Duke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Nat Struct Mol Biol. 2010 Dec;17(12):1492-4. doi: 10.1038/nsmb.1944. Epub 2010 Nov 14.
The monoclonal antibody 13H11 shares part of its epitope in the HIV-1 gp41 membrane-proximal external region (MPER) with the rare, broadly neutralizing human antibody 2F5. Although 13H11 partially cross-blocked 2F5 binding, 13H11 is non-neutralizing and does not block 2F5 neutralization. We show that unlike 2F5, 13H11 binds to a well-defined helical MPER structure that is consistent with the structure of gp41 in a post-fusion six-helix bundle conformation.
单克隆抗体 13H11 与罕见的广谱中和人抗体 2F5 在 HIV-1 gp41 膜近端外部区域 (MPER) 中有部分共同表位。尽管 13H11 部分交叉阻断了 2F5 的结合，但 13H11 是非中和性的，不能阻断 2F5 的中和作用。我们表明，与 2F5 不同，13H11 结合到一个明确的螺旋 MPER 结构，这与融合后六螺旋束构象中的 gp41 结构一致。
