A glutamate-alanine-leucine (EAL) domain protein of Salmonella controls bacterial survival in mice, antioxidant defence and killing of macrophages: role of cyclic diGMP
Article first published online: 8 APR 2005
Volume 56, Issue 5, pages 1234–1245, June 2005
How to Cite
Hisert, K. B., MacCoss, M., Shiloh, M. U., Darwin, K. H., Singh, S., Jones, R. A., Ehrt, S., Zhang, Z., Gaffney, B. L., Gandotra, S., Holden, D. W., Murray, D. and Nathan, C. (2005), A glutamate-alanine-leucine (EAL) domain protein of Salmonella controls bacterial survival in mice, antioxidant defence and killing of macrophages: role of cyclic diGMP. Molecular Microbiology, 56: 1234–1245. doi: 10.1111/j.1365-2958.2005.04632.x
- Issue published online: 8 APR 2005
- Article first published online: 8 APR 2005
- Accepted 22 February, 2005.
Signature-tagged transposon mutagenesis of Salmonella with differential recovery from wild-type and immunodeficient mice revealed that the gene here named cdgR[for c-diguanylate (c-diGMP) regulator] is required for the bacterium to resist host phagocyte oxidase in vivo. CdgR consists solely of a glutamate-alanine-leucine (EAL) domain, a predicted cyclic diGMP (c-diGMP) phosphodiesterase. Disruption of cdgR decreased bacterial resistance to hydrogen peroxide and accelerated bacterial killing of macrophages. An ultrasensitive assay revealed c-diGMP in wild-type Salmonella with increased levels in the CdgR-deficient mutant. Thus, besides its known role in regulating cellulose synthesis and biofilm formation, bacterial c-diGMP also regulates host–pathogen interactions involving antioxidant defence and cytotoxicity.