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Titolo:
VESICULAR STOMATITIS-VIRUS TRANSCRIPTION INHIBITED BY PURIFIED MXA PROTEIN
Autore:
SCHWEMMLE M; WEINING KC; RIGHTER MF; SCHUMACHER B; STAEHELI P;
Indirizzi:
UNIV FREIBURG,INST MED MIKROBIOL & HYG,DEPT VIROL,HERMANN HERDER STR 11 D-79008 FREIBURG GERMANY UNIV FREIBURG,INST MED MIKROBIOL & HYG,DEPT VIROL D-79008 FREIBURG GERMANY
Titolo Testata:
Virology
fascicolo: 1, volume: 206, anno: 1995,
pagine: 545 - 554
SICI:
0042-6822(1995)206:1<545:VSTIBP>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESSENGER-RNA SYNTHESIS; INFLUENZA-VIRUS; ESCHERICHIA-COLI; GENOME RNA; EXPRESSION; GENE; CLONING; RHABDOVIRUS; CONTAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
M. Schwemmle et al., "VESICULAR STOMATITIS-VIRUS TRANSCRIPTION INHIBITED BY PURIFIED MXA PROTEIN", Virology, 206(1), 1995, pp. 545-554

Abstract

MxA is a GTPase encoded by an interferon-inducible human gene. Its constitutive expression renders transfected mammalian cells resistant toinfections with several different RNA viruses, including vesicular stomatitis virus (VSV). Differences in viral RNA levels of VSV-infected cells either expressing or lacking MxA indicated that VSV mRNA synthesis is the principal target of MxA action. We now used purified histidine-tagged MxA (His-MxA) that we produced in Escherichia coil to successfully inhibit VSV in vitro transcription, a reaction catalyzed by VSVribonucleoprotein complexes isolated from virus-infected cells or from purified virions. MxA was inactive when added to preformed VSV mRNAs, arguing against the possibility that it has a negative effect on viral RNA stability. MxA inhibited both leader RNA and mRNA synthesis of VSV, suggesting that it interfered with transcription initiation. The degree of VSV inhibition correlated directly with the specific GTPase activities of the various wild-type MxA preparations. No inhibition ofviral mRNA synthesis was observed when a C-terminally truncated, GTPase-inactive variant of His-MxA was added to the transcription reactions. Purified His-MxA-E645R, a mutant of MxA with normal GTPase activitywhose range of antiviral activity in vivo is altered so that it no longer inhibits VSV, showed no inhibitory effect on VSV in vitro transcription. Since MxA inhibited VSV RNA synthesis in the presence of GMP-PNP or GTP gamma S, GTP analogs that are readily accepted by the viral polymerase but cannot be hydrolyzed by MxA, the possibility was excluded that MxA acts by depleting the viral polymerase for its nucleotide substrates. Thus, binding of GTP rather than its hydrolysis seems of importance for the anti-VSV activity of MxA. (C) 1995 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 16:33:20