Broad and potent neutralization of HIV-1 by a gp41-specific human antibody

Jinghe Huang, Gilad Ofek, Leo Laub, Mark K. Louder, Nicole A. Doria-Rose, Nancy S. Longo, Hiromi Imamichi, Robert T. Bailer, Bimal Chakrabarti, Shailendra K. Sharma, S. Munir Alam, Tao Wang, Yongping Yang, Baoshan Zhang, Stephen A. Migueles, Richard Wyatt, Barton F. Haynes, Peter D. Kwong, John R. Mascola and Mark Connors ()
Additional contact information
Jinghe Huang: HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Gilad Ofek: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Leo Laub: HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Mark K. Louder: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Nicole A. Doria-Rose: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Nancy S. Longo: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Hiromi Imamichi: HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Robert T. Bailer: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Bimal Chakrabarti: IAVI Neutralizing Antibody Center, The Scripps Research Institute
Shailendra K. Sharma: IAVI Neutralizing Antibody Center, The Scripps Research Institute
S. Munir Alam: Duke Human Vaccine Institute, Duke University
Tao Wang: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Yongping Yang: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Baoshan Zhang: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Stephen A. Migueles: HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Richard Wyatt: IAVI Neutralizing Antibody Center, The Scripps Research Institute
Barton F. Haynes: Duke Human Vaccine Institute, Duke University
Peter D. Kwong: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
John R. Mascola: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Mark Connors: HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health

Nature, 2012, vol. 491, issue 7424, 406-412

Abstract: Abstract Characterization of human monoclonal antibodies is providing considerable insight into mechanisms of broad HIV-1 neutralization. Here we report an HIV-1 gp41 membrane-proximal external region (MPER)-specific antibody, named 10E8, which neutralizes ∼98% of tested viruses. An analysis of sera from 78 healthy HIV-1-infected donors demonstrated that 27% contained MPER-specific antibodies and 8% contained 10E8-like specificities. In contrast to other neutralizing MPER antibodies, 10E8 did not bind phospholipids, was not autoreactive, and bound cell-surface envelope. The structure of 10E8 in complex with the complete MPER revealed a site of vulnerability comprising a narrow stretch of highly conserved gp41-hydrophobic residues and a critical arginine or lysine just before the transmembrane region. Analysis of resistant HIV-1 variants confirmed the importance of these residues for neutralization. The highly conserved MPER is a target of potent, non-self-reactive neutralizing antibodies, suggesting that HIV-1 vaccines should aim to induce antibodies to this region of HIV-1 envelope glycoprotein.

Date: 2012
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/nature11544 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:491:y:2012:i:7424:d:10.1038_nature11544

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature11544

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().