Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins

R. Virkola (Corresponding Author), Mirko Brummer, H. Rauvala, L. van Alphen, T.K. Korhonen

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

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.
Original languageEnglish
Pages (from-to)5696 - 5701
Number of pages6
JournalInfection and Immunity
Volume68
Issue number10
Publication statusPublished - 2000
MoE publication typeA1 Journal article-refereed

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Haemophilus influenzae type b
Extracellular Matrix Proteins
Haemophilus influenzae
Fibronectins
Heparin
Carrier Proteins
Glass
Molecular Weight
pleiotrophin
Escherichia coli

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Virkola, R., Brummer, M., Rauvala, H., van Alphen, L., & Korhonen, T. K. (2000). Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins. Infection and Immunity, 68(10), 5696 - 5701.
Virkola, R. ; Brummer, Mirko ; Rauvala, H. ; van Alphen, L. ; Korhonen, T.K. / Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins. In: Infection and Immunity. 2000 ; Vol. 68, No. 10. pp. 5696 - 5701.
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abstract = "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.",
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Virkola, R, Brummer, M, Rauvala, H, van Alphen, L & Korhonen, TK 2000, 'Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins', Infection and Immunity, vol. 68, no. 10, pp. 5696 - 5701.

Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins. / Virkola, R. (Corresponding Author); Brummer, Mirko; Rauvala, H.; van Alphen, L.; Korhonen, T.K.

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

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins

AU - Virkola, R.

AU - Brummer, Mirko

AU - Rauvala, H.

AU - van Alphen, L.

AU - Korhonen, T.K.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

M3 - Article

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JO - Infection and Immunity

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Virkola R, Brummer M, Rauvala H, van Alphen L, Korhonen TK. Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins. Infection and Immunity. 2000;68(10):5696 - 5701.