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Titolo:
Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus
Autore:
Graff, J; Richards, OC; Swiderek, KM; Davis, MT; Rusnak, F; Harmon, SA; Jia, XY; Summers, DF; Ehrenfeld, E;
Indirizzi:
Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA Univ Calif Irvine Irvine CA USA 92697 iol & Biochem, Irvine, CA 92697 USA Univ Calif Irvine, Dept Microbiol & Mol Genet, Irvine, CA 92697 USA Univ Calif Irvine Irvine CA USA 92697 l & Mol Genet, Irvine, CA 92697 USA Inst City Hope, Beckman Res Inst, Duarte, CA 91010 USA Inst City Hope Duarte CA USA 91010 Beckman Res Inst, Duarte, CA 91010 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 7, volume: 73, anno: 1999,
pagine: 6015 - 6023
SICI:
0022-538X(199907)73:7<6015:HAVCPV>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECOMBINANT VACCINIA VIRUS; TANDEM MASS-SPECTROMETRY; A VIRUS; 3C PROTEINASE; SUBSTRATE-SPECIFICITY; SUBVIRAL PARTICLES; RNA TRANSCRIPTS; BS-C-1 CELLS; POLYPROTEIN; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Graff, J NIAID,0892, LID, Mol Hepatol Sect, Bldg 7,Room 200,7 Ctr Dr, Bethesda, MD 2 NIAID Bldg 7,Room 200,7 Ctr Dr Bethesda MD USA 20892 thesda, MD 2
Citazione:
J. Graff et al., "Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus", J VIROLOGY, 73(7), 1999, pp. 6015-6023

Abstract

Hepatitis A virus (HAV) encodes a single polyprotein which is posttranslationally processed into the functional structural and nonstructural proteins. Only one protease, viral protease 3C, has been implicated in the nine protein scissions. Processing of the capsid protein precursor region generatesa unique intermediate, PX (VP1-2A), which accumulates in infected cells and is assumed to serve as precursor to VP1 found in virions, although the details of this reaction have not been determined. Coexpression in transfected cells of a variety of P1 precursor proteins with viral protease 3C demonstrated efficient production of PX, as well as VP0 and VP3; however, no mature VP1 protein was detected. To identify the C-terminal amino acid residue of HAV VPI, we performed peptide sequence analysis by protease-catalyzed [O-18]H2O incorporation followed by liquid chromatography ion-trap microspraytandem mass spectrometry of HAV VP1 isolated from purified virions. Two different cell culture-adapted isolates of HAV, strains HM175pE and HM175p35,were used for these analyses. VP1 preparations from both virus isolates contained heterogeneous C termini. The predominant C-terminal amino acid in both virus preparations was VP1-Ser274, which is located N terminal to a methionine residue in VP1-2A. In addition, the analysis of HM175pE recovered smaller amounts of amino acids VP1-Glu273 and VP1-Thr272. In the case of HM175p35, which contains valine at amino acid position VP1-273, VP1-Thr272 wasfound in addition to VP1-Ser274. The data suggest that HAV 3C is not the protease responsible for generation of the VP1 C terminus. We propose the involvement of host cell protease(s) in the production of HAV VP1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 05:41:44