Abstract
Background Recently, a genome-wide association study identified 3 amino acids (residues 67, 70, 97) in the HLA-B peptide binding groove that explain the classical HLA class I associations with HIV-1 immune control. However, how amino acid substitutions at these positions affect HIV-1 immune defense remains unclear. Leukocyte Immunoglobulin Like Receptors (LILR) are a class of immunoregulatory molecules that are expressed on myeloid dendritic cells and interact with HLA class I molecules as their physiologic ligands. Here, we assessed how different amino acids in the HLA-B binding groove may influence their binding to LILRs. Methods
Highlights
A genome-wide association study identified 3 amino acids in the HLA-B peptide binding groove that explain the classical HLA class I associations with HIV-1 immune control
Leukocyte Immunoglobulin Like Receptors (LILR) are a class of immunoregulatory molecules that are expressed on myeloid dendritic cells and interact with HLA class I molecules as their physiologic ligands
No significant correlations were observed when HLA-LILRB1 binding scores were used instead of leukocyte immunoglobulin like receptors B2 (LILRB2). These data suggest that amino acid polymorphisms at position 67, 70 and 97 of the HLA-B binding groove influence HIV-1 immune control through altered interactions with the immunomodulatory LILRB2 receptor
Summary
A genome-wide association study identified 3 amino acids (residues 67, 70, 97) in the HLA-B peptide binding groove that explain the classical HLA class I associations with HIV-1 immune control. Interactions between HLA-B and leukocyte immunoglobulin like receptors B2 (LILRB2) correlate with HIV-1 disease outcomes E Martin Gayo1*, D Jones2, F Pereyra1, M Lichterfeld3, RL Allen2, XG Yu1 From AIDS Vaccine 2012 Boston, MA, USA.
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