Journal
STRUCTURE
Volume 19, Issue 5, Pages 691-699Publisher
CELL PRESS
DOI: 10.1016/j.str.2011.02.012
Keywords
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Funding
- NIH
- New York University Center for AIDS Research (CFAR) [AI027742]
- NIH [AI084119, AI082274, AI036085, HL059725, AI077451, GM088118]
- Bill & Melinda Gates Foundation
- Department of Veterans Affairs
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The quaternary neutralizing epitope (ONE) of HIV-1 gp120 is preferentially expressed on the trimeric envelope spikes of intact HIV virions, and ONE-specific monoclonal antibodies (mAbs) potently neutralize HIV-1. Here, we present the crystal structures of the Fabs of human mAb 2909 and macaque mAb 2.5B. Both. mAbs have long beta hairpin CDR H3 regions >20 angstrom in length that are each situated at the center of their respective antigen-binding sites. Computational analysis showed that the paratopes include the whole CDR H3, while additional CDR residues form shallow binding pockets. Structural modeling suggests a way to understand the configuration of QNEs and the antigen-antibody interaction for ONE mAbs. Our data will be useful in designing immunogens that may elicit potent neutralizing QNE Abs.
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