Cytotoxic T lymphocytes recognize structurally diverse, clade-specific and cross-reactive peptides in human immunodeficiency virus type-1 gag through HLA-B53.
Dorrell, L;
Willcox, BE;
Jones, EY;
Gillespie, G;
Njai, H;
Sabally, S;
Jaye, A;
DeGleria, K;
Rostron, T;
Lepin, E;
+3 more...McMichael, A;
Whittle, H;
Rowland-Jones, S;
(2001)
Cytotoxic T lymphocytes recognize structurally diverse, clade-specific and cross-reactive peptides in human immunodeficiency virus type-1 gag through HLA-B53.
European journal of immunology, 31 (6).
pp. 1747-1756.
ISSN 0014-2980
DOI: https://doi.org/10.1002/1521-4141(200106)31:6<1747::aid-immu1747>3.0.co;2-l
Permanent Identifier
Use this Digital Object Identifier when citing or linking to this resource.
Human immunodeficiency virus type-1 (HIV-1) cytotoxic T lymphocyte (CTL) epitopes have largely been defined in Caucasian populations infected with clade B virus. Identification of potentially protective CTL epitopes in non-B clade-infected African subjects is important for vaccine development. In a study of CTL responses in clade A-infected Gambians, using cytotoxicity, interferon-gamma (IFN-gamma) enzyme-linked immunospot (ELISpot) and HLA-B53-peptide tetramer assays, we identified three HLA-B53-restricted epitopes in HIV-1 gag p24. CTL specific for an epitope in a highly immunogenic region of the p24 protein showed no cross-reactivity to other HIV-1 clades. Two of the epitopes would not have been predicted from the peptide-binding motif due to the absence of a proline anchor at position 2. Structural analysis of HLA-B53 and its relative, HLA B35, enabled us to re-define the peptide-binding motif to include other P2 anchors. These results demonstrate the value of combined immunological and structural analyses in defining novel CTL epitopes and have implications for HIV-1 vaccine design.
