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Published on: April 2, 2015
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.
Abstract:
The small hydrophobic (SH) protein is a short channel-forming polypeptide encoded by the human respiratory syncytial virus (hRSV). Deletion of SH protein leads to the viral attenuation in mice and primates, and delayed apoptosis in infected cells. We have used a membrane-based yeast two-hybrid system (MbY2H) and a library from human lung cDNA to detect proteins that bind SH protein. This led to the identification of a membrane protein, B-cell associated protein 31 (BAP31). Transfected SH protein co-localizes with transfected BAP31 in cells, and pulls down endogenous BAP31. Titration of purified C-terminal endodomain of BAP31 against isotopically labeled SH protein in detergent micelles suggests direct interaction between the two proteins. Given the key role of BAP31 in protein trafficking and its critical involvement in pro- and anti-apoptotic pathways, this novel interaction may constitute a potential drug target.
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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