@article{2697,
  keywords = {Amino Acid Sequence, Animals, Antibody Specificity, Antigens, Bacterial, Bacterial Proteins, Cloning, Molecular, Epitopes, B-Lymphocyte, Epitopes, T-Lymphocyte, leprosy, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Mycobacterium leprae, Mycobacterium tuberculosis, Recombinant Fusion Proteins, Sequence Analysis, Protein, Sequence Homology, Amino Acid, Subcellular Fractions},
  author = {Spencer JS and Marques MA and Lima MC B S and Junqueira-Kipnis AP and Gregory B and Truman RW and Brennan PJ},
  title = {Antigenic specificity of the Mycobacterium leprae homologue of ESAT-6.},
  abstract = {<p>The sequence of the Mycobacterium leprae homologue of ESAT-6 shows only 36% amino acid correspondence to that from Mycobacterium tuberculosis. Anti-M. leprae ESAT-6 polyclonal and monoclonal antibodies and T-cell hybridomas reacted only with the homologous protein and allowed identification of the B- and T-cell epitopes. The protein is expressed in M. leprae and appears in the cell wall fraction. Thus, M. leprae ESAT-6 shows promise as a specific diagnostic agent for leprosy.</p>},
  year = {2002},
  journal = {Infection and immunity},
  volume = {70},
  pages = {1010-3},
  month = {2002 Feb},
  issn = {0019-9567},
  url = {https://www.ncbi.nlm.nih.gov/pmc/articles/PMC127711/pdf/1114.pdf},
  doi = {10.1128/iai.70.2.1010-1013.2002},
  language = {eng},
}