HIV-1 envelope glycoprotein
The HIV-1 envelope glycoprotein is composed of a receptor binding subunit, gp120 that is non-covalently linked to the membrane anchored fusion protein, gp41. Triggered by cellular receptor binding, the trimeric envelope complex mediates fusion of viral and cellular membranes through the rearrangement of the fusion protein subunit into a six helical bundle core structure. Our interest is to understand the structural transitions that gp41 undergoes from a native conformation to a fusion intermediate conformation and the final post fusion structure. Because gp41 contains highly conserved epitopes within its membrane proximal region (MPR), we aim to understand their conformation that is recognized by broadly neutralizing antibodies in order to exploit the structural knowledge for vaccine development.