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Updated: Jun 26, 2026
11:28
Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus
Published on: October 7, 2011
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.
Summary
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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