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HIV-1 envelope trimer elicits more potent neutralizing antibody responses than monomeric gp120.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2012 Jul 24; Vol. 109 (30), pp. 12111-6. Date of Electronic Publication: 2012 Jul 05. - Publication Year :
- 2012
-
Abstract
- HIV-1 envelope glycoprotein is the primary target for HIV-1-specific antibodies. The native HIV-1 envelope spike on the virion surface is a trimer, but trimeric gp140 and monomeric gp120 currently are believed to induce comparable immune responses. Indeed, most studies on the immunogenicity of HIV-1 envelope oligomers have revealed only marginal improvement over monomers. We report here that suitably prepared envelope trimers have nearly all the antigenic properties expected for native viral spikes. These stable, rigorously homogenous trimers have antigenic properties markedly different from those of monomeric gp120s derived from the same sequences, and they induce potent neutralizing antibody responses for a cross-clade set of tier 1 and tier 2 viruses with titers substantially higher than those elicited by the corresponding gp120 monomers. These results, which demonstrate that there are relevant immunologic differences between monomers and high-quality envelope trimers, have important implications for HIV-1 vaccine development.
- Subjects :
- Animals
Chromatography, Gel
Enzyme-Linked Immunosorbent Assay
Guinea Pigs
Humans
Neutralization Tests
Surface Plasmon Resonance
Ultracentrifugation
Antibodies, Neutralizing immunology
HIV Antibodies immunology
HIV Envelope Protein gp120 immunology
HIV-1 immunology
Protein Multimerization immunology
env Gene Products, Human Immunodeficiency Virus immunology
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 109
- Issue :
- 30
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 22773820
- Full Text :
- https://doi.org/10.1073/pnas.1204533109