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Paramyxovirus membrane fusion: lessons from the F and HN atomic structures

Robert A Lamb1, Reay G Paterson, Theodore S Jardetzky

  • 1Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500, USA. ralamb@northwestern.edu

Virology
|December 21, 2005
PubMed

Insights

Paramyxoviruses use two key proteins, hemagglutinin/neuraminidase (HN) and fusion (F) proteins, to enter cells. Recent atomic structures of these viral proteins advance understanding of paramyxovirus entry mechanisms.

Area of Science:

  • Virology
  • Structural Biology
  • Cellular Biology

Background:

  • Paramyxoviruses infect cells via membrane fusion at neutral pH.
  • Viral entry relies on two key glycoproteins: attachment protein (e.g., hemagglutinin/neuraminidase or HN) and fusion (F) protein.
  • The precise trigger mechanism for paramyxovirus membrane fusion remains unclear.

Purpose of the Study:

  • To describe the knowledge gained from recent atomic structures of paramyxovirus HN and F proteins.
  • To elucidate the mechanism of viral membrane fusion in paramyxoviruses.

Main Methods:

  • Analysis of atomic structures of paramyxovirus fusion (F) and hemagglutinin/neuraminidase (HN) proteins.
  • Review of recent scientific literature on paramyxovirus glycoproteins.

Main Results:

  • Atomic structures of paramyxovirus F and HN proteins have been determined in the last five years.
  • These structures provide insights into the molecular mechanisms of viral entry.

Conclusions:

  • Structural data on F and HN proteins are crucial for understanding paramyxovirus cell entry.
  • Further research is needed to fully elucidate the trigger mechanism of paramyxovirus membrane fusion.

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