@article{19057,
  keywords = {Alleles, Amino Acid Sequence, Antigens, Bacterial, Chaperonin 10, Clone Cells, Epitopes, T-Lymphocyte, HLA-DR Antigens, HLA-DRB5 Chains, Humans, Molecular Sequence Data, Mycobacterium leprae, Sequence Homology, Amino Acid, T-Lymphocytes},
  author = {Kim J and Sette A and Rodda S and Southwood S and Sieling P A and Mehra V and Ohmen J D and Oliveros J and Appella E and Higashimoto Y and Rea T H and Bloom B R and Modlin R L},
  title = {Determinants of T cell reactivity to the Mycobacterium leprae GroES homologue.},
  abstract = {<p>The 10-kDa protein Ag of Mycobacterium leprae, a human GroES hsp10 cognate, is a major T cell Ag in human leprosy infection. We investigated the mechanism for T cell responsiveness to this Ag according to the trimolecular interaction between T cell, peptide, and Ag-presenting element. This research was accomplished by mapping T cell epitopes in leprosy patients and correlating these responses with peptide-MHC binding affinities. We found that the majority of tuberculoid leprosy patients responded to peptides corresponding to residues 25-39 and 28-42. Truncation analysis of these peptides mapped the exact epitope to be within the overlapping region comprising residues 28-39. Responsiveness was correlated with the HLA-DRB5*0101 allele, which bound the peptides with moderate affinity. This allele is linked to HLA-DR2, which is associated with the resistant form of leprosy. Therefore, T cell responsiveness in tuberculoid leprosy may be mediated by the ability of HLA-DRB5*0101 to bind and present peptides of the immunodominant 10-kDa Ag.</p>},
  year = {1997},
  journal = {Journal of immunology (Baltimore, Md. : 1950)},
  volume = {159},
  pages = {335-43},
  month = {1997 Jul 01},
  issn = {0022-1767},
  language = {eng},
}