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Titolo:
INVOLVEMENT OF THE MUTATED M-PROTEIN IN ALTERED BUDDING POLARITY OF APANTROPIC MUTANT, F1-R, OF SENDAI VIRUS
Autore:
TASHIRO M; MCQUEEN NL; SETO JT; KLENK HD; ROTT R;
Indirizzi:
NATL INST HLTH,DEPT VIROL 1,SHINJUKU KU,TOYAMA 1-23-1 TOKYO 162 JAPAN CALIF STATE UNIV LOS ANGELES,DEPT BIOL & MICROBIOL LOS ANGELES CA 90032 UNIV MARBURG,INST VIROL D-35037 MARBURG GERMANY UNIV GIESSEN,INST VIROL D-35392 GIESSEN GERMANY
Titolo Testata:
Journal of virology
fascicolo: 9, volume: 70, anno: 1996,
pagine: 5990 - 5997
SICI:
0022-538X(1996)70:9<5990:IOTMMI>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
DARBY CANINE KIDNEY; INTESTINAL EPITHELIAL-CELLS; PLASMA-MEMBRANE PROTEINS; MDCK CELLS; GOLGI-COMPLEX; FUSION GLYCOPROTEIN; NUCLEOTIDE-SEQUENCE; APICAL MEMBRANE; MICROTUBULES; ORGANIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
M. Tashiro et al., "INVOLVEMENT OF THE MUTATED M-PROTEIN IN ALTERED BUDDING POLARITY OF APANTROPIC MUTANT, F1-R, OF SENDAI VIRUS", Journal of virology, 70(9), 1996, pp. 5990-5997

Abstract

Wild-type Sendai virus buds at the apical plasma membrane domain of polarized epithelial MDCK cells, whereas a pantropic mutant, F1-R, budsat both the apical and basolateral domains. In F1-R-infected cells, polarized protein transport and the microtubule network are impaired. It has been suggested that the mutated F and/or M proteins in F1-R are responsible for these changes (M, Tashiro, J. T. Seto, H.-D. Klenk, and R. Rott, J. Virol. 67:5902-5910, 1993). To clarify which gene or mutation(s) was responsible for the microtubule disruption which leads toaltered budding of FL-R, MDCK cell lines containing the M gene of either the wild type or F1-R were established. When mild-type M protein was expressed at a level corresponding to that synthesized in virus-infected cells, cellular polarity and the integrity of the microtubules were affected to some extent. On the other hand, expression of the mutated FI-R M protein resulted in the formation of giant cells about 40 times larger than normal MDCK cells. Under these conditions, the effects on the microtubule network were enhanced. The microtubules were disrupted and polarized protein transport was impaired as indicated by thenonpolarized secretion of gp80, a host cell glycoprotein normally secreted from the apical domain, and bipolar budding of wild-type and FI-R Sendai viruses. The mutated F glycoprotein of FI-R was transported bipolarly in cells expressing the F1-R M protein, whereas it was transported predominantly to the apical domain when expressed alone or in cells coexpressing the wild-type M protein. These findings indicate thatthe M protein of F1-R is involved in the disruption of the microtubular network, leading to impairment of cellular polarity, bipolar transport of the F glycoprotein, and bipolar budding of the virus.

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Documento generato il 17/01/20 alle ore 20:09:38