IQUIBICEN   23947
INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CIENCIAS EXACTAS Y NATURALES
Unidad Ejecutora - UE
artículos
Título:
Membrane localizacion of Junín virus glycoproteins requires cholesterol and cholesterol rich membranes integrity
Autor/es:
SANDRA M. CORDO, AYELÉN VALKO, GUADALUPE M. MARTINEZ AND NÉLIDA A. CANDURRA
Revista:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Editorial:
ACADEMIC PRESS INC ELSEVIER SCIENCE
Referencias:
Lugar: Amsterdam; Año: 2013 vol. 430 p. 912 - 917
ISSN:
0006-291X
Resumen:
Arenavirus morphogenesis and budding occurs at cellular plasma membrane; however, the nature of membrane assembly sites remains poorly understood. In this study we examined the effect of several cholesterol-lowering agents on Junín virus (JUNV) multiplication. We found that cholesterol cell depletion reduced JUNV infectivity and glycoprotein 1 (GP1) expression. Analysis of membrane protein insolubility in Triton X-100 suggested that JUNV GP1 associate with cholesterol enriched membranes. Rafts dissociation conditions like warm detergent extraction as well as cholesterol removal by methyl-β-cyclodextrin compound shown to impaired JUNV GP1 cholesterol enriched membrane association. Specific cross-linking experiment with anti-GP1 antibodies demonstrated to improve detergent insolubility at 37ºC by rafts stabilization. These results show evidence of JUNV GP1 association to cholesterol enriched membranes. Functional role of these microdomains in the process of viral assembly and budding must be disclosed