Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Antibodies, Monoclonal / chemistry*
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Antibodies, Monoclonal / immunology
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Crystallography, X-Ray
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HIV Antibodies / chemistry*
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HIV Antibodies / immunology
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HIV Envelope Protein gp41 / chemistry*
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HIV Envelope Protein gp41 / immunology*
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HIV-1 / immunology
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Humans
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Immunoglobulin Fab Fragments / chemistry
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Models, Molecular
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Molecular Sequence Data
Substances
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Antibodies, Monoclonal
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HIV Antibodies
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HIV Envelope Protein gp41
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Immunoglobulin Fab Fragments
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gp41 protein, Human immunodeficiency virus 1