Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion.
Nat Commun
; 2: 577, 2011 Dec 06.
Article
em En
| MEDLINE
| ID: mdl-22146396
ABSTRACT
Multiple surface envelope proteins are involved in the human herpes simplex virus type 1 entry and fusion. Among them, glycoprotein D (gD) has an important role by binding to the host receptors such as herpes virus entry mediator and nectin-1. Although the complex structure of gD with herpes virus entry mediator has been established, the binding mode of gD with the nectin-1 is elusive. Nectin-1 is a member of the immunoglobulin (Ig)-like (three Ig-like domains) cell adhesion molecules and is believed to form a homodimer to exert its functions. Here we report the complex structure of gD and nectin-1 (three Ig domains), revealing that gD binds the first Ig domain of nectin-1 in a similar mode to the nectin-1 homodimer interaction. The key amino acids responsible for nectin-1 dimerization are also used for gD/nectin-1 binding. This result indicates that binding of gD to nectin-1 would preclude the nectin-1 dimerization, consequently abolishing its cell adhesion function.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Receptores Virais
/
Proteínas Recombinantes
/
Moléculas de Adesão Celular
/
Proteínas do Envelope Viral
/
Herpesvirus Humano 1
/
Internalização do Vírus
/
Herpes Simples
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article