Molecular mechanism of SCARB2-mediated attachment and uncoating of EV71
Protein & Cell
; (12): 692-703, 2014.
Article
en En
| WPRIM
| ID: wpr-757655
Biblioteca responsable:
WPRO
ABSTRACT
Unlike the well-established picture for the entry of enveloped viruses, the mechanism of cellular entry of non-enveloped eukaryotic viruses remains largely mysterious. Picornaviruses are representative models for such viruses, and initiate this entry process by their functional receptors. Here we present the structural and functional studies of SCARB2, a functional receptor of the important human enterovirus 71 (EV71). SCARB2 is responsible for attachment as well as uncoating of EV71. Differences in the structures of SCARB2 under neutral and acidic conditions reveal that SCARB2 undergoes a pivotal pH-dependent conformational change which opens a lipid-transfer tunnel to mediate the expulsion of a hydrophobic pocket factor from the virion, a pre-requisite for uncoating. We have also identified the key residues essential for attachment to SCARB2, identifying the canyon region of EV71 as mediating the receptor interaction. Together these results provide a clear understanding of cellular attachment and initiation of uncoating for enteroviruses.
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Fisiología
/
Unión Proteica
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Conformación Proteica
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Ácidos
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Virión
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ARN Viral
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Datos de Secuencia Molecular
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Química
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Secuencia de Aminoácidos
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Homología de Secuencia de Aminoácido
Tipo de estudio:
Prognostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Protein & Cell
Año:
2014
Tipo del documento:
Article