TY - JOUR
KW - Alleles
KW - Amino Acid Sequence
KW - Antigens, Bacterial
KW - Chaperonin 10
KW - Clone Cells
KW - Epitopes, T-Lymphocyte
KW - HLA-DR Antigens
KW - HLA-DRB5 Chains
KW - Humans
KW - Molecular Sequence Data
KW - Mycobacterium leprae
KW - Sequence Homology, Amino Acid
KW - T-Lymphocytes
AU - Kim J
AU - Sette A
AU - Rodda S
AU - Southwood S
AU - Sieling P A
AU - Mehra V
AU - Ohmen J D
AU - Oliveros J
AU - Appella E
AU - Higashimoto Y
AU - Rea T H
AU - Bloom B R
AU - Modlin R L
AB - <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>
BT - Journal of immunology (Baltimore, Md. : 1950)
C1 - http://www.ncbi.nlm.nih.gov/pubmed/9200471?dopt=Abstract
DA - 1997 Jul 01
IS - 1
J2 - J. Immunol.
LA - eng
N2 - <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>
PY - 1997
SP - 335
EP - 43
T2 - Journal of immunology (Baltimore, Md. : 1950)
TI - Determinants of T cell reactivity to the Mycobacterium leprae GroES homologue.
VL - 159
SN - 0022-1767
ER -