Finely tuned WspRs help bacteria beat body by building biofilm

The authors determined the crystal structure of WspR and followed up with biochemical analysis of the enzyme. This work showed that WspR exists in an active form that produces c-di-GMP and is then bound by c-di-GMP and forced into an inactive form. The study therefore reveals a finely balanced equilibrium between the synthesis and degradation of this key player in biofilm formation.

New approaches to controlling the behavior of bacteria responsible for chronic infections can be envisaged. Because the signalling molecules involved in biofilm formation, such as c-di-GMP, are uniquely found in bacteria, the authors hope that there is potential for new therapeutic treatments based on this work; if you interrupted this bacterial signalling it would have no negative effect on the human host but could be devastating for the bacteria.

Citation: De N, Pirruccello M, Krasteva PV, Bae N, Raghavan RV, et al. (2008) Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS Biol 6(3): e67.doi:10.1371/journal.pbio.0060067

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