Differential binding of Shiga toxin 2 to human and murine neutrophils

被引：32

作者：

Griener, Thomas P.

Mulvey, George L.

Marcato, Paola

Armstrong, Glen D. ^{[1
]}

机构：

[1] Univ Calgary, Hlth Sci Ctr, Dept Microbiol & Infect Dis, Calgary, AB T2N 4N1, Canada

[2] Dalhousie Univ, Dept Microbiol & Immunol, Sir Charles Tupper Med Bldg, Halifax, NS B3H 1X5, Canada

来源：

JOURNAL OF MEDICAL MICROBIOLOGY | 2007年 / 56卷 / 11期

关键词：

D O I：

10.1099/jmm.0.47282-0

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 AB(5)-type, exotoxins, consisting of a globotriaosylceramide (Gb(3))-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 Gb(3)-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.

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页码：1423 / 1430

页数：8

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