG 360
Qy 361 CLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEDVPF 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 CLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEDVPF 420
Qy 421 HSSYAHSQSLDRLMNPLIDQYLYYLSRTNTPSGTTTQSRLQFSQAGASDIRDQSRNWLPG 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 HSSYAHSQSLDRLMNPLIDQYLYYLSRTNTPSGTTTQSRLQFSQAGASDIRDQSRNWLPG 480
Qy 481 PCYRQQRVSKTSADNNNSEYSWTGATKYHLNGRDSLVNPGPAMASHKDDEEKFFPQSGVL 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 PCYRQQRVSKTSADNNNSEYSWTGATKYHLNGRDSLVNPGPAMASHKDDEEKFFPQSGVL 540
Qy 541 IFGKQGSEKTNVDIEKVMITDEEEIRTTNPVATEQYGSVSTNLQRGNRQAATADVNTQGV 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 IFGKQGSEKTNVDIEKVMITDEEEIRTTNPVATEQYGSVSTNLQRGNRQAATADVNTQGV 600
Qy 601 LPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQILIKNTPVPANPSTT 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 LPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQILIKNTPVPANPSTT 660
Qy 661 FSAAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVY 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 FSAAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVY 720
Qy 721 SEPRPIGTRYLTRNL 735
|||||||||||||||
Db 721 SEPRPIGTRYLTRNL 735
Adeno-associated virus - 2 capsid protein VP1, SEQ ID:2.
WO2017058892-A2.
Query Match 100.0%; Score 3994; Length 735;
Best Local Similarity 100.0%;
Matches 735; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MAADGYLPDWLEDTLSEGIRQWWKLKPGPPPPKPAERHKDDSRGLVLPGYKYLGPFNGLD 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MAADGYLPDWLEDTLSEGIRQWWKLKPGPPPPKPAERHKDDSRGLVLPGYKYLGPFNGLD 60
Qy 61 KGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHADAEFQERLKEDTSFGGNLGRAVFQ 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 KGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHADAEFQERLKEDTSFGGNLGRAVFQ 120
Qy 121 AKKRVLEPLGLVEEPVKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDAD 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 AKKRVLEPLGLVEEPVKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDAD 180
Qy 181 SVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNSSGNWHCDSTWMGDRVI 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNSSGNWHCDSTWMGDRVI 240
Qy 241 TTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLI 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 TTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLI 300
Qy 301 NNNWGFRPKRLNFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 NNNWGFRPKRLNFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQG 360
Qy 361 CLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEDVPF 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 CLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEDVPF 420
Qy 421 HSSYAHSQSLDRLMNPLIDQYLYYLSRTNTPSGTTTQSRLQFSQAGASDIRDQSRNWLPG 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 HSSYAHSQSLDRLMNPLIDQYLYYLSRTNTPSGTTTQSRLQFSQAGASDIRDQSRNWLPG 480
Qy 481 PCYRQQRVSKTSADNNNSEYSWTGATKYHLNGRDSLVNPGPAMASHKDDEEKFFPQSGVL 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 PCYRQQRVSKTSADNNNSEYSWTGATKYHLNGRDSLVNPGPAMASHKDDEEKFFPQSGVL 540
Qy 541 IFGKQGSEKTNVDIEKVMITDEEEIRTTNPVATEQYGSVSTNLQRGNRQAATADVNTQGV 600
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Db 541 IFGKQGSEKTNVDIEKVMITDEEEIRTTNPVATEQYGSVSTNLQRGNRQAATADVNTQGV 600
Qy 601 LPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQILIKNTPVPANPSTT 660
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Db 601 LPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQILIKNTPVPANPSTT 660
Qy 661 FSAAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVY 720
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Db 661 FSAAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVY 720
Qy 721 SEPRPIGTRYLTRNL 735
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Db 721 SEPRPIGTRYLTRNL 735