Binding of extracellular matrix proteins to Aspergillus fumigatus conidia
- 1 December 1996
- journal article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 64 (12), 5239-47
- https://doi.org/10.1128/iai.64.12.5239-5247.1996
Abstract
As detected by confocal immunofluorescence microscopy, binding of fibronectin and laminin appeared to be associated with the protrusions present on the outer cell wall layer of resting Aspergillus fumigatus conidia. Flow cytometry confirmed that binding of laminin to conidia was dose dependent and saturable. Laminin binding was virtually eliminated in trypsin-treated organisms, thus suggesting the protein nature of the binding site. Conidia were also able to specifically adhere to laminin immobilized on microtiter plates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting (immunoblotting) with laminin and antilaminin antibody of whole conidial homogenates allowed identification, among the complex array of protein and glycoprotein species, of one polypeptide with an apparent molecular mass of 37 kDa which specifically interacts with laminin. The fact that binding of conidia to soluble or immobilized laminin or fibronectin was inhibited by fibronectin or laminin, respectively, suggests the existence of common binding sites for both ligands on the surface of conidia. Intact conidia were also able to adhere to type I and IV collagen immobilized on microtiter plates; adhesion was found to be dose dependent and saturable. Adhesion to immobilized type I and IV collagen was markedly inhibited by laminin and weakly inhibited by fibronectin. Coincubation of conidia with Arg-Gly-Asp (RGD) peptides caused a dose-dependent decrease in binding of cells to immobilized or soluble fibronectin, yet interaction of cells with soluble or immobilized laminin and type I and IV collagen remained unaffected. Interactions described here could be important in mediating attachment of the fungus to host tissues, thus playing a role in the establishment of the disease.Keywords
This publication has 19 references indexed in Scilit:
- Cell wall protein and glycoprotein constituents of Aspergillus fumigatus that bind to polystyrene may be responsible for the cell surface hydrophobicity of the myceliumMicrobiology, 1996
- The search for virulence determinants in Aspergillus fumigatusTrends in Microbiology, 1995
- Study of surface carbohydrates on isolated Golgi subfractions by fluorescent‐lectin binding and flow cytometryCytometry, 1995
- MSCRAMM-MEDIATED ADHERENCE OF MICROORGANISMS TO HOST TISSUESAnnual Review of Microbiology, 1994
- Interaction between Aspergillus fumigatus and basement membrane laminin: Binding and substrate degradationBiology of the Cell, 1993
- Basement Membrane Proteins: Structure, Assembly, and Cellular InteractionsCritical Reviews in Biochemistry and Molecular Biology, 1992
- AspergillosisEuropean Journal of Clinical Microbiology & Infectious Diseases, 1989
- Specific binding of collagen type IV to Streptococcus pyogenesFEMS Microbiology Letters, 1989
- The emergence of fungi as major hospital pathogensJournal of Hospital Infection, 1988
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970