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Background  The  Francisella tularensis  protein MglA performs complex regulatory functions since it influences the expression of more than 100 genes and proteins in  F. tularensis . Besides regulating the  igl  operon, it has been suggested that it also regulates several factors such as SspA, Hfq, CspC, and UspA, all important to stress adaptation. Therefore, it can be hypothesized that MglA plays an important role for  Francisella  stress responses in general and for the oxidative stress response specifically.    Results  We investigated the oxidative stress response of the Δ mglA  mutant of the live vaccine strain (LVS) of  F. tularensis  and found that it showed markedly diminished growth and contained more oxidized proteins than the parental LVS strain when grown in an aerobic milieu but not when grown microaerobically. Moreover, the Δ mglA  mutant exhibited an increased catalase activity and reduced expression of the  fsl  operon and  feoB  in the aerobic milieu. The mutant was also found to be less susceptible to H 2 O 2 . The aberrant catalase activity and gene expression was partially normalized when the Δ mglA  mutant was grown in a microaerobic milieu.    Conclusions  Altogether the results show that the Δ mglA  mutant exhibits all the hallmarks of a bacterium subjected to oxidative stress under aerobic conditions, indicating that MglA is required for normal adaptation of  F. tularensis  to oxidative stress and oxygen-rich environments.

The role of MglA for adaptation to oxidative stress of Francisella tularensis LVS