Membrane localization of Junín virus glycoproteins requires cholesterol and cholesterol rich membranes
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 different cholesterol-lowering agents on Junín virus (JUNV) multiplication. We found that cholesterol cell depleti...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2013 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/66284 |
| Acceso en línea: | http://hdl.handle.net/11336/66284 |
| Access Level: | acceso abierto |
| Palabra clave: | Cholesterol Junv Membrane Glycoprotein https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Sumario: | 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 different cholesterol-lowering agents on Junín virus (JUNV) multiplication. We found that cholesterol cell depletion reduced JUNV glycoproteins (GPs) membrane expression and virus budding. Analysis of membrane protein insolubility in Triton X-100 suggested that JUNV GPs associate with cholesterol enriched membranes. Rafts dissociation conditions as warm detergent extraction and cholesterol removal by methyl-b-cyclodextrin compound showed to impair GPs cholesterol enriched membrane association.Analysis of GPs transfected cells showed similar results suggesting that membrane raft association is independent of other viral proteins. |
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