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J Med Microbiol 56 (2007), 1423-1430; DOI: 10.1099/jmm.0.47282-0
© 2007 Society for General Microbiology
ISSN 1473-5644

Differential binding of Shiga toxin 2 to human and murine neutrophils

Thomas P. Griener1, George L. Mulvey1, Paola Marcato2 and Glen D. Armstrong1

1 Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, Calgary, Alberta T2N 4N1, Canada

2 Department of Microbiology and Immunology, Sir Charles Tupper Medical Building, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada

Correspondence
Glen D. Armstrong
glen.armstrong{at}ucalgary.ca

Received 11 March 2007
Accepted 28 June 2007

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.

Abbreviations: AF, Alexa Fluor; EHEC, enterohaemorrhagic Escherichia coli; Gb3, globotriaosylceramide; HI-FBS, heat-inactivated fetal bovine serum; HUS, haemolytic uraemic syndrome; HuSAP, human serum amyloid P component; PE, phycoerythrin; RFU, relative fluorescent unit.




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