@article{mbs:/content/journal/jmm/10.1099/jmm.0.47282-0, author = "Griener, Thomas P. and Mulvey, George L. and Marcato, Paola and Armstrong, Glen D.", title = "Differential binding of Shiga toxin 2 to human and murine neutrophils", journal= "Journal of Medical Microbiology", year = "2007", volume = "56", number = "11", pages = "1423-1430", doi = "https://doi.org/10.1099/jmm.0.47282-0", url = "https://www.microbiologyresearch.org/content/journal/jmm/10.1099/jmm.0.47282-0", publisher = "Microbiology Society", issn = "1473-5644", type = "Journal Article", keywords = "AF, Alexa Fluor", keywords = "Gb3, globotriaosylceramide", keywords = "HuSAP, human serum amyloid P component", keywords = "PE, phycoerythrin", keywords = "RFU, relative fluorescent unit", keywords = "EHEC, enterohaemorrhagic Escherichia coli", keywords = "HUS, haemolytic uraemic syndrome", keywords = "HI-FBS, heat-inactivated fetal bovine serum", abstract = "Shiga toxins (Stx1 and Stx2) are responsible for initiating haemolytic uraemic syndrome, a serious extraintestinal complication caused by enterohaemorrhagic Escherichia coli O157 : H7 infection in humans. Shiga toxins are classical AB5-type exotoxins, consisting of a globotriaosylceramide (Gb3)-binding B subunit pentamer and an enzymic A subunit. It is demonstrated in this study that Stx2 binds to human neutrophils by a non-classical mechanism that is independent of Gb3. In contrast, the investigation revealed that Stx2 binds to murine neutrophils by the classical Gb3-dependent mechanism. Moreover, whereas the human serum amyloid P (HuSAP) component inhibited Stx2 binding to murine neutrophils, HuSAP increased Stx2 binding to human neutrophils by 84.2 % (P≤0.002, Student's t-test). These observations may explain why HuSAP protects mice from the lethal effects of Stx2, whereas there is no indication that HuSAP plays a similar protective role in humans infected by E. coli O157 : H7.", }