ArticlePloS one2012
The type III secreted protein BspR regulates the virulence genes in Bordetella bronchiseptica.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- Architecture and regulatory functions of c-di-GMP signaling in classical Bordetella species.FEMS microbiology reviews · 2026Review
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- Limited response of primary nasal epithelial cells toMicrobiology spectrum · 2025Article
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- Pertussis resurgence: epidemiological trends, pathogenic mechanisms, and preventive strategies.Frontiers in immunology · 2025Review
- T3SS chaperone of the CesT family is required for secretion of the anti-sigma factor BtrA inEmerging microbes & infections · 2023Article
- Bcr4 Is a Chaperone for the Inner Rod Protein in theMicrobiology spectrum · 2022Article
- Omics Analysis of Blood-Responsive Regulon inInternational journal of molecular sciences · 2021Article
- Comparative Phosphoproteomics of Classical Bordetellae Elucidates the Potential Role of Serine, Threonine and Tyrosine Phosphorylation inFrontiers in cellular and infection microbiology · 2021Article
- Transcriptional Downregulation of a Type III Secretion System under Reducing Conditions in Bordetella pertussis.Journal of bacteriology · 2020Article
- Expression of small RNAs of Bordetella pertussis colonizing murine tracheas.Microbiology and immunology · 2020Article
- Review
- Enhancement of immune response against Bordetella spp. by disrupting immunomodulation.Scientific reports · 2019Article
- Comparative Integrated Omics Analysis of the Hfq Regulon inInternational journal of molecular sciences · 2019Article
- BspR/BtrA, an Anti-σ Factor, Regulates the Ability ofmSphere · 2019Article
- Bordetella Pertussis virulence factors in the continuing evolution of whooping cough vaccines for improved performance.Medical microbiology and immunology · 2018Review
- Differential regulation of type III secretion and virulence genes in Bordetella pertussis and Bordetella bronchiseptica by a secreted anti-σ factor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Glutamate Limitation, BvgAS Activation, and (p)ppGpp Regulate the Expression of the Bordetella pertussis Type 3 Secretion System.Journal of bacteriology · 2016Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bordetella bronchiseptica is closely related with B. pertussis and B. parapertussis, the causative agents of whooping cough. These pathogenic species share a number of virulence genes, including the gene locus for the type III secretion system (T3SS) that delivers effector proteins. To identify unknown type III effectors in Bordetella, secreted proteins in the bacterial culture supernatants of wild-type B. bronchiseptica and an isogenic T3SS-deficient mutant were compared with iTRAQ-based, quantitative proteomic analysis method. BB1639, annotated as a hypothetical protein, was identified as a novel type III secreted protein and was designated BspR (Bordetella secreted protein regulator). The virulence of a BspR mutant (ΔbspR) in B. bronchiseptica was significantly attenuated in a mouse infection model. BspR was also highly conserved in B. pertussis and B. parapertussis, suggesting that BspR is an essential virulence factor in these three Bordetella species. Interestingly, the BspR-deficient strain showed hyper-secretion of T3SS-related proteins. Furthermore, T3SS-dependent host cell cytotoxicity and hemolytic activity were also enhanced in the absence of BspR. By contrast, the expression of filamentous hemagglutinin, pertactin, and adenylate cyclase toxin was completely abolished in the BspR-deficient strain. Finally, we demonstrated that BspR is involved in the iron-responsive regulation of T3SS. Thus, Bordetella virulence factors are coordinately but inversely controlled by BspR, which functions as a regulator in response to iron starvation.
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