Structural basis of viral invasion: lessons from paramyxovirus F

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...

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Veröffentlicht in:Current opinion in structural biology Jg. 17; H. 4; S. 427 - 436
Hauptverfasser: Lamb, Robert A, Jardetzky, Theodore S
Format: Journal Article
Sprache:Englisch
Veröffentlicht: England Elsevier Ltd 01.08.2007
Schlagworte:
Crystallography, X-Ray
Human immunodeficiency virus
Membrane Fusion
Microscopy, Electron
Models, Molecular
Paramyxoviridae - physiology
Paramyxovirus
Protein Conformation
Protein Folding
Structure-Activity Relationship
Viral Fusion Proteins - chemistry
Viral Fusion Proteins - metabolism
ISSN:0959-440X, 1879-033X
Online-Zugang:Volltext
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Zusammenfassung: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.
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ISSN:0959-440X
1879-033X
DOI:10.1016/j.sbi.2007.08.016