Journal
CURRENT OPINION IN HIV AND AIDS
Volume 10, Issue 3, Pages 135-143Publisher
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/COH.0000000000000153
Keywords
glycans; gp120-gp41 interface; HIV-1 envelope; neutralizing antibody epitopes
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Funding
- Centre for the AIDS Programme of Research (CAPRISA)
- South African Medical Research Council (MRC)
- National Institutes of Health (NIH) [R01 AI104387-01A1, AI116086-01]
- Center for HIV/AIDS Vaccine Immunology (CHAVI) [AI067854]
- Center for AIDS Vaccine Discovery (CAVD) of the Bill and Melinda Gates Foundation
- South African HIV/AIDS Research and Innovation Platform of the South African Department of Science and Technology
- HIVRAD NIH [AI088610]
- NIAID, NIH, US Department of Health and Human Services [U19 AI51794]
- Wellcome Trust [089933/Z/09/Z]
- Poliomyelitis Research Foundation (PRF) of South Africa
- Fogarty AITRP Fellowship
- Wellcome Trust [089933/Z/09/Z] Funding Source: Wellcome Trust
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Purpose of review To provide an update on neutralizing antibody targets in the context of the recent HIV-1 envelope trimer structure, describe new antibody isolation technologies, and discuss the implications of these data for HIV-1 prevention and therapy. Recent findings Recent advances in B-cell technologies have dramatically expanded the number of antibodies isolated from HIV-infected donors with broadly neutralizing plasma activity. These, together with the first high-resolution crystal and cryo-electron microscopy (cryo-EM) structures of a cleaved, prefusion HIV-1 trimer, have defined new regions susceptible to neutralization. This year, three epitopes in the gp120-gp41 interface were structurally characterized, highlighting the importance of prefusion gp41 as a target. Similar to many other broadly neutralizing antibody epitopes, these new antibodies define a target that is also highly glycan dependent. Collectively, the epitopes for broadly neutralizing antibodies now reveal a continuum of vulnerability spanning the length of the HIV-1 envelope trimer. Summary Progress in the last year has provided support for the use of rationally stabilized whole HIV-1 trimers as immunogens for eliciting antibodies to multiple epitopes. Furthermore, the increasing number of broad and potent antibodies with the potential for synergistic/complementary combinations opens up new avenues for preventing and treating HIV-1 infection.
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