An acidic sphingomyelinase Type C activity from Mycobacterium Tuberculosis

Jorge Castro-Garza, Francisco González-Salazar, Frederick D. Quinn, Russell K. Karls, Laura Hermila De La Garza-Salinas, Francisco J. Guzmán-De La Garza, Javier Vargas-Villarreal

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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- 14C]-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.

Original languageEnglish
Pages (from-to)21-26
Number of pages6
JournalRevista Argentina de Microbiologia
Issue number1
Publication statusPublished - 1 Jan 2016

Bibliographical note

Publisher Copyright:
© 2016 Asociación Argentina de Microbiología.

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Microbiology (medical)


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