Structure and Conservation of Amyloid Spines From the Candida albicans Als5 Adhesin.

ABSTRACT: Candida Als family adhesins mediate adhesion to biological and abiotic substrates, as well as fungal cell aggregation, fungal-bacterial co-aggregation and biofilm formation. 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 force to expose a critical amyloid-forming segment ³²²SNGIVIVATTRTV³³⁴ 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-like/invasin region and three ot

SUBMITTER: Golan N 

PROVIDER: S-EPMC9306254 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature