ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB₅ toxin.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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, 8 citations in OpenAlex.
- Sialoglycan-binding patterns of bacterial ABThe Journal of biological chemistry · 2022Article
- ABToxins · 2022Review
- Structure-function analyses of a pertussis-like toxin from pathogenicThe Journal of biological chemistry · 2017Article
- A novel mechanism of latency in matrix metalloproteinases.The Journal of biological chemistry · 2015Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
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Abstract
AB₅ toxins are key virulence factors found in a range of pathogenic bacteria. AB₅ toxins consist of two components: a pentameric B subunit that targets eukaryotic cells by binding to glycans located on the cell surface and a catalytic A subunit that disrupts host cellular function following internalization. To date, the A subunits of AB₅ toxins either have RNA-N-glycosidase, ADP-ribosyltransferase or serine protease activity. However, it has been suggested that a novel AB₅ toxin produced by clinical isolates of Escherichia coli and Citrobacter freundii has an A subunit with metalloproteinase activity. Here, the expression, purification and crystallization of this novel AB₅ toxin from E. coli (EcxAB) and the collection of X-ray data to 1.9 Å resolution are reported.
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