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Structural basis of viral invasion: lessons from paramyxovirus F

Robert A Lamb1, Theodore S Jardetzky

  • 1Department of Biochemistry, Molecular Biology, Cell Biology, Northwestern University, Evanston, IL 60208, USA.

Current Opinion in Structural Biology
|September 18, 2007
PubMed

Insights

Structural studies of viral fusion proteins reveal how enveloped viruses enter cells. Crystal structures of the paramyxovirus F protein show a novel architecture undergoing significant refolding during membrane fusion.

Area of Science:

  • Structural biology
  • Virology
  • Molecular biology

Background:

  • Enveloped viruses utilize glycoproteins to mediate cell entry.
  • Viral membrane fusion is a critical step in infection, involving significant protein conformational changes.
  • Class I viral fusion proteins, though structurally distinct, share mechanistic similarities.

Purpose of the Study:

  • To elucidate the structural basis of paramyxovirus F protein-mediated membrane fusion.
  • To understand the conformational transitions involved in viral entry.

Main Methods:

  • X-ray crystallography was employed to determine the structures of the paramyxovirus F protein.
  • Analysis of pre-fusion and post-fusion conformations.

Main Results:

  • Crystal structures revealed a novel architecture for the paramyxovirus F protein.
  • The protein undergoes large-scale, irreversible refolding from pre-fusion to post-fusion states.
  • These structural changes provide mechanistic insights into membrane fusion.

Conclusions:

  • The findings expand the understanding of diverse viral membrane fusion machines.
  • The novel architecture and refolding mechanism of the paramyxovirus F protein offer new perspectives on viral entry.

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