Candida albicans Als Adhesins Have Conserved Amyloid-Forming Sequences
| Autor: | Peter N. Lipke, Henry N. Otoo, Kyeng Gea Lee, Wei-Gang Qiu |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Amyloid
Protein Folding Microbiology Conserved sequence Evolution Molecular Fungal Proteins chemistry.chemical_compound Microscopy Electron Transmission mental disorders Candida albicans Amino Acid Sequence Molecular Biology Peptide sequence Conserved Sequence Fungal protein biology Articles General Medicine biology.organism_classification Molecular biology Recombinant Proteins Congo red chemistry Biochemistry Thioflavin Protein folding Peptides Cell Adhesion Molecules |
| Zdroj: | Eukaryotic Cell. 7:776-782 |
| ISSN: | 1535-9786 1535-9778 |
| Popis: | The cell wall-bound Als adhesins of Candida albicans mediate both yeast-to-host tissue adherence and yeast aggregation. This aggregation is amyloid-like, with self-propagating secondary-structure changes, amyloid-characteristic dye binding, and induced birefringence (J. M. Rauceo, N. K. Gaur, K. G. Lee, J. E. Edwards, S. A. Klotz, and P. N. Lipke, Infect. Immun. 72:4948-4955, 2004). Therefore, we determined whether Als proteins could form amyloid fibers with properties like those in cellular aggregation. The β-aggregation predictor TANGO identified a heptapeptide sequence present in a highly conserved sequence with amyloid-forming potential in Als1p, Als3p, and Als5p. A tridecapeptide containing this sequence formed fibers that bound Congo red and thioflavin T and had characteristic amyloid morphology. Als5p 20-431 and Als5p 20-664 , large fragments of Als5p containing the amyloid sequence, also formed amyloid-like fibers and bound Congo red under native conditions. K a / K s analysis showed that the amyloid-forming sequences are highly conserved in Als proteins and evolve more slowly than other regions of the proteins. Therefore, amyloid-forming ability itself is conserved in these proteins. |
| Databáze: | OpenAIRE |
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