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Infection and Immunity, May 1999, p. 2671-2676, Vol. 67, No. 5
Division of General Microbiology, Department
of Biosciences, FIN-00014 University of Helsinki,
Finland,1 and Institut für
Molekulare Infektionsbiologie, Universität Würzburg,
D-97070 Würzburg, Germany2
Received 5 October 1998/Returned for modification 25 November
1998/Accepted 10 February 1999
The adhesion of the S fimbriae of meningitis-associated
Escherichia coli O18ac:K1:H7 to the cellular and the plasma
forms of human fibronectin was studied. E. coli
HB101(pAZZ50) expressing the complete S-fimbria II gene cluster of
E. coli O18 adhered to cellular fibronectin (cFn) on glass
but not to plasma fibronectin (pFn). Adhesion to cFn was specifically
inhibited by neuraminidase treatment of cFn as well as by incubation of
the bacteria with sialyl-
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Cellular Form of Human Fibronectin as an
Adhesion Target for the S Fimbriae of Meningitis-Associated
Escherichia coli
2-3-lactose, a receptor analog of the S
fimbriae. No significant adhesion to cFn or pFn was detected with
E. coli HB101(pAZZ50-67) expressing S fimbriae lacking the
SfaS lectin subunit. Strain HB101(pAZZ50) also adhered to a human
fibroblast cell culture known to be rich in cFn, and the adhesion was
specifically inhibited in the presence of polyclonal antibodies to cFn.
The results show that the SfaS lectin of the S fimbriae mediates the
adherence of meningitis-associated E. coli to sialyl
oligosaccharide chains of cFn.
*
Corresponding author. Mailing address: Division of
General Microbiology, Department of Biosciences, P.O. Box 56, Viikinkaari 9, FIN-00014 University of Helsinki, Finland. Phone:
358-9-70859235. Fax: 358-9-70859262. E-mail:
ritva.virkola{at}helsinki.fi.
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