English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/8549
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: blexibility in aphthovirus receptor usage

Autor Baranowski, Eric; Ruiz-Jarabo, Carmen M.; Sevilla, Noemí ; Andreu, David; Beck, Ewald; Domingo, Esteban
Palabras clave Foot-and-mouth disease virus
Fecha de publicación 2000
EditorAmerican Society for Microbiology
Citación Journal of Virology, 2000, p. 1641-1647, Vol. 74, No. 4
ResumenCell surface molecules that can act as virus receptors may exert an important selective pressure on RNA viral quasispecies. Large population passages of foot-and-mouth disease virus (FMDV) in cell culture select for mutant viruses that render dispensable a highly conserved Arg-Gly-Asp (RGD) motif responsible for integrin receptor recognition. Here, we provide evidence that viability of recombinant FMDVs including a Asp-143Gly change at the RGD motif was conditioned by a number of capsid substitutions selected upon FMDV evolution in cell culture. Multiply passaged FMDVs acquired the ability to infect human K-562 cells, which do not express integrin alpha-v-beta-3. In contrast to previously described cell culture-adapted FMDVs, the RGD-independent infection did not require binding to the surface glycosaminoglycan heparan sulfate (HS). Viruses which do not bind HS and lack the RGD integrin-binding motif replicate efficiently in BHK-21 cells. Interestingly, FMDV mutants selected from the quasispecies for the inability to bind heparin regained sensitivity to inhibition by a synthetic peptide that represents the G-H loop of VP1. Thus, a single amino acid replacement leading to loss of HS recognition can shift preferential receptor usage of FMDV from HS to integrin. These results indicate at least three different mechanisms for cell recognition by FMDV and suggest a potential for this virus to use multiple, alternative receptors for entry even into the same cell type
Versión del editorhttp://jvi.asm.org/cgi/content/full/74/4/1641
URI http://hdl.handle.net/10261/8549
ISSN0022-538X (print)
1098-5514 (online)
Aparece en las colecciones: (CBM) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
EBaranowski_JVirol_1641.pdf118,7 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.