Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans
- Lookup NU author(s)
- 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 |
| Journal | | Proceedings of the National Academy of Sciences. |
| Year | | 2011 |
| Volume | | 108 |
| Issue | | 38 |
| Pages | | 15775-15779 |
| ISSN (print) | | 0027-8424 |
| ISSN (electronic) | | 1091-6490 |
|
|
|
| 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. |
|
|
|
| Publisher | | National Academy of Sciences |
| URL | | http://dx.doi.org/10.1073/pnas.1103496108 |
| DOI | | 10.1073/pnas.1103496108 |
| PubMed id | | 21896717 |
|
|
Actions | |   |
