Document Detail


Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus.
MedLine Citation:
PMID:  16407067     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for inducing membrane fusion, triggered by exposure to the acidic environment of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to interact with the target membrane, and, at the same time, to rearrange into E1 homotrimers that drive the membrane fusion reaction. We previously reported a preliminary Calpha trace of the monomeric E1 glycoprotein ectodomain and its organization on the virus particle. We also reported the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution and describe the amino acids involved in contacts in the virion. These results identify the major determinants for the E1/E2 icosahedral shell formation and open the way to rational mutagenesis approaches to shed light on SFV assembly.
Authors:
Alain Roussel; Julien Lescar; Marie-Christine Vaney; Gisela Wengler; Gerd Wengler; Félix A Rey
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Structure (London, England : 1993)     Volume:  14     ISSN:  0969-2126     ISO Abbreviation:  Structure     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2006-01-12     Completed Date:  2006-04-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  101087697     Medline TA:  Structure     Country:  United States    
Other Details:
Languages:  eng     Pagination:  75-86     Citation Subset:  IM    
Affiliation:
Laboratoire de Virologie Moléculaire and Structurale, UMR 2472/1157 CNRS-INRA and IFR 115, 91198 Gif-sur-Yvette Cedex, France.
Data Bank Information
Bank Name/Acc. No.:
PDB/2ALA
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Crystallography, X-Ray
Glycoproteins
Histidine / genetics
Lipids / physiology
Membrane Fusion / physiology
Membrane Fusion Proteins / chemistry,  genetics,  metabolism
Membrane Glycoproteins / chemistry*,  genetics,  metabolism*
Molecular Sequence Data
Mutation
Protein Binding
Protein Structure, Tertiary
Semliki forest virus / chemistry*,  genetics,  metabolism*
Viral Envelope Proteins / chemistry*,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/E1 glycoprotein, Semliki forest virus; 0/Glycoproteins; 0/Lipids; 0/Membrane Fusion Proteins; 0/Membrane Glycoproteins; 0/Viral Envelope Proteins; 71-00-1/Histidine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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