Viral fusion mechanisms

• Published in: Uirusu Vol. 55; no. 2; pp. 207 - 219
• Main Author: TSURUDOME, Masato
• Format: Journal Article
• Language: Japanese
• Published: Japan The Japanese Society for Virology 2005
• Subjects: Alphavirus; Crystallography, X-Ray; Flavivirus; Fusion Regulatory Protein-1 - physiology; Hemagglutinins, Viral - chemistry; Hemagglutinins, Viral - physiology; Hydrogen-Ion Concentration; Membrane Fusion; Membrane Microdomains - physiology; Paramyxoviridae - physiology; Paramyxovirus; Protein Conformation; rhoA GTP-Binding Protein - physiology; Viral Fusion Proteins - chemistry; Viral Fusion Proteins - classification; Viral Fusion Proteins - physiology
• ISSN: 0042-6857; 1884-3433
• DOI: 10.2222/jsv.55.207

The majority of viral fusion proteins can be divided into two classes. The influenza hemagglutinin (HA) belongs to the class I fusion proteins and undergoes a series of conformational changes at acidic pH, leading to membrane fusion. The crystal structures of the prefusion and the postfusion forms of HA have been revealed in 1981 and 1994, respectively. On the basis of these structures, a model for the mechanism of membrane fusion mediated by the conformational changes of HA has been proposed. The flavivirus E and alphavirus E1 proteins belong to the class II fusion proteins and mediate membrane fusion at acidic pH. Their prefusion structures are distinct from that of HA. Last year, however, it has become evident that the postfusion structures of these class I and class II fusion proteins are similar. The paramyxovirus F protein belongs to the class I fusion proteins. In contrast to HA, an interaction between F and its homologous attachment protein is required for F to undergo the conformational changes. Since F mediates fusion at neutral pH, the infected cells can fuse with neighboring uninfected cells. The crystal structures of F and the attachment protein HN have recently been clarified, which will facilitate studies of the molecular mechanism of F-mediated membrane fusion.