title: Alphavirus structure: activation for entry at the target cell surface.
abstract: A wealth of new data about the 3D organization of alphavirus particles was obtained in the last few years. This includes the crystal structures of the envelope glycoprotein complexes at neutral and at acid pH, as well as electron microscopy reconstructions of intact virions at neutral pH to resolutions between 7Å and 4Å. The combination has provided unprecedented detail in the description of the alphavirus virion. This review surveys the main features discovered and the implications for the biology of the virus, in particular for the process of disassembly of the glycoprotein shell during entry. The major outstanding questions in this area are also identified and discussed.
authors.affiliation: Institut Pasteur, Unité de Virologie Structurale, CNRS UMR 3569, Paris, France.
authors.forename: Marie-Christine
authors.initials: MC
authors.lastname: Vaney
authors.forename: Stéphane
authors.initials: S
authors.lastname: Duquerroy
authors.forename: Félix A
authors.initials: FA
authors.lastname: Rey
mesh_terms: D000524:Alphavirus / Q000502:physiology* / Q000648:ultrastructure*; D000818:Animals; D018360:Crystallography, X-Ray; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D014771:Virion / Q000502:physiology* / Q000648:ultrastructure*; D053586:Virus Internalization