Structural hot spots determine functional diversity of the Candida glabrata epithelial adhesin family
Open accessAbstract
For host colonization, the human fungal pathogen Candida glabrata is known to utilize a large family of highly related surface-exposed cell wall proteins, the lectin-like epithelial adhesins (Epas). To reveal the structure-function relationships within the entire Epa family, we have performed a large scale functional analysis of the adhesion (A) domains of 17 Epa paralogs in combination with three-dimensional structural studies of selected members with cognate ligands. Our study shows that most EpaA domains exert lectin-like functions and together recognize a wide variety of glycans with terminal galactosides for conferring epithelial cell adhesion. We further identify several conserved and variable structural features within the diverse Epa ligand binding pockets, which affect affinity and specificity. These features rationalize why mere phylogenetic relationships within the Epa family are weak indicators for functional classification and explain how Epa-like adhesins have evolved in C. glabrata and related fungal species.
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Adherence analysis of S. cerevisiae strains expressing ligand-binding domains of 15 Epa adhesins individually revealed significant, moderate and very weak adherence to human epithelial colorectal adenocarcinoma cells (Caco2) for Epa1, 6 and 7; Epa8, 9, 12, 15 and 23; and Epa2, 3, 11, 13, 19, 20 and 21, respectively.
“Furthermore, adherence analysis of S. cerevisiae strains expressing ligand-binding domains of 15 Epa adhesins individually revealed significant, moderate and very weak adherence to human epithelial colorectal adenocarcinoma cells (Caco2) for Epa1, 6 and 7, Epa8, 9, 12, 15 and 23, and Epa2, 3, 11, 13, 19, 20 and 21, respectively [45].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [45]
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References 58 · Cited by 40
- Authors
- Diderrich, R., Kock, M., Maestre-Reyna, M., Keller, P., Steuber, H., Rupp, S., Essen, L.-O., & Mösch, H.-U.
- Affiliations
- Philipps University of Marburg (DE)
- Fraunhofer Institute for Interfacial Engineering and Biotechnology (DE)
- University of Stuttgart (DE)
- Corresponding author
- Essen, Lars-Oliver
- Mösch, Hans-Ulrich
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2015-08
- Volume
- 290
- Issue
- 32
- Pages
- 19597-19613
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4528126
- OpenAlex
- W2275145293
- Cited by
- 40
- References
- 58
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 2 · 2022: 3 · 2021: 6 · 2020: 6 · 2019: 6 · 2018: 4 · 2017: 2 · 2016: 5 · 2015: 2
- FWCI
- 1.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) (submittedVersion)
- HZB Repository (Helmholtz-Zentrum Berlin für Materialien und Energie GmbH (HZB)) (submittedVersion, other-oa)
- Fraunhofer-Publica (Fraunhofer-Gesellschaft) (submittedVersion)
- 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 › Glycosylation and Glycoproteins Research
- Keywords
- Candida glabrata, cell wall proteins, host colonization, epithelial cell adhesion, binding pocket, functional diversity, paralogs
- MeSH terms
- Amino Acid Sequence, Binding Sites, Escherichia coli, Biological Evolution, Fungal Proteins, Models, Molecular, Molecular Sequence Data, Phylogeny, Polysaccharides, Protein Binding, Recombinant Proteins, Genetic Variation, Cell Adhesion Molecules, Gene Expression, Sequence Alignment, Crystallography, X-Ray, Lectins, Candida glabrata, Protein Interaction Domains and Motifs
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