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- W2120318443 endingPage "31" @default.
- W2120318443 startingPage "21" @default.
- W2120318443 abstract "Rabies virus is a member of the rhabdovirus family. It enters cells by a process of receptor mediated endocytosis. Following this step, the viral envelope fuses with the endosomal membrane to allow release of the viral nucleocapsid into the cytoplasm. Fusion is induced by the low pH of the endosomal compartment and is mediated by the single viral glycoprotein G, a homotrimeric integral membrane protein. Rabies virus fusion properties are related to different conformational states of G. By different biochemical and biophysical approaches, it has been demonstrated that G can assume at least three different states: the native (N) state detected at the viral surface above pH 7, the activated (A) hydrophobic state which interacts with the target membrane as a first step of the fusion process, and the fusion inactive (I) conformation. Differently from other fusogenic viruses for which low pH-induced conformational changes are irreversible, there is a pH dependent equilibrium between these states, the equilibrium being shifted toward the I-state at low pH. The objective of this review is to detail recent findings on rhabdovirus-induced membrane fusion and to underline the differences that exist between this viral family and influenza virus which is the best known fusogenic virus. These differences have to be taken into consideration if one wants to have a global understanding of virus-induced membrane fusion." @default.
- W2120318443 created "2016-06-24" @default.
- W2120318443 creator A5022285779 @default.
- W2120318443 creator A5028981918 @default.
- W2120318443 creator A5032811653 @default.
- W2120318443 creator A5042051258 @default.
- W2120318443 creator A5067728061 @default.
- W2120318443 creator A5084267146 @default.
- W2120318443 date "1999-01-01" @default.
- W2120318443 modified "2023-10-10" @default.
- W2120318443 title "Rabies virus-induced membrane fusion" @default.
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