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Infection and Immunity, October 2000, p. 5696-5701, Vol. 68, No. 10
Division of General
Microbiology1 and Division of
Biochemistry,2 Department of
Biosciences, and Institute of Biotechnology,3
University of Helsinki, Helsinki, Finland, and Department of
Medical Microbiology, University of Amsterdam, Amsterdam, The
Netherlands4
Received 21 March 2000/Returned for modification 11 May
2000/Accepted 28 June 2000
The interaction of the fimbriae of Haemophilus
influenzae type b (Hib) with two heparin-binding extracellular
matrix proteins, human fibronectin (Fn) and heparin-binding
growth-associated molecule (HB-GAM) from mouse, were studied. The
fimbriated Hib strain 770235 fim+, as well as the recombinant strain
E. coli HB101(pMH140), which expressed Hib fimbriae,
adhered strongly to Fn and HB-GAM immobilized on glass. Purified Hib
fimbriae bound to Fn and HB-GAM, and within the Fn molecule, the
binding was localized to the N-terminal 30,000-molecular-weight (30K)
and 40K fragments, which contain heparin-binding domains I and II,
respectively. Fimbrial binding to Fn, HB-GAM, and the 30K and the 40K
fragments was inhibited by high concentrations of heparin. The results
show that fimbriae of Hib interact with heparin-binding extracellular
matrix proteins. The nonfimbriated Hib strain 770235 fim
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Interaction of Fimbriae of Haemophilus
influenzae Type B with Heparin-Binding Extracellular Matrix
Proteins

and
exhibited a
low level of adherence to Fn but did not react with HB-GAM, indicating
that Hib strains also possess a fimbria-independent mechanism to
interact with Fn.
*
Corresponding author. Mailing address: Division of
General Microbiology, Department of Biosciences, P.O. Box 56 (Viikinkaari 9), FIN-00014 University of Helsinki, Finland. Phone:
358-9-19159235. Fax: 358-9-19159262. E-mail:
ritva.virkola{at}helsinki.fi.
Present address: VTT Biotechnology, FIN-02044 VTT, Espoo, Finland.
Present address: RIVM, LVM-Pb 92, 3720 BA Bilthoven, The Netherlands.
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