Interactions between Candida albicans and the human extracellular matrix component tenascin-C.
Tenascins are large multimeric proteins that contain repeated structural motifs that include epidermal growth factor (EGF)-like repeats, fibronectin type III repeats and a globular fibrinogen-like domain, and are involved in tissue and organ morphogenesis, as well as in adhesion and migration of cells. C. albicans germ-tubes, but not blastospores, were able to bind to soluble human tenascin-C as revealed by an indirect immunofluorescence assay. However, materials present in cell wall extracts from both morphologies attached to tenascin-C immobilized in wells of a microtiter plate. The binding specificity was demonstrated by the inhibitory effect of antibodies against C. albicans cell wall components and an anti-tenascin antibody, but not anti-laminin antibody. Fibronectin, but not fibrinogen, inhibited binding, thus indicating a role of the fibronectin type III repeats in the interaction between the fungus and tenascin-C. Binding of C. albicans cell wall materials to tenascin was RGD- and divalent cation-independent.
López-Ribot
J L
JL
Department of Microbiology and Immunology, Texas Tech University Health Sciences Center, Lubbock 79430, USA.
Bikandi
J
J
San Millán
R S
RS
Chaffin
W L
WL
D002118:Calcium / Q000494:pharmacology; D002176:Candida albicans / Q000378:metabolism*; D002413:Cations, Divalent; D002448:Cell Adhesion / Q000502:physiology; D002457:Cell Extracts; D002473:Cell Wall; D005109:Extracellular Matrix / Q000378:metabolism*; D005340:Fibrinogen / Q000494:pharmacology; D005353:Fibronectins / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D006801:Humans; D008274:Magnesium / Q000494:pharmacology; D011485:Protein Binding; D019063:Tenascin / Q000378:metabolism*
D002413:Cations, Divalent; D002457:Cell Extracts; D005353:Fibronectins; D019063:Tenascin; D005340:Fibrinogen; D008274:Magnesium; D002118:Calcium