Journal
VIROLOGY
Volume 482, Issue -, Pages 105-110Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2015.03.034
Keywords
Small hydrophobic; Respiratory syncytial virus; BAP31; Protein-protein interaction; Paramyxovirus; Membrane protein; Apoptosis; NMR; Yeast-two hybrid
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Funding
- Singapore National Research Foundation [NRF-CRP4-2008-02, RG 51/13]
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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. (C) 2015 Elsevier Inc. All rights reserved.
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