@article{18570,
  keywords = {Antibodies, Monoclonal, Antigens, Bacterial, Bacterial Proteins, CD4-Positive T-Lymphocytes, Chaperonin 60, Chaperonins, Heat-Shock Proteins, Histocompatibility Testing, HLA-DR Antigens, Humans, leprosy, Leprosy, lepromatous, Leprosy, Tuberculoid, Lymphocyte Activation, Mycobacterium leprae, Peptide Fragments, Recombinant Proteins, Trypsin},
  author = {Mitra D K and Mehra N K and Maiti T K and Banerjee A and Taneja V and Rajalingam R and Ahuja R K and Bhattacharya B C},
  title = {CD4+ T-cell responses to recombinant hsp65 and hsp18 of M. leprae and their trypsin-digested fragments in leprosy: diversity in HLA-DR restriction.},
  abstract = {<p>Mycobacterium leprae heat-shock proteins hsp65 and hsp18 have received immense attention as major T-cell target antigens in leprosy. Both of these hsps and their tryptic fragments were characterized for their ability to stimulate CD4+ T cells derived from polar leprosy cases and healthy contacts. The optimal digestion of hsps with trypsin yielded four fragments of hsp65--TDB65-1 (24 kDa), TDB65-2 (18 kDa), TDB65-3 (17 kDa), TDB65-4 (14 kDa)-- and three of hsp18--TDB18-1 (10 kDa), TDB18-2 (5 kDa), TDB18-3 (3 kDa). While all of these tryptic fragments and undigested hsps triggered CD4+ T cells from tuberculoid (TT) leprosy patients and healthy contacts (SI &gt; 2), only two fragments--TDB65-2 and TDB18-3--were found to be stimulatory in anergic lepromatous (LL) leprosy patients (SI = 5.27 and 3.0, respectively). Blocking studies using allele-specific anti-DR monoclonal antibodies revealed multiple HLA-Dr restriction, with DR2 providing the strongest restriction in both TT as well as LL leprosy. These findings indicate that M. leprae hsps and their trypsin-digested fragments are promiscuous and recognizable in the context of diverse HLA alleles, of which DR2 is the most efficient restriction element. The 18-kDa fragment of hsp65 and the 3-kDa fragment of hsp18 are the most versatile fragments that could elicit in vitro proliferation in both polar forms of leprosy.</p>
},
  year = {1995},
  journal = {International journal of leprosy and other mycobacterial diseases : official organ of the International Leprosy Association},
  volume = {63},
  pages = {518-28},
  month = {1995 Dec},
  issn = {0148-916X},
  url = {http://ila.ilsl.br/pdfs/v63n4a02.pdf},
  language = {eng},
}