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PIV5 M protein interaction with host protein angiomotin-like 1

Zifei Pei1, Yuting Bai, Anthony P Schmitt

  • 1Department of Veterinary and Biomedical Sciences, The Pennsylvania State University, University Park, PA 16802, USA.

Virology
|November 26, 2009
PubMed

Insights

Paramyxovirus M proteins are key to virus assembly. Angiomotin-like 1 (AmotL1) interacts with M protein, influencing parainfluenza virus 5 (PIV5) budding and replication.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Paramyxovirus matrix (M) proteins are crucial for viral assembly and budding.
  • M proteins act as adapters, linking viral components and host cell membranes.
  • Host factors may be recruited by M proteins to facilitate virus release.

Purpose of the Study:

  • To identify host factors interacting with the parainfluenza virus 5 (PIV5) M protein.
  • To investigate the role of identified host factors in paramyxovirus assembly and budding.

Main Methods:

  • Yeast two-hybrid screening to identify interacting proteins.
  • Co-immunoprecipitation and mammalian cell transfection to confirm protein interactions.
  • siRNA-mediated gene silencing to assess the role of host factors in virus production.

Main Results:

  • Angiomotin-like 1 (AmotL1) was identified as a PIV5 M protein interacting partner.
  • The interaction between AmotL1 and PIV5 M protein was confirmed in various experimental systems.
  • Overexpression of AmotL1-binding regions inhibited PIV5 VLP production and budding.
  • AmotL1 depletion reduced PIV5 budding, indicating its beneficial role in infection.

Conclusions:

  • AmotL1 is a host factor that interacts with the PIV5 M protein.
  • This interaction plays a significant role in PIV5 assembly and budding.
  • AmotL1 appears to be beneficial for paramyxovirus infection.

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