Open AccessProduction and characterization of peptide mimotopes of phenolic glycolipid‐I of Mycobacterium leprae
Author(s) -
Youn Ju Ho,
Myung HanJeong,
Liav Abraham,
Chatterjee Delphi,
Brennan Patrick J.,
Choi InHong,
Cho SangNae,
Shin JeonSoo
Publication year - 2004
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1016/j.femsim.2004.01.001
Subject(s) - mimotope , mycobacterium leprae , antigen , biology , monoclonal antibody , epitope , immunoassay , microbiology and biotechnology , antibody , leprosy , virology , immunology
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.