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Titolo:
VITRONECTIN RECEPTOR ANTIBODIES INHIBIT INFECTION OF HELA AND A549 CELLS BY ADENOVIRUS-TYPE-12 BUT NOT BY ADENOVIRUS TYPE-2
Autore:
BAI M; CAMPISI L; FREIMUTH P;
Indirizzi:
BROOKHAVEN NATL LAB,DEPT BIOL UPTON NY 11973 BROOKHAVEN NATL LAB,DEPT BIOL UPTON NY 11973
Titolo Testata:
Journal of virology
fascicolo: 9, volume: 68, anno: 1994,
pagine: 5925 - 5932
SICI:
0022-538X(1994)68:9<5925:VRAIIO>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
PENTON BASE; ATTACHMENT; ADHESION; INTEGRIN-ALPHA-V-BETA-3; SEQUENCES; INTEGRINS; SURFACE; VIRION; RGD;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
M. Bai et al., "VITRONECTIN RECEPTOR ANTIBODIES INHIBIT INFECTION OF HELA AND A549 CELLS BY ADENOVIRUS-TYPE-12 BUT NOT BY ADENOVIRUS TYPE-2", Journal of virology, 68(9), 1994, pp. 5925-5932

Abstract

The penton base gene from adenovirus type 12 (Ad12) was sequenced andencodes a 497-residue polypeptide, 74 residues shorter than the penton base from Ad2. The Ad2 and Ad12 proteins are highly conserved at theamino- and carboxy-terminal ends but diverge radically in the centralregion, where 63 residues are missing from the Ad12 sequence. Conserved within this variable region is the sequence Arg-Gly-Asp (RGD), which, in the Ad2 penton base, binds to integrins in the target cell membrane, enhancing the rate or the efficiency of infection. The Ad12 penton base was expressed in Escherichia coli, and the purified refolded protein assembled in vitro with Ad2 fibers. In contrast to the Ad2 penton base, the Ad12 protein failed to cause the rounding of adherent cells or to promote attachment of HeLa S3 suspension cells; however, A549 cells did attach to surfaces coated vith either protein and pretreatment of the cells with an integrin alpha v beta 3 monoclonal antibody reduced attachment to background levels. Treatment of HeLa ind A549 cells with integrin alpha v beta 3 or alpha v beta 5 monoclonal antibodiesor with an RGD-containing fragment of the Ad2 penton base protein inhibited infection by Ad12 but had no effect on and in some cases enhanced infection by Ad2. Purified Ad2 fiber protein reduced the binding ofradiolabeled Ad2 and Ad12 virions to HeLa and A549 cells nearly to background levels, but the concentrations of fiber that strongly inhibited infection by Ad2 only weakly inhibited Ad12 infection. These data suggest that alpha v-containing integrins alone may be sufficient to support infection by Ad12 and that this pathway is not efficiently used by Ad2.

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Documento generato il 13/07/20 alle ore 10:55:35