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Adhesion of conidia and germlings of the plant pathogenic fungus Bipolaris sorokiniana to solid surfaces

粘附 分生孢子 两极 生物 植物 微生物学 化学 有机化学
作者
Dace Apoga,Hans Jansson,Andres Tunlid
出处
期刊:Fungal Biology [Elsevier]
卷期号:105 (10): 1251-1260 被引量:7
标识
DOI:10.1017/s0953756201004683
摘要

Soon after coming in contact with its host, the plant pathogenic fungus Bipolaris sorokiniana produces an extracellular material that appears to be important for adhering conidia and germlings to the host surface. To further understand this step of the infection, the adhesion of B. sorokiniana to artificial solid surfaces was examined. On a hydrophobic (polystyrene) surface adhesion occurred in two stages, the first by conidia and the second by germlings. Conidial adhesion occurred shortly (0-1 h) after hydration. The conidia were easily detached by increasing the shear force and including detergents in the washing buffer. As conidia were hydrophobic, these observations indicate that conidial adhesion to polystyrene is due to weak, hydrophobic interaction. The second stage of adhesion was accompanied by conidial germination and occurred 1-2 h after hydration and contact with the surface. Concomitant with the delayed adhesion, the fungus produced an extracellular matrix (ECM). The adhesion of germlings was firm and surface-unspecific since they adhered to both hydrophobic and hydrophilic (glass) surfaces, Except for strong bases, hydrochloric acid and broad-specificity proteases (including Pronase E), none of the hydrolytic enzymes, electrolyte solutions, ionic and hydrophobic detergents and organic solvents removed germlings from the solid surfaces. The adhesion of germlings incubated in the presence of the protein glycosylation inhibitor tunicamycin or the lectins Con A (Concanavalin A) and GNA (from Galanthus nivalis) was significantly reduced, which indicates the involvement of surface glycoproteins in this process. The surface proteins of germlings were labelled with I-125, extracted and analysed by two-dimensional gel electrophoresis. This revealed about 40 surface proteins over a wide pH range (4-10) with molecular masses between 10 and 100 kDa.

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