title: An acidic sphingomyelinase Type C activity from Mycobacterium tuberculosis.
abstract: Sphingomyelinases (SMases) catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Sphingolipids are recognized as diverse and dynamic regulators of a multitude of cellular processes mediating cell cycle control, differentiation, stress response, cell migration, adhesion, and apoptosis. Bacterial SMases are virulence factors for several species of pathogens. Whole cell extracts of Mycobacterium tuberculosis strains H37Rv and CDC1551 were assayed using [N-methyl-(14)C]-sphingomyelin as substrate. Acidic Zn(2+)-dependent SMase activity was identified in both strains. Peak SMase activity was observed at pH 5.5. Interestingly, overall SMase activity levels from CDC1551 extracts are approximately 1/3 of those of H37Rv. The presence of exogenous SMase produced by M. tuberculosis during infection may interfere with the normal host inflammatory response thus allowing the establishment of infection and disease development. This Type C activity is different from previously identified M. tuberculosis SMases. Defining the biochemical characteristics of M. tuberculosis SMases helps to elucidate the roles that these enzymes play during infection and disease.
authors.affiliation: Centro de Investigación Biomédica del Noreste, Instituto Mexicano del Seguro Social, Monterrey, N.L., México.
authors.forename: Jorge
authors.initials: J
authors.lastname: Castro-Garza
authors.affiliation: Centro de Investigación Biomédica del Noreste, Instituto Mexicano del Seguro Social, Monterrey, N.L., México; Departamento de Ciencias Básicas, División de Ciencias de la Salud, Universidad de Monterrey, San Pedro Garza García, N.L., México.
authors.forename: Francisco
authors.initials: F
authors.lastname: González-Salazar
authors.affiliation: Department of Infectious Diseases, University of Georgia, Athens, GA, USA.
authors.forename: Frederick D
authors.initials: FD
authors.lastname: Quinn
authors.affiliation: Department of Infectious Diseases, University of Georgia, Athens, GA, USA.
authors.forename: Russell K
authors.initials: RK
authors.lastname: Karls
authors.affiliation: Coordinación de Planeación y Enlace Institucional, Instituto Mexicano Del Seguro Social, Delegación Nuevo León, Monterrey, N.L., México.
authors.forename: Laura Hermila
authors.initials: LH
authors.lastname: De La Garza-Salinas
authors.affiliation: Unidad de Investigación Epidemiológica y en Servicios de Salud, Centro de Investigación Biomédica del Noreste, Instituto Mexicano del Seguro Social, Monterrey, N.L., México.
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Guzmán-de la Garza
authors.affiliation: Centro de Investigación Biomédica del Noreste, Instituto Mexicano del Seguro Social, Monterrey, N.L., México. Electronic address: jvargas147@yahoo.com.mx.
authors.forename: Javier
authors.initials: J
authors.lastname: Vargas-Villarreal
mesh_terms: D006863:Hydrogen-Ion Concentration; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D013108:Sphingomyelin Phosphodiesterase / Q000378:metabolism*
chemical_list: D013108:Sphingomyelin Phosphodiesterase
keywords: Esfingomielinasa; Factores de virulencia; Mexico; Mycobacterium tuberculosis; México; Sphingomyelinase; Tuberculosis; Virulence factors