Potent neutralization of hepatitis A virus reveals a receptor mimic mechanism and the receptor recognition site.
Proc Natl Acad Sci U S A
; 114(4): 770-775, 2017 01 24.
Article
en En
| MEDLINE
| ID: mdl-28074040
ABSTRACT
Hepatitis A virus (HAV) infects â¼1.4 million people annually and, although there is a vaccine, there are no licensed therapeutic drugs. HAV is unusually stable (making disinfection problematic) and little is known of how it enters cells and releases its RNA. Here we report a potent HAV-specific monoclonal antibody, R10, which neutralizes HAV infection by blocking attachment to the host cell. High-resolution cryo-EM structures of HAV full and empty particles and of the complex of HAV with R10 Fab reveal the atomic details of antibody binding and point to a receptor recognition site at the pentamer interface. These results, together with our observation that the R10 Fab destabilizes the capsid, suggest the use of a receptor mimic mechanism to neutralize virus infection, providing new opportunities for therapeutic intervention.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Virus de la Hepatitis A
/
Anticuerpos Neutralizantes
Límite:
Animals
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Female
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Humans
Idioma:
En
Año:
2017
Tipo del documento:
Article