Determinants of proteolysis and cell-binding for the shigella flexneri cytotoxin, SigA

Eng G Chua, Keith Al-Hasani, Martin J Scanlon, Ben Adler, Harry Harry Sakellaris

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)

Abstract

Shigella flexneri secretes an enterotoxic, SPATE family autotransporter (AT), SigA, which has cytopathic activity towards cultured epithelial cells. Its cytopathic activity is due to its ability to degrade the cytoskeletal protein, alpha-fodrin. The mechanisms by which AT toxins target cells and tissues differ and the details of how SigA acts are not known. In the current study, the determinants of proteolysis and cell-targeting for SigA were determined. We demonstrate that the SigA passenger or alpha-domain consists of two functionally distinct domains, designated alpha1 and alpha2, which are sufficient to specify proteolytic and cell-binding activities, respectively.
Original languageEnglish
Pages (from-to)613 - 617
Number of pages5
JournalCurrent Microbiology
Volume71
Issue number5
DOIs
Publication statusPublished - 2015

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