Interaction between human BAP31 and respiratory syncytial virus small hydrophobic (SH) protein

Yan Li1, Neeraj Jain1, Suweeraya Limpanawat1

  • 1School of Biological Sciences, Nanyang Technological University, 637551, Singapore.

Virology
|April 10, 2015
PubMed

Insights

Human respiratory syncytial virus (hRSV) small hydrophobic (SH) protein interacts with B-cell associated protein 31 (BAP31). This novel interaction, identified using a membrane-based yeast two-hybrid system, may offer a new drug target.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • The human respiratory syncytial virus (hRSV) small hydrophobic (SH) protein is crucial for viral virulence.
  • Deletion of the SH protein results in viral attenuation and delayed apoptosis in infected cells.

Purpose of the Study:

  • To identify host proteins that interact with the hRSV SH protein.
  • To investigate the functional implications of the SH protein-host interaction.

Main Methods:

  • Utilized a membrane-based yeast two-hybrid system (MbY2H) with a human lung cDNA library.
  • Co-localization studies of transfected SH and BAP31 proteins.
  • Biochemical assays to confirm direct interaction between purified protein domains.

Main Results:

  • Identified B-cell associated protein 31 (BAP31) as an SH protein-binding partner.
  • Demonstrated co-localization of SH and BAP31 in transfected cells.
  • Confirmed direct physical interaction between the C-terminal endodomain of BAP31 and SH protein.

Conclusions:

  • The hRSV SH protein directly interacts with the host protein BAP31.
  • BAP31's known roles in protein trafficking and apoptosis suggest this interaction impacts viral pathogenesis.
  • The SH protein-BAP31 interaction represents a potential therapeutic target for hRSV infections.

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