Location of the Spike Glycoproteins in the Semliki Forest Virus Membrane
AUTOR(ES)
Garoff, Henrik
RESUMO
Labeling experiments with formyl-[35S]-methionyl sulfone methylphosphate and crosslinking studies with dimethylsuberimidate suggest that the spike glycoproteins of Semliki Forest virus extend through the viral membrane into close contact with the nucleocapsid. Based on this finding, we present a mechanism for the formation of virus-specific patches in the host cell plasma membrane during virus assembly.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=434312Documentos Relacionados
- Spike protein oligomerization control of Semliki Forest virus fusion.
- Different membrane anchors allow the Semliki Forest virus spike subunit E2 to reach the cell surface.
- Role of spike protein conformational changes in fusion of Semliki Forest virus.
- Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein.
- Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.
