Unravelling the antigenic landscape of the HIV-1 subtype A envelope of an individual with broad cross-neutralizing antibodies using phage display peptide libraries
| Autor: | Ursula Dietrich, Wouter Janssens, Tessa Dieltjens, Guido Vanham, Sandra Coppens, Leo Heyndrickx, Lies L. Van Nieuwenhove, Michael Humbert, B. Willems |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Identification
Phage display Sequence analysis Cross-neutralization Viral diseases V3 loop HIV Antibodies Antibodies Epitope Bacteriophage Epitopes 03 medical and health sciences Antigen Peptide Library Virology Humans Neutralizing antibody Biology Antigens Viral 030304 developmental biology 0303 health sciences biology 030306 microbiology env Gene Products Human Immunodeficiency Virus biology.organism_classification Molecular biology Antibodies Neutralizing 3. Good health AIDS biology.protein HIV-1 Human medicine Peptides Epitope Mapping Conformational epitope |
| Zdroj: | Journal of Virological Methods; Vol 169 Journal of Virological Methods Journal of virological methods |
| ISSN: | 0166-0934 |
| DOI: | 10.1016/j.jviromet.2010.07.004 |
| Popis: | Broad cross-neutralizing antibodies from persons infected with HIV-1 target a variety of epitopes. Identification of these HIV-1 epitopes may result in an optimal panel of antigenic peptides to be included in a prophylactic vaccine. Phage display peptide libraries were used to unravel the antigenic landscape of an individual (ITM1) infected with HIV-1 subtype A with broad cross-neutralizing antibodies. A stringent selection strategy resulted in the identification of 60 unique HIV-1 peptide phage, which were subjected to sequence analysis and mapped onto the ITM1 envelope sequences. Four groups of peptide phages were found: the first group ( n = 11) were similar with the tip of the V3 loop (KxxHxGPxxxF); the second group ( n = 11) represented the gp41 principal immunodominant domain (CxGxLxCTxNxP); the third group ( n = 16) could be localized in the V2 loop (KxxxHxxxY); and the fourth group ( n = 22) mimicked a conformational epitope (Hxx S / T NxK). All but the V2-binding antibodies were conserved over the 11 years of follow-up. A neutralization inhibition assay revealed the contribution of the V3 antibodies to the neutralizing capacity of the ITM1 plasma. Overall, the ITM1 immunogenic landscape was mapped and a part of the origin of this broad cross-neutralizing activity was demonstrated. |
| Databáze: | OpenAIRE |
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