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For many years, AIDS vaccine development has been hindered by the remarkable diversity, glycosylation, and conformational flexibility of HIV. Most glycoprotein (gp) 120-reactive antibodies are ineffective at neutralizing primary HIV isolates. However, in animal models, the broadly neutralizing antibody b12 is protective. To explore the structure of the gp120-b12 complex, researchers examined crystallizations of b12 complexed with various forms of gp120. This analysis revealed that b12 interacts with gp120 in a well-preserved region that is also the initial point of contact for CD4 binding, which is required for viral-host membrane fusion.
Because conformational flexibility of the HIV envelope protein gp120 can complicate antibody recognition…