Lookup NU author(s): Dr Paula Salgado
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Candida albicans is the most prevalent fungal pathogen in humans and a major source of life-threatening nosocomial infections. The Als (agglutinin-like sequence) glycoproteins are an important virulence factor for this fungus and have been associated with binding of host-cell surface proteins and small peptides of random sequence, the formation of biofilms and amyloid fibers. High-resolution structures of N-terminal Als adhesins (NT-Als; up to 314 amino acids) show that ligand recognition relies on a motif capable of binding flexible C termini of peptides in extended conformation. Central to this mechanism is an invariant lysine that recognizes the C-terminal carboxylate of ligands at the end of a deep-binding cavity. In addition to several protein–peptide interactions, a network of water molecules runs parallel to one side of the ligand and contributes to the recognition of diverse peptide sequences. These data establish NT-Als adhesins as a separate family of peptide-binding proteins and an unexpected adhesion system for primary, widespread protein–protein interactions at the Candida/host-cell interface.
Author(s): Salgado PS, Yan R, Taylor JD, Buchnell L, Jones R, Hoyer L, Matthews SJ, Simpson P, Cota E
Publication type: Article
Journal: Proceedings of the National Academy of Sciences
Print publication date: 20/09/2011
ISSN (print): 0027-8424
ISSN (electronic): 1091-6490
Publisher: National Academy of Sciences
PubMed id: 21896717
Altmetrics provided by Altmetric