Functional analysis of the Candida albicans ALS1 gene product
Abstract
ALS1 encodes a cell surface protein that mediates adherence of Candida albicans to endothelial cells. The predicted Als1p has an N‐terminal region, which contains a signal peptide; a middle region, which contains 20 36‐amino acid tandem repeats; and a C‐terminal region, which contains a glycosylphosphotidylinositol‐anchorage sequence. We used site‐directed mutagenesis to delineate the regions in Als1p required for endothelial cell adherence and cell surface expression of the protein. Mutant alleles of ALS1 containing either deletions or insertions were expressed in the normally non‐adherent Saccharomyces cerevisiae. These transformants were analysed for endothelial cell adherence and cell surface expression of Als1p. We found that mutations centred around amino acid 285 in the N‐terminus completely abolished adherence, but had no effect on cell surface expression of Als1p. Deletion of 15 of the tandem repeats reduced adherence by 50%, whereas deletion of all abolished adherence completely, even though cell surface expression of the N‐terminus of Als1p was maintained. Insertions into the C‐terminus at amino acids 413 and 254 upstream of the stop codon resulted in a modest loss of adherence, while cell surface expression of Als1p was maintained. An insertion at amino acid 249 in the C‐terminus caused complete loss of both adherence and cell surface expression, even though the glycosylphosphotidylinositol‐anchorage sequence remained intact. These data suggest a model of Als1p in which the endothelial cell binding region is localized within its N‐terminus, the tandem repeats are essential for the proper presentation of the binding site, and the C‐terminus is required for localizing Als1p to the cell surface. Copyright © 2004 John Wiley & Sons, Ltd.
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The N-terminal region of Als proteins contains the substrate-binding site.
“Previously, we determined that the N-terminal region of Als proteins contains the substrate-binding site [23,26].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [26]
The N-terminal domain of Als proteins contains the substrate-binding region.
“The N-terminal domain contains the substratebinding region [23,26].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [26]
The adhesive function of Als1 is dramatically reduced when some or all of the tandem repeats are eliminated.
“Previously, we have found that the adhesive function of Als1 is dramatically reduced when some or all of the tandem repeats are eliminated [26].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [26]
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BackgroundSelf-citation
- Authors
- Loza, L., Fu, Y., Ibrahim, A. S., Sheppard, D. C., Filler, S. G., & Edwards, J. E.
- Affiliations
- University of California, Los Angeles (US)
- Corresponding author
- Filler, Scott G.
- Venue
- Yeast
- Publisher
- Wiley
- Published
- 2004-04-14
- Volume
- 21
- Issue
- 6
- Pages
- 473-482
- ISSN
- 0749-503X (ISSN-L)
- 1097-0061
- OpenAlex
- W2046687663
- Cited by
- 78
- References
- 0
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2021: 2 · 2020: 1 · 2019: 3 · 2018: 4 · 2017: 3 · 2016: 5 · 2015: 4 · 2014: 10 · 2013: 1 · 2012: 2
- FWCI
- 1.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Yeast (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Bristol-Myers Squibb
- Toyota USA
- National Institutes of Health (1s10rr013004-01a1)
- National Institute of Allergy and Infectious Diseases (P01 AI-37194, R01AI019990, R01-AI19990, P01AI037194)
- National Institute of Dental and Craniofacial Research (R01DE013974, R01 DE 13974)
- National Center for Research Resources (1S10 RR 13004, M01RR000425, M01-RR00425)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
- Keywords
- Candida albicans, cell surface adhesins, tandem repeats, cell surface expression, N-terminal binding site, Saccharomyces cerevisiae expression
- MeSH terms
- Candida albicans, Cell Adhesion, DNA, Fungal, Flow Cytometry, Fungal Proteins, Humans, Transformation, Genetic, Mutagenesis, Site-Directed, Antibodies, Blocking, Tandem Repeat Sequences, Endothelial Cells
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