Abstract
BST-2 is a human extracellular transmembrane protein that inhibits the release of viruses such as HIV-1 and Ebola from the cell surface. Viruses can evade this inhibition through antagonistic viral protein interactions with BST-2. The BST-2 is a homo-dimer that forms a coiled-coil connected by three disulfide bonds. Recent cellular studies suggest that the extracellular domain of BST-2 is flexible or structurally dynamic. However, x-ray crystallography suggests the coiled-coil structure is rigid. The goal of this study is to understand the relation between the full-length BST-2 structure and function, and the mechanism of viral protein binding. Through limited proteolysis, protein fluorescence, and small-angle x-ray scattering analysis we show that there is a flexible region and a rigid region in the extracellular portion of BST-2. The flexibility of the full-length protein is still unknown. We have purified both the membrane-bound protein of BST-2 and the viral antagonist protein, Vpu for biochemical and structural characterization. We are optimizing conditions for crystallizing the full-length BST-2, Vpu and the BST-2/Vpu complex. This will help us understand how BST-2 functions and the antagonistic interactions with viral proteins.
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