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A novel capsule-mediated virulence mechanism in a bacterial pathogen

ABSTRACT: Bordetella pertussis, the causative agent of whooping cough, produces a microcapsule at its surface but its role in pertussis pathogenesis remained to be investigated.Absence of KpsT, a membrane-associated protein involved in the polysaccharide transport resulted in the down-modulation of a large number of virulence genes which correlated with strong attenuation in vivo.

ORGANISM(S): Bordetella pertussis

PROVIDER: GSE62088 | GEO | 2014/10/07

SECONDARY ACCESSION(S): PRJNA263207

REPOSITORIES: GEO

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Bordetella parapertussis shotgun proteomic analysis reveals physiological response to iron starvation and potential new virulence determinants absent in Bordetella pertussis

Project description:To our knowledge, we provide the first proteomics study of Bordetella parapertussis, one of the causative agents of whooping cough. We compared the identified proteins different to Bordetella pertussis, the other pathogen causing whooping cough. In addition, we extended the study to investigate the proteome response to iron limitation, a stress condition the pathogens face while infection.

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Project description:Bordetella pertussis is the causative agent of human whooping cough, a highly contagious respiratory disease which despite vaccination programs remains the major cause of infant morbidity and mortality. The requirement of the RNA chaperone Hfq for virulence of B. pertussis suggested that Hfq-dependent small regulatory RNAs are involved in the modulation of gene expression. High-throughput RNA sequencing revealed hundreds of putative noncoding RNAs including the RgtA sRNA. Abundance of RgtA is strongly decreased in the absence of the Hfq protein and its expression is modulated by the activities of the two-component regulatory system BvgAS and another response regulator RisA. Whereas RgtA levels were elevated under modulatory conditions or in the absence of bvg genes, deletion of the risA gene completely abolished RgtA expression. Profiling of the ΔrgtA mutant in the ΔbvgA genetic background identified the BP3831 gene encoding a periplasmic amino acid-binding protein of an ABC transporter as a possible target gene. The results of site-directed mutagenesis and in silico analysis indicate that RgtA base-pairs with the region upstream of the start codon of the BP3831 mRNA and thereby weakens the BP3831 protein production. Furthermore, our data suggest that the function of the BP3831 protein is related to transport of glutamate, an important metabolite in the B. pertussis physiology. We propose that the BvgAS/RisA interplay regulates the expression of RgtA which upon infection, when glutamate might be scarce, attenuates translation of the glutamate transporter and thereby assists in adaptation of the pathogen to other sources of energy.

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