Author: Albertini, Aurélie; Bressanelli, Stéphane; Lepault, Jean; Gaudin, Yves
                    Title: Chapter 3 Structure and Working of Viral Fusion Machinery  Cord-id: fnal68y4  Document date: 2011_12_31
                    ID: fnal68y4
                    
                    Snippet: Publisher Summary This chapter discusses the structure and working of viral fusion machinery. The entry of enveloped viruses into cells requires the fusion of viral and cellular membranes, driven by conformational changes in viral glycoproteins. Structural studies have defined three classes of viral membrane fusion proteins. Despite their different structural organizations, all seem to have a common mechanism of action that generates the same lipid organizations during the fusion pathway. The en
                    
                    
                    
                     
                    
                    
                    
                    
                        
                            
                                Document: Publisher Summary This chapter discusses the structure and working of viral fusion machinery. The entry of enveloped viruses into cells requires the fusion of viral and cellular membranes, driven by conformational changes in viral glycoproteins. Structural studies have defined three classes of viral membrane fusion proteins. Despite their different structural organizations, all seem to have a common mechanism of action that generates the same lipid organizations during the fusion pathway. The entry of enveloped viruses into host cells requires binding of the virus to one or more receptors present at the cell surface, followed by fusion of the viral envelope with a cellular membrane. These steps are mediated by virally encoded glycoproteins that promote both receptor recognition and membrane fusion. The first crystal structure of a viral fusion protein ectodomain that has been determined is that of influenza virus hemagglutinin (HA) in its prefusion conformation. The structures of viral fusion glycoproteins, of which the conformational change is triggered at low pH, has allowed the identification of amino acid residues that play the role of pH-sensitive molecular switches.
 
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