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

Robert A. Lamb*, Reay G. Paterson, Theodore S. Jardetzky

*Corresponding author for this work

Research output: Contribution to journalReview article

180 Scopus citations

Abstract

Paramyxoviruses enter cells by fusion of their lipid envelope with the target cell plasma membrane. Fusion of the viral membrane with the plasma membrane allows entry of the viral genome into the cytoplasm. For paramyxoviruses, membrane fusion occurs at neutral pH, but the trigger mechanism that controls the viral entry machinery such that it occurs at the right time and in the right place remains to be elucidated. Two viral glycoproteins are key to the infection process-an attachment protein that varies among different paramyxoviruses and the fusion (F) protein, which is found in all paramyxoviruses. For many of the paramyxoviruses (parainfluenza viruses 1-5, mumps virus, Newcastle disease virus and others), the attachment protein is the hemagglutinin/neuraminidase (HN) protein. In the last 5 years, atomic structures of paramyxovirus F and HN proteins have been reported. The knowledge gained from these structures towards understanding the mechanism of viral membrane fusion is described.

Original languageEnglish (US)
Pages (from-to)30-37
Number of pages8
JournalVirology
Volume344
Issue number1
DOIs
StatePublished - Jan 5 2006

Keywords

  • Attachment protein HN
  • Fusion activation
  • Membrane fusion
  • Paramyxovirus
  • Viral fusion proteins

ASJC Scopus subject areas

  • Virology

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