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The human metapneumovirus fusion protein mediates entry via an interaction with RGD-binding integrins

Reagan G Cox1, S Brent Livesay, Monika Johnson

  • 1Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee, USA.

Journal of Virology
|August 31, 2012
PubMed

Insights

Human metapneumovirus (HMPV) uses its fusion (F) protein to attach to and enter cells, independent of the G protein. This process relies on the F protein

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Paramyxoviruses typically require attachment (G) and fusion (F) proteins for cell entry.
  • Human metapneumovirus (HMPV) is unique, with its F protein suggested to mediate both attachment and fusion.
  • A conserved arginine-glycine-aspartate (RGD) motif in HMPV F and its interaction with integrins were previously noted.

Purpose of the Study:

  • To investigate the role of the HMPV F protein in viral attachment and entry.
  • To determine if HMPV F can mediate infection independently of the G protein.
  • To elucidate the specific cellular receptors involved in HMPV F-mediated entry.

Main Methods:

  • Analysis of HMPV F protein binding and entry mechanisms.
  • Mutation of the invariant F-RGD motif to F-RAE to assess infectivity.
  • Investigation of the dependence of viral RNA transcription on F-integrin interactions.

Main Results:

  • HMPV F mediates viral binding and entry through multiple RGD-binding integrins, independent of the G protein.
  • The F-RGD motif is essential for HMPV infection; mutation to F-RAE severely impairs infectivity.
  • Integrin binding to the F protein is a prerequisite for productive viral RNA transcription.

Conclusions:

  • The HMPV F protein acts as a primary mediator of attachment and fusion, utilizing RGD-binding integrins as cellular receptors.
  • HMPV entry is a stepwise process initiated by F protein interaction with integrins, independent of the G protein.
  • These findings reveal a novel mechanism for paramyxovirus entry, highlighting the central role of the F protein and integrins.

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