Structure–function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design
- 1 July 2010
- journal article
- research article
- Published by Springer Nature in Nature Reviews Immunology
- Vol. 10 (7) , 527-535
- https://doi.org/10.1038/nri2801
Abstract
This Opinion article describes the newly discovered conserved immunological and structural features of the sequence-variable regions of HIV-1 gp120, which the authors suggest warrant the reappraisal of these regions as vaccine targets. One of the main challenges of developing an HIV-1 vaccine lies in eliciting immune responses that can overcome the antigenic variability exhibited by HIV. Most HIV-1 vaccine development has focused on inducing immunity to conserved regions of the HIV-1 envelope. However, new studies of the sequence-variable regions of the HIV-1 gp120 envelope glycoprotein have shown that there are conserved immunological and structural features in these regions. Recombinant immunogens that include these features may provide the means to address the antigenic diversity of HIV-1 and induce protective antibodies that can prevent infection with HIV-1.Keywords
This publication has 133 references indexed in Scilit:
- Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1Virology, 2010
- The use of immune complex vaccines to enhance antibody responses against neutralizing epitopes on HIV-1 envelope gp120Vaccine, 2009
- Structural Basis of the Cross-Reactivity of Genetically Related Human Anti-HIV-1 mAbs: Implications for Design of V3-Based ImmunogensStructure, 2009
- Cross-clade neutralizing antibodies against HIV-1 induced in rabbits by focusing the immune response on a neutralizing epitopeVirology, 2009
- Neutralizing antibody responses to subtype B and C adjuvanted HIV envelope protein vaccination in rabbitsVirology, 2009
- High titer HIV-1 V3-specific antibodies with broad reactivity but low neutralizing potency in acute infection and following vaccinationVirology, 2009
- Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificityVirology, 2008
- Structure of Antibody F425-B4e8 in Complex with a V3 Peptide Reveals a New Binding Mode for HIV-1 NeutralizationJournal of Molecular Biology, 2007
- Structure of a High-affinity “Mimotope” Peptide Bound to HIV-1-neutralizing Antibody b12 Explains its Inability to Elicit gp120 Cross-reactive AntibodiesJournal of Molecular Biology, 2007
- Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesisVirology, 2007