Structural basis of viral invasion: lessons from paramyxovirus F.

Abstract

The structures of glycoproteins that mediate enveloped virus entry into cells have revealed dramatic structural changes that accompany membrane fusion and provided mechanistic insights into this process. The group of class I viral fusion proteins includes the influenza hemagglutinin, paramyxovirus F, HIV env, and other mechanistically related fusogens, but these proteins are unrelated in sequence and exhibit clearly distinct structural features. Recently determined crystal structures of the paramyxovirus F protein in two conformations, representing pre-fusion and post-fusion states, reveal a novel protein architecture that undergoes large-scale, irreversible refolding during membrane fusion, extending our understanding of this diverse group of membrane fusion machines.

• Authors: Robert A Lamb, Theodore S Jardetzky
• Journal: Current opinion in structural biology (Curr Opin Struct Biol) Vol. 17 Issue 4 Pg. 427-36 (Aug 2007) ISSN: 0959-440X [Print] England
• PMID: 17870467 (Publication Type: Comparative Study, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Viral Fusion Proteins

Topics

• Crystallography, X-Ray
• Membrane Fusion
• Microscopy, Electron
• Models, Molecular
• Paramyxoviridae (physiology)
• Protein Conformation
• Protein Folding
• Structure-Activity Relationship
• Viral Fusion Proteins (chemistry, metabolism)