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• W3215744448 abstract "Candida Als family adhesins mediate adhesion to biological and abiotic substrates, as well as fungal cell aggregation and fungal-bacterial co-aggregation. The activity of at least two family members, Als5 and Als1, is dependent on amyloid-like protein aggregation that is initiated by shear force. Each Als adhesin has a ~300-residue N-terminal Ig-like/invasin region. The following 108-residue, low complexity, threonine-rich (T) domain unfolds under shear to expose a critical amyloid-forming segment 322 SNGIVIVATTRTV 334 at the interface between the Ig-like/invasin domain 2 and the T domain of Candida albicans Als5. Amyloid prediction programs identified six potential amyloidogenic sequences in the Ig/invasin region and three others in the T domain of C. albicans Als5. Peptides derived from four of these sequences formed fibrils that bound thioflavin T, the amyloid indicator dye, and three of these revealed atomic-resolution structures of cross-b spines. These are the first atomic-level structures for fungal adhesins. One of these segments, from the T domain, revealed kinked b-sheets, similarly to LARKS (Low-complexity, Amyloid-like, Reversible, Kinked segments) found in human functional amyloids. Based on the cross-b structures in Als proteins, we use evolutionary arguments to identify functional amyloidogenic sequences in other fungal adhesins. Thus, cross-b structures are often involved in fungal pathogenesis and potentially in antifungal therapy." @default.
• W3215744448 created "2021-12-06" @default.
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• W3215744448 date "2021-11-30" @default.
• W3215744448 modified "2023-09-25" @default.
• W3215744448 title "Structure and conservation of amyloid spines from the Candida albicans Als5 adhesin including similarity to human LARKS" @default.
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• W3215744448 doi "https://doi.org/10.1101/2021.11.29.470514" @default.
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