Abstract Selective adhesion of fungal cells to one another and to foreign surfaces is fundamental for the development of multicellular growth forms and the successful colonization of substrates and host organisms. Accordingly, fungi possess diverse cell wall-associated adhesins, mostly large glycoproteins, which present N-terminal adhesion domains at the cell surface for ligand recognition and binding. In order to function as robust adhesins, these glycoproteins must be covalently linkedto the cell wall via C-terminal glycosylphosphatidylinositol (GPI) anchors by transglycosylation. In this review, we summarize the current knowledge on the structural and functional diversity of so far characterized protein families of adhesion domains and set it into a broad context by an in-depth bioinformatics analysis using sequence similarity networks. In addition, we discuss possible mechanisms for the membrane-to-cell wall transfer of fungal adhesins by membrane-anchored Dfg5 transglycosidases.

中文翻译：

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GPI 锚定真菌粘附素的多样性

摘要 真菌细胞彼此之间以及与外来表面的选择性粘附是多细胞生长形式的发展以及基质和宿主生物成功定殖的基础。因此，真菌具有多种细胞壁相关粘附素，主要是大糖蛋白，它们在细胞表面呈现 N 端粘附结构域，用于配体识别和结合。为了起到强大的粘附素的作用，这些糖蛋白必须通过糖基转移通过 C 端糖基磷脂酰肌醇 (GPI) 锚共价连接到细胞壁。在这篇综述中，我们总结了目前关于粘附域特征蛋白家族的结构和功能多样性的当前知识，并通过使用序列相似性网络的深入生物信息学分析将其置于广泛的背景下。