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- Publisher
- Annual Reviews
- Copyright
- Copyright © 2006 by Annual Reviews. All rights reserved
- ISSN
- 0732-0582
- eISSN
- 1545-3278
- DOI
- 10.1146/annurev.immunol.24.021605.090557
- pmid
- 16551265
- Publisher site
- See Article on Publisher Site
Abstract
Abstract The glycoprotein (gp) 120 subunit is an important part of the envelope spikes that decorate the surface of HIV-1 and a major target for neutralizing antibodies. However, immunization with recombinant gp120 does not elicit neutralizing antibodies against multiple HIV-1 isolates (broadly neutralizing antibodies), and gp120 failed to demonstrate vaccine efficacy in recent clinical trials. Ongoing crystallographic studies of gp120 molecules from HIV-1 and SIV increasingly reveal how conserved regions, which are the targets of broadly neutralizing antibodies, are concealed from immune recognition. Based on this structural insight and that from studies of antibody structures, a number of strategies are being pursued to design immunogens that can elicit broadly neutralizing antibodies to gp120. These include ( a ) the construction of mimics of the viral envelope spike and ( b ) the design of antigens specifically tailored to induce broadly neutralizing antibodies.
Journal
Annual Review of Immunology – Annual Reviews
Published: Apr 23, 2006