Journal
MICROBIOLOGICAL RESEARCH
Volume 278, Issue -, Pages -Publisher
ELSEVIER GMBH
DOI: 10.1016/j.micres.2023.127535
Keywords
C-di-GMP; Superoxide dismutase; Anti-oxidation; Oxidative stress
Categories
Ask authors/readers for more resources
In this study, a novel c-di-GMP binding protein SodA that regulates oxidative stress tolerance in S. maltophilia was identified. The enzyme activity of SodA was shown to be directly modulated by c-di-GMP through various in vivo and in vitro experiments.
C-di-GMP is a bacterial second messenger implicated in the regulation of many key functions including antibiotic tolerance and biofilm formation. Our understanding of how c-di-GMP exerts its action via receptors to modulate different biological functions is still limited. Here we used a c-di-GMP affinity pull-down assay coupled to LC-MS/ MS to identify c-di-GMP-binding proteins in the opportunistic pathogen Stenotrophomonas maltophilia. This analysis identified Smlt3238 (SodA), a protein of the superoxide dismutase family, as a c-di-GMP-binding protein. Microscale thermophoresis showed that purified SodA protein bound c-di-GMP with an estimated dissociation constant (Kd) value of 141.5 mu M. Using various in vivo and in vitro experiments, we demonstrated that cdi-GMP modulates the enzyme activity of SodA directly. Circular dichroism experiments revealed that SodA protein gradually altered its basic structure with increasing levels of c-di-GMP. Phenotypic experiments conducted in the presence of a range of intracellular c-di-GMP levels showed that SodA function is modulated by cdi-GMP. The findings thus identify a novel c-di-GMP binding protein that governs oxidative stress tolerance in S. maltophilia.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available