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Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans

Lookup NU author(s): Dr Paula Salgado

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Abstract

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.


Publication metadata

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

Year: 2011

Volume: 108

Issue: 38

Pages: 15775-15779

Print publication date: 20/09/2011

ISSN (print): 0027-8424

ISSN (electronic): 1091-6490

Publisher: National Academy of Sciences

URL: http://dx.doi.org/10.1073/pnas.1103496108

DOI: 10.1073/pnas.1103496108

PubMed id: 21896717


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