Review
Nature Reviews Microbiology 4, 67-76 (January 2006) | doi:10.1038/nrmicro1326
Virus membrane-fusion proteins: more than one way to make a hairpin
Margaret Kielian1 & Félix A. Rey2 About the authors
Abstract
Structure–function studies have defined two classes of viral membrane-fusion proteins that have radically different architectures but adopt a similar overall 'hairpin' conformation to induce fusion of the viral and cellular membranes and therefore initiate infection. In both classes, the hairpin conformation is achieved after a conformational change is triggered by interaction with the target cell. This review will focus in particular on the properties of the more recently described class II proteins.
- View At a Glance
Author affiliations
- Department of Cell Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA. Email: kielian@aecom.yu.edu
- Virologie Moleculaire et Structurale, Unité Mixte de Recherche 2472/1157, Centre National de la Recherche Scientifique — Institut National de la Recherche Agronomique, 1 Avenue de la Terrasse, F-91198 Gif-sur-Yvette Cedex, France; and Virology Department, Institut Pasteur, 25 Rue du Docteur Roux, F-75724 Paris Cedex 15, France. Email: rey@vms.cnrs-gif.fr
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
When it's better to lie lowNature News and Views (25 May 1995)
Virology A class actNature News and Views (22 Jan 2004)
See all 4 matches for News And ViewsRESEARCH
Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformationThe EMBO Journal Article (25 Feb 2004)
Structure of the dengue virus envelope protein after membrane fusionNature Article (22 Jan 2004)
See all 23 matches for Research
