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Comment
. 2008 Jan;28(1):10-2.
doi: 10.1016/j.immuni.2007.12.005.

HIV-1 hides an Achilles' heel in virion lipids

Barton F Haynes  1 , S Munir Alam
Affiliations
Comment

HIV-1 hides an Achilles' heel in virion lipids

Barton F Haynes et al. Immunity. 2008 Jan.

Abstract

In this issue, Sun et al. (2008) model the interface between a neutralizing antibody and HIV-1 glycoprotein 41 (gp41) envelope peptide in lipids. This model could help overcome a roadblock in HIV-1 vaccine development.

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Figures

Figure 1
Figure 1. The Three-Step Process of Neutralizing Antibody 4E10 Binding to HIV-1 Envelope Membrane-Proximal Region
According to the model of Sun et al. (2008), the HIV-1 Envelope (HIV-1 Env) gp41 membrane-proximal region in lipids consists of C- and N-terminal helices connected via a short hinge “kink” (represented by the line between each helix) with the N-terminal helix projected away from the membrane and the kink and C-terminal helix bound in lipid. The binding of 4E10 to HIV-1 Env gp41 may occur in three steps. In the first step, interaction of hydrophobic residues of 4E10 CDRH3 (third complementarity-determining region of heavy chain) with membrane lipids concentrates 4E10 in close proximity to HIV-1 Env gp41 membrane-proximal region. In the second step, 4E10 encounters membrane-bound gp41 antigen, which might involve initial contacts with exposed gp41 residues N671 and W680. Next, 4E10 hydrophobic residues (CDRH2 and CDRH3) facilitate conformational rearrangements of the gp41 membrane-proximal region, which involve peptide side-chain rearrangements, and exposure of key residues (W672, F673). Finally, in the third step, stable docking of 4E10 follows insertion of the exposed residues of gp41 into 4E10-binding pocket.
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