Skip to main content Accessibility help
×
Home

Mechanisms of cell entry by influenza virus

  • Karen J. Cross (a1), Laura M. Burleigh (a1) and David A. Steinhauer (a1)

Abstract

A wide range of viruses, including many human and animal pathogens representing various taxonomic groups, contain genomes that are enclosed in lipid envelopes. These envelopes are generally acquired in the final stages of assembly, as viruses bud from regions of the membrane of the infected cell at which virally encoded membrane proteins have accumulated. The viruses procure their membranes during this process and mature particles ‘pinch off’ from the cellular membranes. Under most circumstances, initiation of another round of infection is dependent on two critical functions supplied by the envelope proteins. The virus must bind to cell-surface receptors of a new host cell, and fusion of the viral and cellular membranes must occur to transfer the viral genome into the cell. Enveloped viruses have evolved a variety of mechanisms to execute these two basic functions. Owing to their relative simplicity, studies of binding and fusion using enveloped viruses and their components have contributed significantly to the overall understanding of receptor–ligand interactions and membrane fusion processes – fundamental activities involved in a plethora of biological functions.

Copyright

Corresponding author

National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, UK. Tel: +44 (0)20 8959 3666 (ext. 2256); Fax: +44 (0)20 8906 4477; E-mail: dsteinh@nimr.mrc.ac.uk

Keywords

Related content

Powered by UNSILO

Mechanisms of cell entry by influenza virus

  • Karen J. Cross (a1), Laura M. Burleigh (a1) and David A. Steinhauer (a1)

Metrics

Altmetric attention score

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed.