PMID: 9548074Apr 21, 1998Paper

Promiscuous T-cell recognition of a rubella capsid protein epitope restricted by DRB1*0403 and DRB1*0901 molecules sharing an HLA DR supertype

Human Immunology
D OuG T Nepom

Abstract

Two T cell clones derived from different donors with HLA-DRB1*0403 or DRB1*0901 phenotype recognize a rubella capsid peptide, C(265-273) in the context of several different HLA-DR molecules in addition to DRB1*0403 and DRB1*0901. All DR molecules restricting the T-cell clones have in common residues, R or Q at position beta 70, R at position beta 71, and E at position beta 74 in pocket '4' of the DR peptide binding groove, suggesting that a DR subregion structure or supertype, "Q/RRE" underlies the promiscuous T-cell recognition of this peptide. Single amino acid substituted analogs of peptide C(263-275) at anchor position 4 for natural residue R were tested for their ability to induce clonal T-cell cytotoxic responses. The results indicated that a positively charged residue, R or K, was required for T-cell recognition, suggesting a possible mechanism of electrostatic interactions between the negatively charged residue E at position beta 74 of these DR molecules and the positively charged residue at anchor position 4 of the peptide in T-cell recognition.

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Citations

Oct 3, 1998·Human Immunology·D OuA J Tingle
Mar 11, 2004·The Journal of Obstetrics and Gynaecology Research·Mitsuo OkuboHiroo Maeda
Jan 13, 2015·Lancet·Nathaniel LambertGregory A Poland
Nov 30, 2004·The Lancet Infectious Diseases·Maher K Gandhi, Rajiv Khanna
Nov 1, 2007·Clinical Pharmacology and Therapeutics·I G OvsyannikovaG A Poland
Feb 3, 2006·Expert Review of Vaccines·Inna G OvsyannikovaGregory A Poland
Sep 3, 2010·The Journal of Immunology : Official Journal of the American Association of Immunologists·John SidneyAlessandro Sette
Feb 9, 2010·The Journal of Immunology : Official Journal of the American Association of Immunologists·John SidneyAlessandro Sette

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