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

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  2. Dr Paula Salgado
Author(s)Salgado PS, Yan R, Taylor JD, Buchnell L, Jones R, Hoyer L, Matthews SJ, Simpson P, Cota E
Publication type Article
JournalProceedings of the National Academy of Sciences
Year2011
Volume108
Issue38
Pages15775-15779
ISSN (print)0027-8424
ISSN (electronic)1091-6490
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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.
PublisherNational Academy of Sciences
URLhttp://dx.doi.org/10.1073/pnas.1103496108
DOI10.1073/pnas.1103496108
PubMed id21896717
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