Role of the Glu residues of the influenza hemagglutinin fusion peptide in the pH dependence of fusion activity.
Virology
; 289(2): 353-61, 2001 Oct 25.
Article
en En
| MEDLINE
| ID: mdl-11689057
To elucidate the role of the fusion peptide in influenza hemagglutinin (HA)-mediated fusion, we compared pH-dependent conformational changes and fusion mediated by wild-type and a mutant HA in which Glu residues at positions 11 and 15 of the fusion peptide are substituted for valine. The pH dependence of conformational changes and kinetics of fusion with erythrocytes was the same for both forms of HA. The time for commitment and the temperature dependence of HA-mediated fusion were also the same. However, striking differences were observed between wild-type and mutant fusion peptides in their interactions with lipid membranes at neutral and acidic pH. Since elimination of the negatively charged residues allows the exposed fusion peptide to penetrate the bilayer at pH values closer to neutral, but does not affect conformational changes and fusion activity in intact HA, we conclude that conformational changes are tightly coupled to fusion peptide insertion in the overall HA-mediated fusion cascade.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ácido Glutámico
/
Glicoproteínas Hemaglutininas del Virus de la Influenza
/
Fusión de Membrana
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Virology
Año:
2001
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos