Abstract
Amyloid structures assemble through a repeating type of bonding called “cross-β”, in which identical sequences in many protein molecules form β-sheets that interdigitate through side chain interactions. We review the structural characteristics of such bonds. Single cell force microscopy (SCFM) shows that yeast expressing Als5 adhesin from Candida albicans demonstrate the empirical characteristics of cross-β interactions. These properties include affinity for amyloid-binding dyes, birefringence, critical concentration dependence, repeating structure, and inhibition by anti-amyloid agents. We present a model for how cross-β bonds form in trans between two adhering cells. These characteristics also apply to other fungal adhesins, so the mechanism appears to be an example of a new type of cell–cell adhesion.
Highlights
IntroductionWe have recently discovered that amyloid-like bonds form between cells in fungal biofilms [1,2]
Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Croix du Sud, Abstract: Amyloid structures assemble through a repeating type of bonding called “cross-β”, in which identical sequences in many protein molecules form β-sheets that interdigitate through side chain interactions
Cell bonds, and this discovery extends to roles in pathogenesis and biofilm formation
Summary
We have recently discovered that amyloid-like bonds form between cells in fungal biofilms [1,2]. These bonds show properties of cross-β aggregation, like the bonds formed between amyloid proteins in neurodegenerative diseases [3,4,5]. Cell bonds, and this discovery extends to roles in pathogenesis and biofilm formation If this new type of cell-to-cell bond formation proves to be general [6,7,8,9], there are important implications for the treatment of invasive fungal infections and for cell adhesion and histogenesis in other fungi and in animals [10,11,12,13]. Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations
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