Lipid modification of the Cu,Zn superoxide dismutase from Mycobacterium tuberculosis.

摘要: The leader sequence of Mycobacterium tuberculosis Cu,Zn superoxide dismutase (Cu,ZnSOD) contains a prokaryotic membrane lipoprotein attachment site. In the present study, we have found that protein, which exhibits detectable SOD activity, is lipid-modified and associated with bacterial when expressed either in M. or Escherichia coli. These results provide first demonstration lipid modification Cu,ZnSOD. An analysis sodC genes available databases indicates same signal for also gene products from other mycobacteria Gram-positive bacteria and, uniquely, two distinct Gram-negative bacterium Salmonella typhimurium. Evidence provided an up-regulation response to phagocytosis by human macrophages, suggesting Cu,ZnSOD involved mechanisms facilitate mycobacterial intracellular growth.