01826nas a2200373   4500000000100000008004100001260001600042653002200058653001200080653002600092653002700118653002400145653001600169653001100185653001200196653000900208653002400217653002200241653002500263653002000288100001200308700001200320700001100332700001700343700001500360700001100375700001000386700001100396245010700407300000900514490000700523520090800530022001401438       2004                            d  c2004 May 0110aAmino Acid Motifs10aAnimals10aAntibodies, Bacterial10aAntibodies, Monoclonal10aAntigens, Bacterial10aGlycolipids10aHumans10aleprosy10aMice10aMice, Inbred BALB C10aMolecular Mimicry10aMycobacterium leprae10aPeptide Library1 aYoun JH1 aMyung H1 aLiav A1 aChatterjee D1 aBrennan PJ1 aChoi I1 aCho S1 aShin J00aProduction and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae.  a51-70 v413 a<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>  a0928-8244