2005
DOI: 10.1590/s0100-879x2005000600002
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Abstract: Enveloped viruses always gain entry into the cytoplasm by fusion of their lipid envelope with a cell membrane. Some enveloped viruses fuse directly with the host cell plasma membrane after virus binding to the cell receptor. Other enveloped viruses enter the cells by the endocytic pathway, and fusion depends on the acidification of the endosomal compartment. In both cases, virus-induced membrane fusion is triggered by conformational changes in viral envelope glycoproteins. Two different classes of viral fusion… Show more

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Cited by 35 publications
(30 citation statements)
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“…Thus, reversibility of the low-pH-induced fusogenic transition is not necessary for these proteins. Biochemical, structural and functional properties of rhabdovirus G suggested that it was distinct from both class I and class II viral fusion proteins that had been already described [29,53]. Indeed, the pH-dependent equilibrium between the different states of G, the absence of predicted a-helical coiled-coil motif characteristic of class I viral fusion proteins [40] and the absence of activating cleavage (neither in G nor in an accompanying protein) strongly suggested that G could define a new category of fusogenic glycoproteins.…”
Section: Class I and Class Ii Fusion Proteinsmentioning
confidence: 84%
“…Thus, reversibility of the low-pH-induced fusogenic transition is not necessary for these proteins. Biochemical, structural and functional properties of rhabdovirus G suggested that it was distinct from both class I and class II viral fusion proteins that had been already described [29,53]. Indeed, the pH-dependent equilibrium between the different states of G, the absence of predicted a-helical coiled-coil motif characteristic of class I viral fusion proteins [40] and the absence of activating cleavage (neither in G nor in an accompanying protein) strongly suggested that G could define a new category of fusogenic glycoproteins.…”
Section: Class I and Class Ii Fusion Proteinsmentioning
confidence: 84%
“…As the presenting protein, to facilitate viropexis membrane fusion of the G-protein, viruses are required to reconfigure from a non-fusogenic to a fusogenic state, reviewed by Da Poian et al [46]. Using a model devised by Walker & Kongsuwan [47], Rocha et al [48] proposed hypothetical fusion peptides are positioned between residues 142 and 159.…”
Section: Discussionmentioning
confidence: 99%
“…Viral fusion proteins are grouped in three major classes based on structural differences (Da Poian, Carneiro and Stauffer 2005;Harrison 2008;Modis 2014). Flaviviruses and alphaviruses bear class II fusion proteins, which are β-sheet-rich proteins that form homodimers at neutral pH, with the hydrophobic fusion loop located at the distal end of DII, buried in the dimer interface (Pierson and Kielian 2013).…”
Section: E Protein-mediated Membrane Fusionmentioning
confidence: 99%