Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: implications for F-G complex formation.
J Virol
; 83(17): 8998-9001, 2009 Sep.
Article
em En
| MEDLINE
| ID: mdl-19553334
ABSTRACT
Hendra virus F protein-promoted membrane fusion requires the presence of the viral attachment protein, G. However, events leading to the association of these glycoproteins remain unclear. Results presented here demonstrate that Hendra virus G undergoes slower secretory pathway trafficking than is observed for Hendra virus F. This slowed trafficking is not dependent on the G protein cytoplasmic tail, the presence of the G receptor ephrin B2, or interaction with other viral proteins. Instead, Hendra virus G was found to undergo intrinsically slow oligomerization within the endoplasmic reticulum. These results suggest that the critical F-G interactions occur only after the initial steps of synthesis and cellular transport.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas do Envelope Viral
/
Proteínas Virais de Fusão
/
Vírus Hendra
/
Multimerização Proteica
Limite:
Animals
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article