Interaction of fimbriae of Haemophilus influenzae type B with heparin-binding extracellular matrix proteins.
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.
Virkola
R
R
Division of General Microbiology, and Institute of Biotechnology, University of Helsinki, Helsinki, Finland. ritva.virkola@helsinki.fi
Brummer
M
M
Rauvala
H
H
van Alphen
L
L
Korhonen
T K
TK
D000818:Animals; D001422:Bacterial Adhesion; D002352:Carrier Proteins / Q000378:metabolism; D016207:Cytokines / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D019741:Haemophilus influenzae type b / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D015151:Immunoblotting; D051379:Mice
D002352:Carrier Proteins; D016207:Cytokines; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; C066845:pleiotrophin; D006493:Heparin