Hydrophobic and charged residues in the central segment of the measles virus hemagglutinin stalk mediate transmission of the fusion-triggering signal.
J Virol
; 87(18): 10401-4, 2013 Sep.
Article
em En
| MEDLINE
| ID: mdl-23864629
ABSTRACT
The pH-independent measles virus membrane fusion process begins when the attachment protein H binds to a receptor. Knowing that the central segment of the tetrameric H stalk transmits the signal to the fusion protein trimer, we investigated how. We document that exact conservation of most residues in the 92 through 99 segment is essential for function. In addition, hydrophobic and charged residues in the 104 through 125 segment, arranged with helical periodicity, are critical for F protein interactions and signal transmission.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas Virais
/
Internalização do Vírus
/
Vírus do Sarampo
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article