The virulence domain of Shigella IcsA contains a subregion with specific host cell adhesion function.
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Date
2020
Authors
Qin, J.
Doyle, M.T.
Tran, E.N.H.
Morona, R.
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Mantis, N.J.
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PLoS ONE, 2020; 15(1):e0227425-1-e0227425-19
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Jilong Qin, Matthew Thomas Doyle, Elizabeth Ngoc Hoa Tran, Renato Morona
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Abstract
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.
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© 2020 Qin et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.