03273nas a2200505   4500000000100000008004100001260001300042653002400055653001200079653002300091653002700114653002700141653001100168653001500179653001600194653001200210653000900222653002400231653001500255653002800270653002500298653003100323653001300354653001200367653002500379653001800404653001700422100001500439700001000454700001500464700002400479700001600503700001200519700001400531700001500545700001000560700001100570700001500581245013500596856007100731300001200802490000700814520193200821022001402753       2004                            d  c2004 Jun10aAmino Acid Sequence10aAnimals10aBacterial Proteins10aEpitopes, B-Lymphocyte10aEpitopes, T-Lymphocyte10aHumans10aHybridomas10aImmune Sera10aleprosy10aMice10aMice, Inbred BALB C10aMice, Nude10aMolecular Sequence Data10aMycobacterium leprae10aMycobacterium tuberculosis10aPeptides10aRabbits10aRecombinant Proteins10aT-Lymphocytes10aTuberculosis1 aSpencer JS1 aKim H1 aMarques AM1 aGonzalez-Juarerro M1 aLima MC B S1 aVissa V1 aTruman RW1 aGennaro ML1 aCho S1 aCole S1 aBrennan PJ00aComparative analysis of B- and T-cell epitopes of Mycobacterium leprae and Mycobacterium tuberculosis culture filtrate protein 10.  uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC415692/pdf/1683-03.pdf  a3161-700 v723 a<p>Culture filtrate protein 10 (CFP-10) from Mycobacterium tuberculosis is a well-characterized immunodominant 10-kDa protein antigen known to elicit a very potent early gamma interferon response in T cells from M. tuberculosis-infected mice and humans. The sequence of the Mycobacterium leprae homologue of CFP-10 shows only 40% identity (60% homology) at the protein level with M. tuberculosis CFP-10 and thus has the potential for development as a T- or B-cell reactive antigen for specific diagnosis of leprosy. Antisera raised in mice or rabbits against recombinant M. leprae and M. tuberculosis CFP-10 proteins reacted only with homologous peptides from arrays of overlapping synthetic peptides, indicating that there was no detectable cross-reactivity at the antibody level. Sera from leprosy and tuberculosis patients were also specific for the homologous protein or peptides and showed distinct patterns of recognition for either M. leprae or M. tuberculosis CFP-10 peptides. At the cellular level, only 2 of 45 mouse T-cell hybridomas raised against either M. leprae or M. tuberculosis CFP-10 displayed a cross-reactive response against the N-terminal heterologous CFP-10 peptide, the region that exhibits the highest level of identity in the two proteins; however, the majority of peptide epitopes recognized by mouse T-cell hybridomas specific for each protein did not cross-react with heterologous peptides. Coupled with the human serology data, these results raise the possibility that peptides that could be used to differentiate infections caused by these two related microorganisms could be developed. Immunohistochemical staining of sections of M. leprae-infected nude mouse footpads resulted in strongly positive staining in macrophages and dendritic cells, as well as weaker staining in extracellular areas, suggesting that M. leprae CFP-10, like its homologue in M. tuberculosis, is a secreted protein.</p>  a0019-9567