Genome polyprotein

Details

Name
Genome polyprotein
Synonyms
  • 3.6.1.15
  • P2A
Gene Name
Not Available
Organism
HHAV
Amino acid sequence
>lcl|BSEQ0007430|Genome polyprotein
MNMSRQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGS
HQVEPLRTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGL
LRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVV
RIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLT
PLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWT
SIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDL
VFDFQVFPTKYHSGRLLFCFVPGNELIDVSGITLKQATTAPCAVMDITGVQSTLRFRVPW
ISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFA
PLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMKDLKGKANRGKMDVSGVQAPV
GAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTF
PITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTP
WVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLV
SIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVD
DPRSEEDKRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKIS
LFYTEEHEIMKFSWRGVTADTRALRRFGFSLAAGRSVWTLEMDAGVLTGRLIRLNDEKWT
EMKDDKIVSLIEKFTSNKYWSKVNFPHGMLDLEEIAANSKDFPNMSETDLCFLLHWLNPK
KINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLKSMMFGFHHSVTVEIINTVLC
FVKSGILLYVIQQLNQDEHSHIIGLLRVMNYADIGCSVISCGKVFSKMLETVFNWQMDSR
MMELRTQSFSNWLRDICSGITIFKNFKDAIYWLYTKLKDFYEVNYGKKKDILNILKDNQQ
KIEKAIEEADEFCILQIQDVEKFEQYQKGVDLIQKLRTVHSMAQVDPNLMVHLSPLRDCI
ARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIY
TKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPMRLNMASLEEKGRHFSS
PFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDMLNVNLAKTNDAIKD
MSCVDLIMDGHNVSLMDLLSSLVMTVEIRKQNMTEFMELWSQGISDDDNDSAVAEFFQSF
PSGEPSNSKLSGFFQSVTNHKWVAVGAAVGILGVLVGGWFVYKHFSRKEEEPIPAEGVYH
GVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGVKDDWLLV
PSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITQ
HFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAW
RGKGEGLPGMCGGALVSSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIESQRI
MKVEFTQCSMNVVSKTLFRKSPIYHHIDKTMINFPAAMPFSKAEIDPMAVMLSKYSLPIV
EEPEDYKEASIFYQNKIVGKTQLVDDFLDLDMAITGAPGIDAINMDSSPGFPYVQEKLTK
RDLIWLDENGLLLGVHPRLAQRILFNTVMMENCSDLDVVFTTCPKDELRPLEKVLESKTR
AIDACPLDYSILCRMYWGPAISYFHLNPGFHTGVAIGIDPDRQWDELFKTMIRFGDVGLD
LDFSAFDASLSPFMIREAGRIMSELSGTPSHFGTALINTIIYSKHLLYNCCYHVCGSMPS
GSPCTALLNSIINNVNLYYVFSKIFGKSPVFFCQALKILCYGDDVLIVFSRDVQIDNLDL
IGQKIVDEFKKLGMTATSADKNVPQLKPVSELTFLKRSFNLVEDRIRPAISEKTIWSLIA
WQRSNAEFEQNLENAQWFAFMHGYEFYQKFYYFVQSCLEKEMIEYRLKSYDWWRMRFYDQ
CFICDLS
Number of residues
2227
Molecular Weight
251506.45
Theoretical pI
6.48
GO Classification
Functions
ATP binding / cysteine-type endopeptidase activity / ion channel activity / RNA binding / RNA helicase activity / RNA-directed RNA polymerase activity / structural molecule activity
Processes
pore formation by virus in membrane of host cell / protein oligomerization / RNA-protein covalent cross-linking / suppression by virus of host gene expression / suppression by virus of host MAVS activity / suppression by virus of host MAVS activity by MAVS proteolysis / transcription, DNA-templated / viral entry into host cell / viral RNA genome replication / virion attachment to host cell
Components
host cell cytoplasmic vesicle membrane / host cell mitochondrial outer membrane / integral to membrane of host cell / membrane / viral capsid
General Function
Structural molecule activity
Specific Function
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with HAVCR1 to provide virion attachment to target cell (By similarity).Protein VP0: VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, HAV VP4 does not seem to be myristoylated and has not been detected in mature virions, supposedly owing to its small size.VP1-2A precursor is a component of immature procapsids and corresponds to an extended form of the structural protein VP1. The C-terminal domain of VP1-2A, protein 2A, acts as an assembly signal that allows pentamerization of P1-2A, which is the precursor of the structural proteins. 2A is proteolytically removed from particulate VP1-2A by a host protease and does not seem to be found in mature particles.Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability.Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).Protein 3A, via its hydrophobic domain, serves as membrane anchor to the 3AB and 3ABC precursors.The 3AB precursor interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs.The 3ABC precursor is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein.Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer.Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Also cleaves host proteins such as PCBP2.RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Virion
Gene sequence
>lcl|BSEQ0020720|Genome polyprotein
ATGAACATGTCTAGACAAGGTATTTTCCAGACTGTTGGGAGTGGTCTTGACCACATCCTG
TCTTTGGCAGACATTGAGGAAGAGCAAATGATTCAATCAGTTGATAGGACTGCAGTGACT
GGTGCTTCTTATTTTACTTCTGTGGATCAATCTTCAGTTCATACAGCTGAGGTTGGATCA
CACCAGGTTGAACCTTTGAGAACCTCTGTTGATAAACCCGGTTCAAAGAAGACTCAGGGA
GAGAAATTTTTCTTGATTCATTCTGCAGATTGGCTTACTACACATGCTCTTTTCCATGAA
GTTGCAAAATTGGATGTGGTGAAATTATTATACAATGAGCAGTTTGCTGTTCAAGGGTTG
TTGAGATACCATACATATGCAAGATTTGGCATTGAAATTCAAGTTCAGATAAACCCTACA
CCTTTCCAACAGGGGGGATTGATCTGTGCTATGGTTCCTGGTGACCAGAGCTATGGTTCT
ATAGCATCATTGACTGTTTATCCTCATGGTTTGTTAAATTGCAATATTAACAATGTGGTT
AGAATAAAGGTTCCATTTATTTACACAAGAGGTGCTTACCACTTTAAAGATCCACAATAC
CCAGTTTGGGAATTGACAATTAGAGTTTGGTCAGAATTAAATATTGGGACAGGAACTTCA
GCTTATACTTCACTCAATGTTTTAGCTAGATTTACAGATTTGGAGTTGCATGGATTAACT
CCTCTTTCTACACAAATGATGAGAAATGAATTTAGGGTCAGTACTACTGAGAATGTGGTG
AATCTGTCAAATTATGAAGATGCAAGAGCAAAGATGTCTTTTGCTTTGGATCAGGAAGAT
TGGAAATCTGATCCGTCCCAGGGTGGTGGGATCAAAATTACTCATTTTACTACTTGGACA
TCTATTCCAACTTTGGCTGCTCAGTTTCCATTTAATGCTTCAGACTCAGTTGGTCAACAA
ATTAAAGTTATTCCAGTTGACCCATATTTTTTCCAAATGACAAATACGAATCCTGACCAA
AAATGTATAACTGCTTTGGCTTCTATTTGTCAGATGTTTTGTTTTTGGAGAGGAGATCTT
GTCTTTGATTTTCAAGTTTTTCCCACCAAATATCATTCAGGTAGATTACTGTTTTGTTTT
GTTCCTGGCAATGAGCTAATAGATGTTTCTGGAATCACATTAAAGCAAGCAACTACTGCT
CCTTGTGCAGTAATGGATATTACAGGAGTGCAGTCAACTTTGAGATTTCGTGTTCCCTGG
ATTTCTGACACTCCTTACAGAGTGAACAGGTATACAAAGTCAGCACATCAGAAAGGTGAG
TACACTGCCATTGGGAAGCTTATTGTGTATTGTTATAACAGATTGACCTCTCCTTCTAAC
GTTGCTTCCCATGTCAGAGTGAATGTTTATCTTTCAGCAATTAACTTGGAATGTTTTGCT
CCTCTTTATCATGCTATGGATGTTACTACACAAGTTGGAGATGATTCTGGAGGTTTTTCA
ACAACAGTTTCTACAGAACAGAATGTTCCAGATCCCCAAGTTGGTATAACAACCATGAAA
GATTTGAAAGGAAAAGCTAACAGAGGGAAAATGGATGTTTCAGGAGTACAAGCACCTGTG
GGAGCTATCACAACAATTGAGGATCCAGTTTTAGCAAAGAAAGTACCTGAGACATTTCCT
GAATTGAAACCTGGAGAATCCAGACATACATCAGATCATATGTCCATCTACAAGTTTATG
GGAAGGTCTCATTTCTTGTGCACTTTTACATTCAATTCAAATAATAAAGAGTACACATTT
CCTATAACCTTGTCTTCAACCTCTAATCCTCCTCATGGTTTGCCATCAACACTGAGGTGG
TTTTTCAACTTGTTTCAGTTGTATAGAGGGCCTTTAGATCTGACAATTATTATTACAGGA
GCAACTGATGTAGATGGCATGGCCTGGTTCACTCCAGTAGGTCTTGCCGTTGATACTCCT
TGGGTAGAGAAGGAGTCAGCTTTGTCTATTGACTACAAAACTGCTCTTGGAGCTGTCAGA
TTTAACACAAGGAGAACAGGGAACATTCAGATTAGATTACCATGGTATTCTTATTTATAT
GCTGTGTCTGGAGCACTGGATGGTTTGGGTGACAAGACAGATTCTACATTTGGATTGGTT
TCTATTCAGATTGCAAATTACAATCATTCTGATGAATACTTGTCTTTTAGTTGTTATTTG
TCTGTCACAGAACAATCAGAGTTTTATTTTCCCAGAGCTCCATTGAACTCAAATGCCATG
TTATCCACTGAATCAATGATGAGCAGAATTGCAGCTGGAGACTTGGAGTCATCAGTGGAT
GATCCTAGATCAGAGGAAGATAAAAGATTTGAGAGTCATATAGAATGCAGGAAGCCATAT
AAAGAACTGAGATTAGAAGTTGGGAAACAAAGACTCAAGTATGCTCAGGAAGAATTGTCA
AATGAAGTACTTCCACCCCCTAGGAAAATGAAGGGACTGTTTTCACAAGCCAAAATTTCT
CTTTTTTATACTGAGGAGCATGAAATAATGAAGTTTTCCTGGAGAGGTGTGACTGCTGAT
ACTAGAGCTTTAAGGAGGTTTGGATTCTCTTTGGCCGCAGGCAGAAGTGTGTGGACTCTT
GAAATGGATGCTGGGGTTCTTACTGGGAGACTGATTAGATTGAATGATGAGAAATGGACA
GAAATGAAGGATGACAAGATTGTTTCATTGATTGAAAAGTTTACAAGTAACAAATATTGG
TCCAAAGTGAATTTCCCACATGGGATGTTGGATCTTGAAGAAATTGCTGCCAATTCTAAG
GATTTTCCTAACATGTCTGAAACGGATTTGTGTTTCTTGCTGCATTGGTTAAATCCAAAG
AAAATTAATTTAGCAGATAGAATGCTTGGATTGTCTGGAGTTCAGGAAATTAAAGAACAA
GGTGTTGGATTAATAGCAGAGTGTAGAACTTTCTTAGATTCTATTGCTGGAACTTTAAAA
TCTATGATGTTTGGATTTCATCATTCTGTGACTGTTGAAATTATAAACACTGTGCTCTGT
TTTGTTAAGAGTGGAATTTTGCTTTATGTAATACAACAATTGAATCAGGATGAACATTCT
CACATAATTGGTTTGTTGAGAGTCATGAATTATGCAGATATTGGTTGTTCAGTTATTTCA
TGTGGCAAAGTTTTTTCCAAAATGCTGGAAACAGTCTTTAATTGGCAAATGGACTCCAGA
ATGATGGAGTTAAGGACTCAGAGTTTTTCCAACTGGTTAAGAGATATTTGTTCTGGGATC
ACCATTTTTAAAAACTTCAAGGATGCAATTTATTGGCTTTATACAAAATTAAAGGACTTT
TATGAAGTGAATTATGGCAAGAAGAAGGACATTTTAAATATTCTTAAAGATAACCAACAA
AAAATAGAGAAAGCCATTGAGGAAGCCGATGAATTTTGCATTTTGCAAATCCAAGATGTG
GAAAAATTTGAACAGTATCAGAAAGGGGTTGACTTGATACAAAAATTGAGAACTGTTCAT
TCAATGGCTCAGGTTGATCCAAATTTAATGGTTCATTTGTCACCTTTGAGAGATTGTATA
GCAAGAGTTCATCAGAAACTTAAAAACCTTGGATCTATAAATCAGGCAATGGTAACGAGA
TGTGAGCCAGTTGTTTGTTATTTATATGGCAAAAGAGGGGGAGGAAAGAGCTTAACATCA
ATTGCATTGGCAACCAAAATTTGTAAACATTATGGTGTTGAGCCTGAAAAGAATATCTAT
ACTAAACCTGTGGCTTCAGATTACTGGGATGGATATAGTGGACAATTAGTTTGCATCATT
GATGATATTGGCCAAAACACAACAGATGAGGATTGGTCAGATTTTTGTCAGTTAGTGTCA
GGATGTCCAATGAGATTAAACATGGCCTCTCTTGAGGAGAAGGGTAGGCATTTTTCTTCT
CCTTTTATAATAGCAACTTCAAATTGGTCAAATCCAAGTCCAAAAACAGTTTATGTTAAG
GAAGCAATTGACCGCAGACTCCATTTCAAGGTTGAAGTTAAACCTGCTTCATTTTTCAAA
AATCCTCACAATGATATGTTGAATGTTAATTTAGCTAAAACAAATGATGCAATCAAAGAT
ATGTCTTGTGTTGATTTGATAATGGATGGACATAATGTTTCATTGATGGATTTGCTCAGT
TCTTTAGTCATGACAGTTGAAATTAGAAAACAAAACATGACTGAATTCATGGAGTTGTGG
TCTCAGGGAATTTCAGATGATGATAATGATAGTGCAGTAGCTGAGTTTTTCCAGTCTTTT
CCATCTGGTGAACCATCGAACTCTAAATTATCTGGCTTTTTCCAATCTGTTACTAATCAC
AAGTGGGTTGCTGTGGGAGCTGCAGTTGGCATTCTTGGAGTGCTCGTTGGAGGATGGTTT
GTGTATAAGCATTTCTCCCGCAAAGAGGAGGAACCAATCCCAGCTGAAGGGGTATATCAT
GGTGTAACTAAGCCCAAGCAAGTGATTAAATTAGATGCAGATCCAGTAGAATCTCAGTCA
ACTTTGGAAATAGCAGGACTGGTTAGGAAGAACTTGGTTCAGTTTGGAGTTGGAGAGAAG
AATGGATGTGTGAGATGGGTTATGAATGCCTTGGGAGTGAAAGATGATTGGCTGCTTGTG
CCTTCCCATGCTTATAAATTTGAGAAAGATTATGAAATGATGGAGTTTTATTTTAATAGA
GGTGGAACTTACTATTCAATTTCAGCTGGTAATGTTGTTATTCAATCTTTGGATGTGGGA
TTCCAGGATGTTGTTCTGATGAAGGTTCCTACAATTCCTAAGTTTAGAGATATTACTCAG
CATTTTATTAAGAAAGGGGATGTGCCTAGAGCTTTGAATCGCCTGGCAACATTAGTGACA
ACTGTAAATGGAACCCCTATGTTAATTTCTGAGGGCCCACTAAAGATGGAAGAGAAAGCT
ACTTATGTTCATAAGAAAAATGATGGTACAACAGTTGATTTAACTGTGGATCAGGCATGG
AGAGGAAAAGGCGAAGGTCTTCCTGGAATGTGTGGTGGGGCCTTGGTTTCATCGAATCAA
TCTATACAGAATGCAATCTTGGGCATCCATGTTGCTGGAGGAAATTCAATTCTTGTTGCA
AAATTGGTTACTCAAGAAATGTTCCAAAATATTGATAAGAAAATTGAAAGTCAGAGAATT
ATGAAAGTGGAGTTTACTCAGTGTTCAATGAATGTGGTCTCCAAAACGCTTTTTAGAAAG
AGTCCCATTTATCATCACATTGATAAAACCATGATTAATTTTCCTGCAGCTATGCCCTTT
TCTAAAGCTGAAATTGATCCAATGGCTGTGATGTTATCTAAGTATTCATTACCTATTGTA
GAAGAACCAGAGGATTATAAAGAGGCTTCAATTTTTTATCAAAATAAAATAGTGGGTAAG
ACTCAGTTAGTTGATGATTTTTTAGATCTTGATATGGCCATTACAGGGGCCCCAGGAATT
GATGCTATCAACATGGATTCATCTCCTGGATTTCCTTATGTCCAGGAGAAGTTGACCAAA
AGAGATTTAATTTGGTTGGATGAAAATGGTTTATTGCTGGGAGTTCATCCAAGATTGGCT
CAGAGAATCTTATTCAATACTGTCATGATGGAAAATTGTTCTGATTTGGATGTTGTTTTT
ACAACCTGTCCAAAAGATGAATTGAGACCATTAGAGAAAGTGTTGGAATCAAAAACAAGA
GCTATTGATGCTTGTCCTCTGGATTACTCAATTTTGTGCCGAATGTATTGGGGTCCAGCT
ATTAGTTATTTTCATTTGAATCCAGGTTTCCATACAGGTGTTGCTATTGGCATAGATCCT
GATAGACAGTGGGATGAATTATTTAAAACAATGATAAGATTCGGAGATGTTGGTCTTGAT
TTAGATTTCTCTGCTTTTGATGCTAGTCTTAGTCCATTTATGATTAGAGAAGCAGGTAGA
ATCATGAGTGAACTATCTGGAACTCCATCCCATTTTGGCACAGCTCTTATCAATACTATC
ATTTATTCCAAGCATTTGCTGTATAACTGTTGTTACCATGTCTGTGGTTCAATGCCCTCT
GGGTCTCCTTGTACAGCTTTGCTAAATTCAATTATTAATAATGTCAATTTGTATTATGTG
TTTTCCAAGATATTTGGAAAGTCTCCAGTTTTCTTTTGTCAGGCTTTGAAGATTCTCTGT
TATGGAGATGATGTTTTAATAGTTTTCTCTCGAGATGTTCAGATTGATAATCTTGATTTG
ATTGGACAAAAAATTGTAGATGAGTTTAAGAAACTTGGCATGACAGCTACTTCTGCTGAC
AAGAATGTACCTCAGCTGAAACCAGTTTCGGAATTGACTTTTCTCAAAAGATCTTTCAAT
TTGGTAGAGGATAGAATTAGACCTGCAATTTCGGAAAAAACAATTTGGTCTTTAATAGCA
TGGCAGAGAAGTAACGCTGAGTTTGAGCAGAATTTAGAAAATGCTCAGTGGTTTGCTTTT
ATGCATGGCTATGAGTTTTATCAGAAATTTTATTATTTTGTTCAGTCCTGTTTGGAGAAA
GAGATGATAGAATACAGACTTAAATCTTATGATTGGTGGAGAATGAGATTTTATGACCAG
TGTTTCATTTGTGACCTTTCATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP08617
UniProtKB Entry NamePOLG_HAVHM
GenBank Protein ID329583
GenBank Gene IDM14707
General References
  1. Cohen JI, Ticehurst JR, Purcell RH, Buckler-White A, Baroudy BM: Complete nucleotide sequence of wild-type hepatitis A virus: comparison with different strains of hepatitis A virus and other picornaviruses. J Virol. 1987 Jan;61(1):50-9. [Article]
  2. Cohen JI, Rosenblum B, Ticehurst JR, Daemer RJ, Feinstone SM, Purcell RH: Complete nucleotide sequence of an attenuated hepatitis A virus: comparison with wild-type virus. Proc Natl Acad Sci U S A. 1987 Apr;84(8):2497-501. [Article]
  3. Lemon SM, Murphy PC, Shields PA, Ping LH, Feinstone SM, Cromeans T, Jansen RW: Antigenic and genetic variation in cytopathic hepatitis A virus variants arising during persistent infection: evidence for genetic recombination. J Virol. 1991 Apr;65(4):2056-65. [Article]
  4. Baroudy BM, Ticehurst JR, Miele TA, Maizel JV Jr, Purcell RH, Feinstone SM: Sequence analysis of hepatitis A virus cDNA coding for capsid proteins and RNA polymerase. Proc Natl Acad Sci U S A. 1985 Apr;82(7):2143-7. [Article]
  5. Martin A, Escriou N, Chao SF, Girard M, Lemon SM, Wychowski C: Identification and site-directed mutagenesis of the primary (2A/2B) cleavage site of the hepatitis A virus polyprotein: functional impact on the infectivity of HAV RNA transcripts. Virology. 1995 Oct 20;213(1):213-22. [Article]
  6. Ticehurst JR, Racaniello VR, Baroudy BM, Baltimore D, Purcell RH, Feinstone SM: Molecular cloning and characterization of hepatitis A virus cDNA. Proc Natl Acad Sci U S A. 1983 Oct;80(19):5885-9. [Article]
  7. Jia XY, Ehrenfeld E, Summers DF: Proteolytic activity of hepatitis A virus 3C protein. J Virol. 1991 May;65(5):2595-600. [Article]
  8. Tesar M, Harmon SA, Summers DF, Ehrenfeld E: Hepatitis A virus polyprotein synthesis initiates from two alternative AUG codons. Virology. 1992 Feb;186(2):609-18. [Article]
  9. Tesar M, Jia XY, Summers DF, Ehrenfeld E: Analysis of a potential myristoylation site in hepatitis A virus capsid protein VP4. Virology. 1993 Jun;194(2):616-26. [Article]
  10. Jia XY, Summers DF, Ehrenfeld E: Primary cleavage of the HAV capsid protein precursor in the middle of the proposed 2A coding region. Virology. 1993 Mar;193(1):515-9. [Article]
  11. Tesar M, Pak I, Jia XY, Richards OC, Summers DF, Ehrenfeld E: Expression of hepatitis A virus precursor protein P3 in vivo and in vitro: polyprotein processing of the 3CD cleavage site. Virology. 1994 Feb;198(2):524-33. [Article]
  12. Probst C, Jecht M, Gauss-Muller V: Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1. J Virol. 1997 Apr;71(4):3288-92. [Article]
  13. Teterina NL, Bienz K, Egger D, Gorbalenya AE, Ehrenfeld E: Induction of intracellular membrane rearrangements by HAV proteins 2C and 2BC. Virology. 1997 Oct 13;237(1):66-77. [Article]
  14. Kusov YY, Probst C, Jecht M, Jost PD, Gauss-Muller V: Membrane association and RNA binding of recombinant hepatitis A virus protein 2C. Arch Virol. 1998;143(5):931-44. [Article]
  15. Probst C, Jecht M, Gauss-Muller V: Processing of proteinase precursors and their effect on hepatitis A virus particle formation. J Virol. 1998 Oct;72(10):8013-20. [Article]
  16. Feigelstock D, Thompson P, Mattoo P, Zhang Y, Kaplan GG: The human homolog of HAVcr-1 codes for a hepatitis A virus cellular receptor. J Virol. 1998 Aug;72(8):6621-8. [Article]
  17. Beneduce F, Ciervo A, Kusov Y, Gauss-Muller V, Morace G: Mapping of protein domains of hepatitis A virus 3AB essential for interaction with 3CD and viral RNA. Virology. 1999 Nov 25;264(2):410-21. [Article]
  18. Graff J, Richards OC, Swiderek KM, Davis MT, Rusnak F, Harmon SA, Jia XY, Summers DF, Ehrenfeld E: Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus. J Virol. 1999 Jul;73(7):6015-23. [Article]
  19. Jecht M, Probst C, Gauss-Muller V: Membrane permeability induced by hepatitis A virus proteins 2B and 2BC and proteolytic processing of HAV 2BC. Virology. 1998 Dec 5;252(1):218-27. [Article]
  20. Probst C, Jecht M, Gauss-Muller V: Intrinsic signals for the assembly of hepatitis A virus particles. Role of structural proteins VP4 and 2A. J Biol Chem. 1999 Feb 19;274(8):4527-31. [Article]
  21. Cohen L, Benichou D, Martin A: Analysis of deletion mutants indicates that the 2A polypeptide of hepatitis A virus participates in virion morphogenesis. J Virol. 2002 Aug;76(15):7495-505. [Article]
  22. Rachow A, Gauss-Muller V, Probst C: Homogeneous hepatitis A virus particles. Proteolytic release of the assembly signal 2A from procapsids by factor Xa. J Biol Chem. 2003 Aug 8;278(32):29744-51. Epub 2003 Jun 2. [Article]
  23. Peters H, Kusov YY, Meyer S, Benie AJ, Bauml E, Wolff M, Rademacher C, Peters T, Gauss-Muller V: Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization. Biochem J. 2005 Jan 15;385(Pt 2):363-70. [Article]
  24. Yang Y, Liang Y, Qu L, Chen Z, Yi M, Li K, Lemon SM: Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor. Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7253-8. Epub 2007 Apr 16. [Article]
  25. Zhang B, Seitz S, Kusov Y, Zell R, Gauss-Muller V: RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease. Biochem Biophys Res Commun. 2007 Dec 28;364(4):725-30. Epub 2007 Oct 15. [Article]
  26. Allaire M, Chernaia MM, Malcolm BA, James MN: Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature. 1994 May 5;369(6475):72-6. [Article]
  27. Bergmann EM, Mosimann SC, Chernaia MM, Malcolm BA, James MN: The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. J Virol. 1997 Mar;71(3):2436-48. [Article]
  28. Bergmann EM, Cherney MM, Mckendrick J, Frormann S, Luo C, Malcolm BA, Vederas JC, James MN: Crystal structure of an inhibitor complex of the 3C proteinase from hepatitis A virus (HAV) and implications for the polyprotein processing in HAV. Virology. 1999 Dec 5;265(1):153-63. [Article]
  29. Yin J, Cherney MM, Bergmann EM, Zhang J, Huitema C, Pettersson H, Eltis LD, Vederas JC, James MN: An episulfide cation (thiiranium ring) trapped in the active site of HAV 3C proteinase inactivated by peptide-based ketone inhibitors. J Mol Biol. 2006 Aug 25;361(4):673-86. Epub 2006 Jul 7. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04634N-BENZYLOXYCARBONYL-L-SERINE-BETALACTONEexperimentalunknownDetails
DB04029PhenylalanylamideexperimentalunknownDetails