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

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.

The C-terminal domain of BinA is responsible for Bacillus sphaericus binary toxin BinA-BinB interaction.

The binary toxin (Bin) from Bacillus sphaericus consists of two polypeptides, BinA (42 kDa) and BinB (51 kDa) that work together to kill susceptible mosquito larvae. To investigate the functional regions of BinA involved in the interaction with BinB, four BinA truncated fragments, from both N- and C- termini, were constructed and expressed in Escherichia coli. Neither individual nor a mixture of fragments of BinA showed larvicidal activity against Culex quinquefasciatus larvae even using a high dose of toxins. Far-Western dot blot analysis showed strong binding of both C-terminal fragments (17 and 28 kDa) to BinB protein. This is the first report to demonstrate that the C-terminal part of BinA plays an important role for the interaction with BinB.