Interaction of human fibronectin with Candida glabrata epithelial adhesin 6 (Epa6)

Zajac, Dorota; Karkowska-Kuleta, Justyna; Bochenska, Oliwia; Rapala-Kozik, Maria; Kozik, Andrzej

doi:10.18388/abp.2016_1328

Cited by 26Antifungal resistance and susceptibilityFungal and yeast genetics researchFungal Infections and Studies

Interaction of human fibronectin with Candida glabrata epithelial adhesin 6 (Epa6)

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Zajac, Dorota, Karkowska-Kuleta, Justyna, Bochenska, Oliwia, Rapala-Kozik, Maria, Kozik, Andrzej·2016·Acta Biochimica Polonica

DOI 10.18388/abp.2016_1328

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Abstract

Adherence of pathogens to extracellular matrix proteins and host cells is one of the essential steps in the microbial colonization of the human organism. The adhesion of C. glabrata, i.e. the second major causative agent of human disseminated candidiases after C. albicans, to the host epithelium mainly engages specific fungal cell wall proteins - epithelial adhesins (Epa) - in particular, Epa1, Epa6 and Epa7. The aim of the present study was to identify the major Epa protein involved in the interactions with the human extracellular matrix protein - fibronectin - and to present the kinetic and thermodynamic characteristics of these interactions. A relatively novel gel-free approach, i.e. the "cell surface shaving" that consists in short treatment of fungal cells with trypsin was employed to identify the C. glabrata surfaceome. Epa6 was purified, and the isolated protein was characterized in terms of its affinity to human fibronectin using a microplate ligand-binding assay and surface plasmon resonance measurements. The dissociation constants for the binding of Epa6 to fibronectin were determined to range between 9.03 × 10(-9) M and 7.22 × 10(-8) M, depending on the method used (surface plasmon resonance measurements versus the microplate ligand-binding assay, respectively). The identified fungal pathogen-human host protein-protein interactions might become a potential target for novel anticandidal therapeutic approaches.

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Epa6 mediates binding of C. glabrata to the human extracellular matrix protein fibronectin.
“Epa6 is also known to mediate binding of C. glabrata to the human extracellular matrix protein, fibronectin [133].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [133]

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Authors: Zajac, D., Karkowska-Kuleta, J., Bochenska, O., Rapala-Kozik, M., & Kozik, A.
Affiliations: Jagiellonian University (PL)
ORCID: Kozik, Andrzej
Venue: Acta Biochimica Polonica
Publisher: Frontiers Media SA
Published: 2016-07-30
Volume: 63
Issue: 3
Pages: 417-26
ISSN: 0001-527X (ISSN-L)
1734-154X
DOI: 10.18388/abp.2016_1328
OpenAlex: W2489471518
Cited by: 26
References: 59
Citations by year: 2026: 5 · 2025: 3 · 2024: 2 · 2023: 3 · 2021: 2 · 2020: 6 · 2019: 1 · 2018: 4
FWCI: 1.54
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by-sa
Locations: Acta Biochimica Polonica (publishedVersion, cc-by-sa)
PubMed (publishedVersion)
Jagiellonian University Repository (Jagiellonian University) (submittedVersion, cc-by-nc-nd)
Funders: European Commission (POIG.02.01.00-12-167/08, POIG.02.01.00-12-064/08)
Uniwersytet Jagielloński w Krakowie
European Regional Development Fund (POIG..02.01.00-12-167/08)
Topics: Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
Keywords: Candida glabrata, fibronectin, fungal adhesion, host-pathogen interaction, trypsinization, surfaceome, binding affinity, dissociation constant, extracellular matrix, systemic candidiasis
MeSH terms: Cell Wall, Fibronectins, Fungal Proteins, Humans, Kinetics, Protein Binding, Lectins, Candida glabrata, Immobilized Proteins

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Interaction of human fibronectin with Candida glabrata epithelial adhesin 6 (Epa6)

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