02139nas a2200289 4500000000100000008004100001260001600042100002200058700002200080700002200102700002400124700002500148700002100173700002100194700002400215700002200239700001400261700001700275700002300292700002500315700002500340700002000365700002200385245013100407520129700538022001401835 2011 d c2011 May 251 aSerafín-López J1 aTalavera-Paulin M1 aAmador-Molina J C1 aAlvarado-Riverón M1 aVilchis-Landeros M M1 aMéndez-Ortega P1 aFafutis-Morris M1 aParedes-Cervantes V1 aLópez-Santiago R1 aLeón C I1 aGuerrero M I1 aRibas-Aparicio R M1 aMendoza-Hernández G1 aCarreño-Martínez C1 aEstrada-Parra S1 aEstrada-García I00aEnoyl-CoA Hydratase and Ag85B of Mycobacterium habana are specifically recognized by antibodies in sera from leprosy patients.3 aLeprosy is an infectious disease caused by Mycobacterium leprae which is a non-cultivable bacterium. One of the principal goals of leprosy research is to develop serological tests that will allow identification and early treatment of leprosy patients. M. habana is a cultivable non-pathogenic mycobacterium and candidate vaccine for leprosy, and several antigens that cross-react between M. leprae and M. habana have been discovered. The aim of the present study was to extend the identification of cross-reactive antigens in by identifying M. habana proteins that reacted by immunoblotting with antibodies in sera samples from leprosy patients but not with antibodies in sera from tuberculosis patients (TB) or healthy donors (HD). A 28 kDa antigen that specifically reacted with sera from leprosy patients was identified. To further characterize this antigen, protein spots in two dimensional (2DE) Western blots were aligned with Coomassie blue-stained gels and analyzed by mass spectrometry. Two proteins were identified: enoyl- coenzyme A hydratase (lipid metabolism) (ML2498) and antigen 85B (Ag85B, mycolyltransferase) (ML2028). These proteins represent promising candidates for the design of a reliable tool for the serodiagnosis of LL cases which is the most frequent form in Mexico. a1556-679X