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The stx gene, found in Shiga toxin-producing Escherichia coli (STEC) and enterohemorrhagic E. coli (EHEC), encodes Shiga toxin, a potent bacterial AB5 protein toxin. Shiga toxin consists of a single enzymatic A subunit and a pentameric B subunit-binding moiety. The toxin is primarily responsible for the severe clinical manifestations of STEC infection, including hemorrhagic colitis and hemolytic-uremic syndrome, by disrupting host cell protein synthesis[1][3]. The gene is often located on a bacteriophage and can move between bacteria, contributing to the emergence of new pathogenic strains[5]. While the stx gene itself is not a therapeutic target (it encodes the toxin, not the receptor or enzyme targeted by therapy), its product, Shiga toxin, is the actual virulence factor implicated in disease. The stx gene is a critical biomarker for STEC diagnosis, and its presence is closely monitored in public health surveillance[1][3].
The stx gene encodes Shiga toxin, an AB5 protein toxin that inhibits protein synthesis in host cells by N-glycosidase activity targeting the 28S rRNA of the 60S ribosome[1][3]. The pentameric B subunit binds to the host cell receptor globotriaosylceramide (Gb3), facilitating uptake; the A subunit is cleaved and its active A1 fragment traffics to the cytosol to irreversibly inactivate the ribosome[1][3].
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