Fab-independent antiadhesion effects of secretory immunoglobulin A on S-fimbriated Escherichia coli are mediated by sialyloligosaccharides

被引：62

作者：

Schroten, H

Stapper, C

Plogmann, R

Köhler, H

Hacker, J

Hanisch, FG

机构：

[1] Univ Dusseldorf, Zentrum Kinderheilkunde, D-40225 Dusseldorf, Germany

[2] Univ Wurzburg, Inst Mol Infekt Biol, Wurzburg, Germany

[3] Univ Cologne, Inst Biochem 2, Koln, Germany

来源：

INFECTION AND IMMUNITY | 1998年 / 66卷 / 08期

关键词：

D O I：

10.1128/IAI.66.8.3971-3973.1998

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

S-fimbriated Escherichia coli strains cause sepsis and meningitis in newborns and are known to recognize the carbohydrate sequence sialyl-(alpha 2-3)-galactoside. We show that adhesion of cloned S-fimbriated E. coli to human epithelial cells is inhibited Fab independently by sialyloligosaccharides on secretory immunoglobulin A (s-IgA), This indicates an anti-infective function of s-IgA (Fc), particularly in early human milk.

引用

收藏

页码：3971 / 3973

页数：3

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