11 July 2012
Vol 4, Issue 142

About The Cover

Cover image expansion

ONLINE COVER Schematic Representation of the HIV-1 Envelope Glycoprotein (Env) Trimeric Spike. Shown is the molecular surface of the crystal structure of the core gp120 exterior Env (light blue) modeled inside the cryo-EM density (external blue sheen) defined by the Subramaniam group at the NIH. On the surface of the left most core monomer are the residue contacts for the human broadly neutralizing monoclonal antibody (mAb) VRC01 within the primary receptor CD4 binding site (yellow and orange) and for the non-broadly neutralizing CD4 binding site-directed mAbs (red and orange; orange are common footprint residues) elicited by soluble Env trimers in nonhuman primates. The VRC01 mAb is able to access its epitope by a side approach to the HIV-1 primary isolate spike and neutralize diverse viruses (yellow mAb, right, heading for its yellow/orange CD4 binding site footprint/epitope). However, the non-broad vaccine-induced mAbs (not shown) described by Sundling et al. cannot access their red/orange epitope by the same orientation due to clashes with trimer-axial elements of the spike and are unable to neutralize most circulating HIV-1 isolates. [CREDIT: CHRISTIAN POULSEN AND CHRISTINA CORBACI, SCRIPPS RESEARCH INSTITUTE, SAN DIEGO, CALIFORNIA]