IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Virkola, R.
Right arrow Articles by Korhonen, T. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Virkola, R.
Right arrow Articles by Korhonen, T. K.

Infection and Immunity, October 2000, p. 5696-5701, Vol. 68, No. 10
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

Ritva Virkola,1,* Mirko Brummer,1,dagger Heikki Rauvala,2,3 Loek van Alphen,4,Dagger and Timo K. Korhonen1

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- 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.

dagger Present address: VTT Biotechnology, FIN-02044 VTT, Espoo, Finland.

Dagger Present address: RIVM, LVM-Pb 92, 3720 BA Bilthoven, The Netherlands.

Infection and Immunity, October 2000, p. 5696-5701, Vol. 68, No. 10
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2000 by the American Society for Microbiology. All rights reserved.