Journal
NATURE MICROBIOLOGY
Volume 2, Issue 6, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nmicrobiol.2017.27
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Funding
- BBSRC [BB/L007959/1]
- Wellcome Trust Research Career Development Fellowship [WT097411MA]
- Lister Institute of Preventive Medicine
- Canadian Institutes of Health Research [MOP-14687]
- Cystic Fibrosis Canada
- Canadian Foundation of Innovation
- Biotechnology and Biological Sciences Research Council [BB/L007959/1] Funding Source: researchfish
- Medical Research Council [MR/J006874/1] Funding Source: researchfish
- BBSRC [BB/L007959/1] Funding Source: UKRI
- MRC [MR/J006874/1] Funding Source: UKRI
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Pseudomonas aeruginosa is a Gram-negative bacterial pathogen associated with acute and chronic infections. The universal cyclic-di-GMP second messenger is instrumental in the switch from a motile lifestyle to resilient biofilm as in the cystic fibrosis lung. The SadC diguanylate cyclase is associated with this patho-adaptive transition. Here, we identify an unrecognized SadC partner, WarA, which we show is a methyltransferase in complex with a putative kinase, WarB. We established that WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Together, WarA and WarB have structural similarities with the bifunctional Escherichia coli lipopolysaccharide (LPS) O antigen regulator WbdD. Strikingly, WarA influences P. aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, and by using a zebrafish infection model, we implicate WarA in the ability of P. aeruginosa to evade detection by the host.
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