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- W2006089188 abstract "The membrane proximal ectodomain region (MPER) of HIV-1 gp41 is the target of broadly neutralizing antibodies (BNAbs), 4E10, 2F5 and Z13e1. To unravel the molecular basis of BNAbs interference with virus entry, we have characterized BNAb-induced MPER conformational changes by a combination of electron paramagnetic resonance (EPR), nuclear magnetic resonance (NMR) and surface plasmon resonance (SPR) techniques. The analyses of MPER revealed a tilted N-terminal α helix connected via a short hinge to a flat C-terminal helical segment. This metastable L-shaped structure is immersed in viral membrane and, therefore, less accessible to immune attack. 4E10, a potent BNAb, was found to largely alter MPER membrane orientation, extracting buried W672 and F673 residues after initial encounter with the surface-embedded MPER. MPER conformational changes induced by other mAbs with various neutralizing potency were also determined. The data suggest that 2F5 and 4E10 HIV BNAbs may block viral fusion by perturbing the orientation of MPER relative to the lipid bilayer, extracting buried tryptophan residues in the process. These findings have important implications for the design of vaccines to elicit effective broadly neutralizing antibodies." @default.
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- W2006089188 date "2009-02-01" @default.
- W2006089188 modified "2023-09-28" @default.
- W2006089188 title "Conformational Changes of HIV-1 gp41 Membrane Proximal Ectodomain Region Induced by Broadly Neutralizing Antibodies" @default.
- W2006089188 doi "https://doi.org/10.1016/j.bpj.2008.12.3807" @default.
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