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Mol Microbiol. 2010 Aug;77(4):930-42. doi: 10.1111/j.1365-2958.2010.07259.x. Epub 2010 Jun 21.

H-NOX regulation of c-di-GMP metabolism and biofilm formation in Legionella pneumophila.

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Departments of ChemistryMolecular and Cell Biology, University of California, Berkeley, CA 94720, USA.


Haem Nitric oxide/OXygen (H-NOX) binding domains are a family of haemoprotein sensors that are widespread in bacterial genomes, but limited information is available on their function. Legionella pneumophila is the only prokaryote found, thus far, to encode two H-NOX proteins. This paper presents data supporting a role for one of the L. pneumophila H-NOXs in the regulation of biofilm formation.


(i) unmarked deletions in the hnox1 gene do not affect growth rate in liquid culture or replication in permissive macrophages; (ii) the Δhnox1 strain displays a hyper-biofilm phenotype; (iii) the gene adjacent to hnox1 is a GGDEF-EAL protein, lpg1057, and overexpression in L. pneumophila of this protein, or the well-studied diguanylate cyclase, vca0956, results in a hyper-biofilm phenotype; (iv) the Lpg1057 protein displays diguanylate cyclase activity in vitro and this activity is inhibited by the Hnox1 protein in the Fe(II)-NO ligation state, but not the Fe(II) unligated state; and (v) consistent with the Hnox1 regulation of Lpg1057, unmarked deletions of lpg1057 in the Δhnox1 background results in reversion of the hyper-biofilm phenotype back to wild-type biofilm levels. Taken together, these results suggest a role for hnox1 in regulating c-di-GMP production by lpg1057 and biofilm formation in response to NO.

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