Crystal structure of glycoprotein E2 from bovine viral diarrhea virus.
Proc Natl Acad Sci U S A
; 110(17): 6805-10, 2013 Apr 23.
Article
em En
| MEDLINE
| ID: mdl-23569276
ABSTRACT
Pestiviruses, including bovine viral diarrhea virus, are important animal pathogens and are closely related to hepatitis C virus, which remains a major global health threat. They have an outer lipid envelope bearing two glycoproteins, E1 and E2, required for cell entry. They deliver their genome into the host cell cytoplasm by fusion of their envelope with a cellular membrane. The crystal structure of bovine viral diarrhea virus E2 reveals a unique protein architecture consisting of two Ig-like domains followed by an elongated ß-stranded domain with a new fold. E2 forms end-to-end homodimers with a conserved C-terminal motif rich in aromatic residues at the contact. A disulfide bond across the interface explains the acid resistance of pestiviruses and their requirement for a redox activation step to initiate fusion. From the structure of E2, we propose alternative possible membrane fusion mechanisms. We expect the pestivirus fusion apparatus to be conserved in hepatitis C virus.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Modelos Moleculares
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Proteínas do Envelope Viral
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Vírus da Diarreia Viral Bovina Tipo 1
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Estados Unidos