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T3SS chaperone of the CesT family is required for secretion of the anti-sigma factor BtrA in Bordetella pertussis
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SYSNO ASEP 0578519 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název T3SS chaperone of the CesT family is required for secretion of the anti-sigma factor BtrA in Bordetella pertussis Tvůrce(i) Držmíšek, Jakub (MBU-M) ORCID
Petráčková, Denisa (MBU-M) RID, ORCID
Dienstbier, Ana (MBU-M) ORCID
Čurnová, Ivana (MBU-M) ORCID
Večerek, Branislav (MBU-M) RID, ORCIDČíslo článku 2272638 Zdroj.dok. Emerging Microbes & Infections . - : Nature Publishing Group
Roč. 12, č. 2 (2023)Poč.str. 13 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova enteropathogenic escherichia-coli ; iii secretion ; virulence ; system ; bronchiseptica ; locus ; pathogenesis ; adaptation ; motility ; provides ; Bordetella pertussis ; t3ss ; CesT chaperone ; anti-sigma factor ; biofilm Obor OECD Microbiology CEP GA23-05634S GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 001095744600001 EID SCOPUS 85175561930 DOI 10.1080/22221751.2023.2272638 Anotace Bordetella pertussis is a Gram-negative, strictly human re-emerging respiratory pathogen and the causative agent of whooping cough. Similar to other Gram-negative pathogens, B. pertussis produces the type III secretion system, but its role in the pathogenesis of B. pertussis is enigmatic and yet to be elucidated. Here, we combined RNA-seq, LC-MS/MS, and co-immunoprecipitation techniques to identify and characterize the novel CesT family T3SS chaperone BP2265. We show that this chaperone specifically interacts with the secreted T3SS regulator BtrA and represents the first non-flagellar chaperone required for the secretion of an anti-sigma factor. In its absence, secretion but not production of BtrA and most T3SS substrates is severely impaired. It appears that the role of BtrA in regulating T3SS extends beyond its activity as an antagonist of the sigma factor BtrS. Predictions made by artificial intelligence system AlphaFold support the chaperone function of BP2265 towards BtrA and outline the structural basis for the interaction of BtrA with its target BtrS. We propose to rename BP2265 to BtcB for the Bordetella type III chaperone of BtrA.In addition, the absence of the BtcB chaperone results in increased expression of numerous flagellar genes and several virulence genes. While increased production of flagellar proteins and intimin BipA translated into increased biofilm formation by the mutant, enhanced production of virulence factors resulted in increased cytotoxicity towards human macrophages. We hypothesize that these phenotypic traits result indirectly from impaired secretion of BtrA and altered activity of the BtrA/BtrS regulatory node. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2024 Elektronická adresa https://www.tandfonline.com/doi/full/10.1080/22221751.2023.2272638
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