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Virulence Regulation with Venus Flytrap Domains: Structure and Function of the Periplasmic Moiety of the Sensor-Kinase BvgS


Bacteria make use of two-component transduction systems, composed of a sensor-kinase and a response regulator, to perceive environmental signals and orchestrate an appropriate response. The virulence regulon of the whooping cough agent Bordetella pertussis is controlled by the two-component system BvgAS. The sensor-kinase BvgS harbor extra-cytoplasmic Venus flytrap perception domains similar to those found in neuronal receptors, and it is the prototype of a large bacterial protein family. We report the atomic structure of the extra-cytoplasmic moiety of BvgS, which shows a novel dimeric arrangement. We show that the virulent phase of B. pertussis that occurs by default corresponds to a specific conformation of BvgS generated by the periplasmic architecture itself and by the differential dynamics of its Venus flytrap domains. The perception of negative signals by the periplasmic domains causes BvgS to shift to a different conformation that corresponds to the avirulent phase of the bacteria. In addition to contributing to our understanding of virulence regulation by B. pertussis at a time of whooping cough re-emergence, this study also paves the way to the mechanistic exploration of the homologous sensor-kinases found in various bacterial pathogens.


Vyšlo v časopise: Virulence Regulation with Venus Flytrap Domains: Structure and Function of the Periplasmic Moiety of the Sensor-Kinase BvgS. PLoS Pathog 11(3): e32767. doi:10.1371/journal.ppat.1004700
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004700

Souhrn

Bacteria make use of two-component transduction systems, composed of a sensor-kinase and a response regulator, to perceive environmental signals and orchestrate an appropriate response. The virulence regulon of the whooping cough agent Bordetella pertussis is controlled by the two-component system BvgAS. The sensor-kinase BvgS harbor extra-cytoplasmic Venus flytrap perception domains similar to those found in neuronal receptors, and it is the prototype of a large bacterial protein family. We report the atomic structure of the extra-cytoplasmic moiety of BvgS, which shows a novel dimeric arrangement. We show that the virulent phase of B. pertussis that occurs by default corresponds to a specific conformation of BvgS generated by the periplasmic architecture itself and by the differential dynamics of its Venus flytrap domains. The perception of negative signals by the periplasmic domains causes BvgS to shift to a different conformation that corresponds to the avirulent phase of the bacteria. In addition to contributing to our understanding of virulence regulation by B. pertussis at a time of whooping cough re-emergence, this study also paves the way to the mechanistic exploration of the homologous sensor-kinases found in various bacterial pathogens.


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