The virulence domain of Shigella IcsA contains a subregion with specific host cell adhesion function

Autoři: Jilong Qin aff001;  Matthew Thomas Doyle aff001;  Elizabeth Ngoc Hoa Tran aff001;  Renato Morona aff001
Působiště autorů: School of Biological Sciences, Department of Molecular & Biomedical Sciences, Research Centre for Infectious Diseases, University of Adelaide, Adelaide, Australia aff001
Vyšlo v časopise: PLoS ONE 15(1)
Kategorie: Research Article


Shigella species cause bacillary dysentery, especially among young individuals. Shigellae target the human colon for invasion; however, the initial adhesion mechanism is poorly understood. The Shigella surface protein IcsA, in addition to its role in actin-based motility, acts as a host cell adhesin through unknown mechanism(s). Here we confirmed the role of IcsA in cell adhesion and defined the region required for IcsA adhesin activity. Purified IcsA passenger domain was able block S. flexneri adherence and was also used as a molecular probe that recognised multiple components from host cells. The region within IcsA’s functional passenger domain (aa 138–148) was identified by mutagenesis. Upon the deletion of this region, the purified IcsAΔ138–148 was found to no longer block S. flexneri adherence and had reduced ability to interact with host molecules. Furthermore, S. flexneri expressing IcsAΔ138–148 was found to be significantly defective in both cell adherence and invasion. Taken together, our data identify an adherence region within the IcsA functional domain and provides useful information for designing therapeutics for Shigella infection.

Klíčová slova:

Adhesins – Centrifugation – HeLa cells – Host cells – Nitrocellulose – Shigella – Shigella flexneri – Shigellosis


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