Evidence that the fusion protein of respiratory syncytial virus exists as a dimer in its native form. Brief report.
Arch Virol
; 106(3-4): 327-34, 1989.
Article
em En
| MEDLINE
| ID: mdl-2774976
ABSTRACT
The quaternary structure of respiratory syncytial virus (RSV) fusion protein has been studied. Crosslinking studies were done to stabilize the noncovalently associated proteins. These stable, heat-resistant, covalently linked complexes were analyzed by sodium dodecyl sulfate-polyacrylamide electrophoresis. In situ crosslinking studies demonstrated that the fusion protein of RSV exists as a dimer in its native form on the surface of infected cells. The purified protein was also found to be present predominantly as a dimer. In addition, the results suggest that F1 subunits may play a role in the dimerization of the fusion protein.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Vírus Sinciciais Respiratórios
/
Proteínas Virais
/
Proteína HN
/
Antígenos Virais
Idioma:
En
Revista:
Arch Virol
Ano de publicação:
1989
Tipo de documento:
Article