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Journal of Virology, June 2006, p. 6093-6105, Vol. 80, No. 12
0022-538X/06/$08.00+0     doi:10.1128/JVI.00205-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Crystal Structures of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralizing Antibody 2219 in Complex with Three Different V3 Peptides Reveal a New Binding Mode for HIV-1 Cross-Reactivity

Robyn L. Stanfield,1* Miroslaw K. Gorny,3 Susan Zolla-Pazner,3 and Ian A. Wilson1,2*

Department of Molecular Biology,1 the Skaggs Institute for Chemical Biology, the Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037,2 New York VA Medical Center and New York University School of Medicine, New York, New York 100103

Received 27 January 2006/ Accepted 2 April 2006

Human monoclonal antibody 2219 is a neutralizing antibody isolated from a human immunodeficiency virus type 1-infected individual. 2219 was originally selected for binding to a V3 fusion protein and can neutralize primary isolates from subtypes B, A, and F. Thus, 2219 represents a cross-reactive, human anti-V3 antibody. Fab 2219 binds to one face of the variable V3 ß-hairpin, primarily contacting conserved residues on the N-terminal ß-strand of V3, leaving the V3 crown or tip largely accessible. Three V3/2219 complexes reveal the antibody-bound conformations for both the N- and C-terminal regions that flank the V3 crown and illustrate how twisting of the V3 loop alters the relative dispositions and pairing of the amino acids in the adjacent V3 ß-strands and how the antibody can accommodate V3 loops with different sequences.

* Corresponding author. Mailing address: Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037. Phone: (858) 784-9706. Fax: (858) 784-2980. E-mail for Robyn L. Stanfield: robyn{at}scripps.edu. E-mail for Ian A. Wilson: wilson{at}scripps.edu.

Journal of Virology, June 2006, p. 6093-6105, Vol. 80, No. 12
0022-538X/06/$08.00+0     doi:10.1128/JVI.00205-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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