title: Cell surface properties of Aspergillus fumigatus conidia: correlation between adherence, agglutination, and rearrangements of the cell wall.
abstract: Culture conditions that lead to swelling and germination dramatically influence cell surface characteristics and properties of Aspergillus fumigatus conidia. Conidial adherence to polystyrene and agglutination markedly increased during swelling, in a time-dependent manner. Agglutination appeared to be sensitive to cycloheximide and calcium. Removal of cell wall polysaccharides by lyticase or sodium metaperiodate suppressed agglutination of conidia. Proteinase K weakly decreased it whereas dithiothreitol strongly dispersed the cells. These observations suggest that both cell surface carbohydrates and proteins are involved in the agglutination process. Electron microscopic observations demonstrated that the cell wall of conidia was subject to some rearrangements during swelling, involving degradation and loss of the external convoluted layer, and subsequent exposure of underlying ligands. This was confirmed using lectins labelled with gold or fluorescein isothiocyanate, which showed that some carbohydrates, particularly those acting as ligands for peanut agglutinin, are largely exposed during the process. Finally, SDS-PAGE revealed major protein changes between resting and swollen conidia. We conclude that the ability of A. fumigatus conidia to aggregate correlates with an increase in adherence and biochemical reorganization of the cell wall.
authors.affiliation: Laboratoire de parasitologie-mycologie, Centre hospitalier universitaire, Angers, France.
authors.forename: G
authors.initials: G
authors.lastname: Tronchin
authors.forename: J P
authors.initials: JP
authors.lastname: Bouchara
authors.forename: M
authors.initials: M
authors.lastname: Ferron
authors.forename: G
authors.initials: G
authors.lastname: Larcher
authors.forename: D
authors.initials: D
authors.lastname: Chabasse
mesh_terms: D001232:Aspergillus fumigatus / Q000254:growth & development / Q000502:physiology* / Q000648:ultrastructure*; D001665:Binding Sites; D002240:Carbohydrate Sequence; D002448:Cell Adhesion / Q000502:physiology; D002473:Cell Wall / Q000502:physiology / Q000648:ultrastructure; D005656:Fungal Proteins / Q000378:metabolism; D037102:Lectins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D037102:Lectins; D008565:Membrane Proteins; D011134:Polysaccharides