ArticleCurrent microbiology2015
Determinants of Proteolysis and Cell-Binding for the Shigella flexneri Cytotoxin, SigA.
Article in Current microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- The crystal structure of the toxin EspC from enteropathogenicGut microbes · 2025Article
- SepA EnhancesmBio · 2021Article
- Pathogenicity Factors of Genomic Islands in Intestinal and ExtraintestinalFrontiers in microbiology · 2020Review
- Investigating the Relatedness of Enteroinvasive Escherichia coli to Other E. coli and Shigella Isolates by Using Comparative Genomics.Infection and immunity · 2016Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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, α-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 α-domain consists of two functionally distinct domains, designated α1 and α2, which are sufficient to specify proteolytic and cell-binding activities, respectively.
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