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Threonine-Rich Repeats Increase Fibronectin Binding in the Candidaalbicans Adhesin Als5p
Open accessAbstract
Commensal and pathogenic states of Candida albicans depend on cell surface-expressed adhesins, including those of the Als family. Mature Als proteins consist of a 300-residue N-terminal region predicted to have an immunoglobulin (Ig)-like fold, a 104-residue conserved Thr-rich region (T), a central domain of a variable number of tandem repeats (TR) of a 36-residue Thr-rich sequence, and a heavily glycosylated C-terminal Ser/Thr-rich stalk region, also of variable length (N. K. Gaur and S. A. Klotz, Infect. Immun. 65: 5289-5294, 1997). Domain deletions in ALS5 were expressed in Saccharomyces cerevisiae to excrete soluble protein and for surface display. Far UV circular dichroism indicated that soluble Ig-T showed a single negative peak at 212 nm, consistent with previous data indicating that this region has high beta-sheet content with very little alpha-helix. A truncation of Als5p with six tandem repeats (Ig-T-TR(6)) gave spectra with additional negative ellipticity at 200 nm and, at 227 to 240 nm, spectra characteristic of a structure with a similar fraction of beta-sheet but with additional structural elements as well. Soluble Als5p Ig-T and Ig-T-TR(6) fragments bound to fibronectin in vitro, but the inclusion of the TR region substantially increased affinity. Cellular adhesion assays with S. cerevisiae showed that the Ig-T domain mediated adherence to fibronectin and that TR repeats greatly increased cell-to-cell aggregation. Thus, the TR region of Als5p modulated the structure of the Ig-T region, augmented cell adhesion activity through increased binding to mammalian ligands, and simultaneously promoted fungal cell-cell interactions.
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“In addition, Rauceo et al. [38] reported that the absence of tandem repeats reduced the binding affinity of Als5.”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [38]
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BackgroundSelf-citation
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Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells
Phan, Q. T., Myers, C. L., Fu, Y., Sheppard, D. C., Yeaman, M. R., Welch, W. H., Ibrahim, A. S., Edwards, J. E., & Filler, S. G. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050064 · Cited by 641
“[38] reported that the absence of tandem repeats reduced the binding affinity of Als5.”
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Candida albicans Als3, a multifunctional adhesin and invasin
Liu, Y., & Filler, S. G. (2011) · Eukaryotic Cell · doi:10.1128/ec.00279-10 · Cited by 354
Complementary Adhesin Function in C. albicans Biofilm Formation
Nobile, C. J., Schneider, H. A., Nett, J. E., Sheppard, D. C., Filler, S. G., Andes, D. R., & Mitchell, A. P. (2008) · Current Biology · doi:10.1016/j.cub.2008.06.034 · Cited by 351
Wang, C.-S., & Leger, R. S. (2007) · Eukaryotic Cell · doi:10.1128/ec.00409-06 · Cited by 337
“The working model for ALS proteins is that the tandem repeats are heavily glycosylated to produce a rigid elongated structure that holds the adhesive N-terminal domain at the cell surface (14, 25).”
Background
Metadata
- Authors
- Rauceo, J. M., De Armond, R., Otoo, H., Kahn, P. C., Klotz, S. A., Gaur, N. K., & Lipke, P. N.
- Affiliations
- City University of New York (US)
- Southern Arizona VA Health Care System, Tucson, Arizona
- Rutgers, The State University of New Jersey (US)
- University of Arizona (US)
- Southern Arizona VA Health Care System (US)
- Venue
- Eukaryotic Cell
- Publisher
- American Society for Microbiology
- Published
- 2006-10
- Volume
- 5
- Issue
- 10
- Pages
- 1664-1673
- ISSN
- 1535-9778 (ISSN-L)
- 1535-9786
- PMC
- PMC1595330
- OpenAlex
- W2146537281
- Cited by
- 115
- References
- 38
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 5 · 2016: 4 · 2015: 3 · 2014: 14 · 2013: 9 · 2012: 11
- FWCI
- 4.08
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Eukaryotic Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- U.S. Public Health Service (S06 60654)
- National Institute of General Medical Sciences (F31GM070122)
- National Center for Research Resources (RR 030307)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- Candida albicans, fibronectin binding, immunoglobulin-like domains, protein secondary structure, β-sheet content, cell adhesion, cell-cell aggregation, fungal virulence
- MeSH terms
- Animals, Candida albicans, Cell Adhesion, Circular Dichroism, Concanavalin A, Fibronectins, Fungal Proteins, Horseradish Peroxidase, Immunoglobulins, Peptide Fragments, Protein Binding, Substrate Specificity, Threonine, Yeasts, Cell Adhesion Molecules, Protein Structure, Secondary, Protein Structure, Tertiary, Repetitive Sequences, Amino Acid
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