@article{17409,
  keywords = {Amino Acid Sequence, Antibodies, Bacterial, Antibody Specificity, Antigen-Antibody Reactions, Antigens, Bacterial, B-Lymphocytes, Binding Sites, Antibody, Enzyme-Linked Immunosorbent Assay, Epitopes, Ethiopia, Humans, Leprosy, Borderline, Leprosy, lepromatous, Leprosy, Tuberculoid, Longitudinal studies, Molecular Sequence Data, Mycobacterium leprae, Peptide Fragments, Peptide Mapping},
  author = {Filley E and Thole J E and Rook G A and Nagai S and Waters M and Drijfhout J W and Rinke de Wit T F and Vries R R and Abou-Zeid C},
  title = {Identification of an antigenic domain on Mycobacterium leprae protein antigen 85B, which is specifically recognized by antibodies from patients with leprosy.},
  abstract = {<p>Sixty-three overlapping 15-oligomer peptides covering the 30-kDa protein antigen 85B of Mycobacterium leprae were tested by ELISA to identify epitopes recognized by human antibodies. Serum samples from patients with lepromatous leprosy (LL) reacted mainly with peptides comprising amino acid regions (AA) 206-230, 251-280, and 291-325. Sera of patients with active tuberculosis who responded to the native 30-kDa antigen did not recognize these peptides. The antibody-binding specificity to the defined B cell regions was evaluated in a blind study with 71 serum samples from patients and household contacts living in Ethiopia where leprosy is endemic. The peptide of AA 256-280 was recognized by 88% of LL patients, 15% of patients with tuberculoid leprosy, and none of the contacts. These findings suggest that there are major linear B cell epitopes on the M. leprae 30-kDa protein that are recognized by lepromin-negative LL patients, whereas lepromin-positive patients respond preferentially to conformational epitopes.</p>},
  year = {1994},
  journal = {The Journal of infectious diseases},
  volume = {169},
  pages = {162-9},
  month = {1994 Jan},
  issn = {0022-1899},
  doi = {10.1093/infdis/169.1.162},
  language = {eng},
}