| Autor: |
Chen X; Laboratory of Immunoregulation, NIAID, NIH, Bethesda, Maryland, USA., Scala G, Quinto I, Liu W, Chun TW, Justement JS, Cohen OJ, vanCott TC, Iwanicki M, Lewis MG, Greenhouse J, Barry T, Venzon D, Fauci AS |
| Jazyk: |
angličtina |
| Zdroj: |
Nature medicine [Nat Med] 2001 Nov; Vol. 7 (11), pp. 1225-31. |
| DOI: |
10.1038/nm1101-1225 |
| Abstrakt: |
The antigenic polymorphism of HIV-1 is a major obstacle in developing an effective vaccine. Accordingly, we screened random peptide libraries (RPLs) displayed on phage with antibodies from HIV-infected individuals and identified an array of HIV-specific epitopes that behave as antigenic mimics of conformational epitopes of gp120 and gp41 proteins. We report that the selected epitopes are shared by a collection of HIV-1 isolates of clades A-F. The phage-borne epitopes are immunogenic in rhesus macaques, where they elicit envelope-specific antibody responses. Upon intravenous challenge with 60 MID50 of pathogenic SHIV-89.6PD, all monkeys became infected; however, in contrast to the naive and mock-immunized monkeys, four of five mimotope-immunized monkeys experienced lower levels of peak viremia, followed by viral set points of undetectable or transient levels of viremia and a mild decline of CD4+ T cells, and were protected from progression to AIDS-like illness. These results provide a new approach to the design of broadly protective HIV-1 vaccines. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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