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The Serine Protease Autotransporters TagB, TagC, and Sha from Extraintestinal Pathogenic Escherichia coli Are Internalized by Human Bladder Epithelial Cells and Cause Actin Cytoskeletal Disruption

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Pokharel, Parvil, Diaz, Jérémy, Bessaiah, h, Houle, Sébastien, Guerrero-Barrera, a et Dozois, Charles M. ORCID: https://orcid.org/0000-0003-4832-3936 (2020). The Serine Protease Autotransporters TagB, TagC, and Sha from Extraintestinal Pathogenic Escherichia coli Are Internalized by Human Bladder Epithelial Cells and Cause Actin Cytoskeletal Disruption International Journal of Molecular Sciences , vol. 21 , nº 9:e3047. p. 1-23. DOI: 10.3390/ijms21093047.

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Résumé

TagB, TagC (tandem autotransporter genes B and C), and Sha (Serine-protease hemagglutinin autotransporter) are recently described members of the SPATE (serine protease autotransporters of Enterobacteriaceae) family. These SPATEs can cause cytopathic effects on bladder cells and contribute to urinary tract infection in a mouse model. Bladder epithelial cells form an important barrier in the urinary tract. Some SPATEs produced by pathogenic E. coli are known to breach the bladder epithelium. The capacity of these newly described SPATEs to alter bladder epithelial cells and the role of the serine protease active site were investigated. All three SPATE proteins were internalized by bladder epithelial cells and altered the distribution of actin cytoskeleton. Sha and TagC were also shown to degrade mucin and gelatin respectively. Inactivation of the serine catalytic site in each of these SPATEs did not affect secretion of the SPATEs from bacterial cells, but abrogated entry into epithelial cells, cytotoxicity, and proteolytic activity. Thus, our results show that the serine catalytic triad of these proteins is required for internalization in host cells, actin disruption, and degradation of host substrates such as mucin and gelatin.

Type de document: Article
Mots-clés libres: 5637 bladder cells; SPATEs; UTIs; actin; cytotoxicity; gelatin; mucin; serine proteases
Centre: Centre INRS-Institut Armand Frappier
Date de dépôt: 20 juill. 2021 21:39
Dernière modification: 15 févr. 2022 15:41
URI: https://espace.inrs.ca/id/eprint/11664

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