@article{6077,
  keywords = {Amino Acid Motifs, Animals, Antibodies, Bacterial, Antibodies, Monoclonal, Antigens, Bacterial, Glycolipids, Humans, leprosy, Mice, Mice, Inbred BALB C, Molecular Mimicry, Mycobacterium leprae, Peptide Library},
  author = {Youn JH and Myung H and Liav A and Chatterjee D and Brennan PJ and Choi I and Cho S and Shin J},
  title = {Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae.},
  abstract = {<p>Phenolic glycolipid-I (PGL-I), a Mycobacterium leprae-specific antigen, has been widely used for the serodiagnosis of leprosy and has been implicated in the pathogenesis of leprosy. In an effort to produce an alternate antigen of PGL-I, the mimotope peptides of PGL-I, W(T/R)LGPY(V/M), were obtained using a monoclonal antibody, III603.8, specific to PGL-I by a phage library. The biotin-labeled predominant mimotope peptide of PGLP1, WTLGPYV, bound to III603.8 in a dose-dependent manner in an immunoassay. However, PGLP1 did not bind to anti-PGL-I antibodies in the serum samples from leprosy patients that were reactive to PGL-I. Although the mimotope peptide of WTLGPYV was not effective as an alternate antigen of PGL-I for the serodiagnosis of leprosy, but it would be of interest to know how the mimotope peptides mimic the role of PGL-I antigen in the pathogenesis of M. leprae infection.</p>},
  year = {2004},
  journal = {FEMS immunology and medical microbiology},
  volume = {41},
  pages = {51-7},
  month = {2004 May 01},
  issn = {0928-8244},
  doi = {10.1016/j.femsim.2004.01.001},
  language = {eng},
}