02688nas a2200445 4500000000100000008004100001260006000042653002200102653003100124653002400155653002300179653002000202653002400222653001100246653001200257653001800269653002500287100002200312700002200334700002200356700002400378700002500402700002100427700002100448700002400469700002200493700001400515700001700529700002300546700002500569700002500594700002000619700002100639245014400660856007300804300001300877490000700890520133100897022001402228 2011 d c2011 JulbAmerican Society for MicrobiologyaWashington10aAntibodies, Viral10aAntigen-Antibody Reactions10aAntigens, Bacterial10aBacterial Proteins10aCross Reactions10aEnoyl-CoA Hydratase10aHumans10aleprosy10aMycobacterium10aMycobacterium leprae1 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-Garcia I00aEnoyl-coenzyme A hydratase and antigen 85B of Mycobacterium habana are specifically recognized by antibodies in sera from leprosy patients. uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3147323/pdf/zcd1097.pdf a1097-1030 v183 a
Leprosy is an infectious disease caused by Mycobacterium leprae, which is a noncultivable 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 nonpathogenic 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 by identifying M. habana proteins that reacted by immunoblotting with antibodies in serum samples from leprosy patients but not with antibodies in sera from tuberculosis (TB) patients or healthy donors (HDs). A 28-kDa antigen that specifically reacted with sera from leprosy patients was identified. To further characterize this antigen, protein spots were aligned in two-dimensional polyacrylamide gels and Western blots. Spots cut out from the gels were then 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 lepromatous leprosy, which is the most frequent form in Mexico.
a1556-679X