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Integrin alphavbeta1 promotes infection by human metapneumovirus

Gabriella Cseke1, Melissa S Maginnis, Reagan G Cox

  • 1Department of Chemistry, Vanderbilt University College of Arts and Sciences, Nashville, TN 37232, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 24, 2009
PubMed

Insights

Human metapneumovirus (hMPV) uses its fusion (F) protein to enter cells by binding to alphavbeta1 integrin. This discovery provides a target for developing new antiviral therapies against hMPV infections.

Area of Science:

  • Virology
  • Cell Biology
  • Immunology

Background:

  • Human metapneumovirus (hMPV) is a significant cause of lower respiratory tract infections globally.
  • The hMPV fusion (F) protein is a key viral surface protein and a primary target for protective immunity.
  • The presence of an Arg-Gly-Asp (RGD) motif in the hMPV F protein suggests interaction with integrins for cell entry.

Purpose of the Study:

  • To identify the specific cellular receptor used by hMPV for cell entry.
  • To investigate the role of integrins in hMPV infection.
  • To determine if alphavbeta1 integrin serves as a functional receptor for hMPV.

Main Methods:

  • Utilized the divalent cation chelator EDTA to assess hMPV infectivity.
  • Employed function-blocking antibodies against alphavbeta1 integrin.
  • Conducted gene transfection and siRNA knockdown experiments to manipulate alphav and beta1 integrin expression.
  • Tested binding of wild-type and mutant recombinant hMPV F proteins to cells.

Main Results:

  • EDTA inhibited hMPV infectivity, unlike in respiratory syncytial virus (RSV) infections.
  • Antibodies targeting alphavbeta1 integrin blocked hMPV entry.
  • Upregulation of alphav or beta1 integrins in nonpermissive cells enhanced hMPV infectivity.
  • Silencing alphav and beta1 integrins reduced hMPV infection.
  • Recombinant hMPV F protein demonstrated cell binding, while an RGE-mutant F protein did not.

Conclusions:

  • Alphavbeta1 integrin functions as a cellular receptor for hMPV.
  • The RGD motif on the hMPV F protein is critical for binding to alphavbeta1 integrin.
  • Understanding this interaction opens avenues for novel hMPV therapeutic strategies.

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