Cell wall protein mannosylation determines Candida albicans cell surface hydrophobicity
Cell wall protein mannosylation determines Candida albicans cell surface hydrophobicity
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DOI：
10.1099/00221287-143-9-3015
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发表时间：
1997-09-01
期刊：
影响因子：
--
通讯作者：
Hazen, KC
中科院分区：
文献类型：
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作者：
Masuoka, J;Hazen, KC
细胞表面疏水性 (CSH) 已被证明是机会致病性酵母白色念珠菌粘附于表面的能力的重要因素。与亲水细胞相比，疏水细胞更容易粘附到宿主组织上，并且更能抵抗吞噬细胞的杀伤。因此，CSH 在白色念珠菌的致病性中起着重要作用。先前的工作表明 CSH 与细胞壁蛋白糖基化之间存在关系。目前的工作测试了以下假设：外链甘露糖基化的变化（而不是寡糖基团的完全丧失）足以调节 CSH。这些研究将野生型细胞与改变了甘露糖基化且在野生型细胞亲水性条件下呈疏水性的变体进行了比较。细胞表面消化物的成分分析表明，野生型细胞表面蛋白的糖基化比变体中的糖基化广泛得多。识别白色念珠菌甘露聚糖酸不稳定和酸稳定部分的抗体不仅显示野生型和变异细胞之间的差异，而且还显示野生型亲水性和野生型疏水性细胞之间的差异。结果表明，白色念珠菌表面疏水区域的暴露可能与磷酸二酯连接的酸不稳定甘露糖基的丰度有关，而不是与细胞壁蛋白上外链甘露糖基的完全丧失有关。
Cell surface hydrophobicity (CSH) has been shown to be an important factor in the ability of the opportunistic pathogenic yeast Candida albicans to adhere to surfaces. Hydrophobic cells adhere more readily to host tissue, and are more resistant to phagocytic killing, than hydrophilic cells. Consequently, CSH plays an important role in the pathogenicity of C. albicans. Previous work suggested a relationship between CSH and cell wall protein glycosylation. The present work tests the hypothesis that changes in outer chain mannosylation, rather than complete loss of oligosaccharide groups, are sufficient to modulate CSH. These studies compared wild-type cells to a variant that has altered mannosylation and is hydrophobic under conditions in which wild-type cells are hydrophilic. Composition analysis of cell surface digests showed that the glycosylation of wild-type cell surface proteins was much more extensive than that seen in the variant. Antibodies which recognize the acid-labile and acid-stable portions of C. albicans mannan showed not only differences between wild-type and variant cells but also differences between wild-type hydrophilic and wild-type hydrophobic cells. The results suggest that exposure of surface hydrophobic regions on C. albicans may be related to the abundance of phosphodiester-linked, acid-labile mannosyl groups rather than the complete loss of outer chain mannosylation on cell wall proteins.