Journal
SCIENCE IMMUNOLOGY
Volume 2, Issue 7, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciimmunol.aal2200
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Funding
- NIH, National Institute of Allergy and Infectious Diseases, Division of AIDS grant for the Duke Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVI-ID) [UM1 AI 100645]
- Collaboration for AIDS Vaccine Discovery grant from the Bill and Melinda Gates Foundation [OPP1115416]
- Interdisciplinary Research Training Program in AIDS [T32 AI007392]
- Duke Center for AIDS Research [P30 AI 64518]
- Defense Threat Reduction Agency [HDTRA1-12-C-0105]
- Intramural Research Program of the Vaccine Research Center, National Institute of Allergy and Infectious Diseases
- Cancer Prevention Research Institute of Texas [RP100890]
- Office of Basic Energy Sciences, Office of Science, U.S. Department of Energy [W-31-109-Eng-38]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [P30AI064518, ZIAAI005010, T32AI007392, UM1AI100645] Funding Source: NIH RePORTER
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Induction of broadly neutralizing antibodies (bnAbs) is a goal of HIV-1 vaccine development. Antibody 10E8, reactive with the distal portion of the membrane-proximal external region (MPER) of HIV-1 gp41, is broadly neutralizing. However, the ontogeny of distal MPER antibodies and the relationship of memory B cell to plasma bnAbs are poorly understood. HIV-1-specific memory B cell flow sorting and proteomic identification of anti-MPER plasma antibodies from an HIV-1-infected individual were used to isolate broadly neutralizing distal MPER bnAbs of the same B cell clonal lineage. Structural analysis demonstrated that antibodies from memory B cells and plasma recognized the envelope gp41 bnAb epitope in a distinct orientation compared with other distal MPER bnAbs. The unmutated common ancestor of this distal MPER bnAb was autoreactive, suggesting lineage immune tolerance control. Construction of chimeric antibodies of memory B cell and plasma antibodies yielded a bnAb that potently neutralized most HIV-1 strains.
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