TRADD is required to prevent apoptosis, according to PLoS Biology paper.
Researchers from GSF–National Research Centre for Environment and Health say that they have identified the way that the Epstein-Barr virus manipulates tumor necrosis factor-receptor 1-associated death domain protein (TRADD) to establish itself in the host.
Epstein-Barr virus alters the way B lymphocytes behave, transforming them into cancerous cells that survive and divide more than they should, the team explains. They studied the way that TRADD interacts with LMP1, a protein produced by the virus that is essential for cell transformation. The scientists genetically altered cells so that they wouldn’t produce any TRADD and found that these cells didn’t respond to the transformation signals sent by the LMP1 protein.
The research group also studied the shape of the viral protein LMP1 and say that a region of it binds to TRADD in a unique way. When TRADD is bound to LMP1, it is unable to interact with the molecules that it normally would and hence it cannot cause cell death, they explain.
The investigators also took this TRADD binding site and used it to replace the TRADD binding site on the host cellular protein that mediates cell death. This was enough to convert the cellular protein into a nonapoptotic receptor and thus to stop TRADD from inducing apoptosis, they report.
The study is published on January 15 in PLoS Biology.