Cited by 28Antifungal resistance and susceptibilityFungal and yeast genetics researchFungal Infections and Studies

Human oral keratinocyte E-cadherin degradation by Candida albicans and Candida glabrata

Pärnänen, Pirjo, Meurman, Jukka H., Samaranayake, Lakshman, Virtanen, Ismo·2010·Journal of Oral Pathology & Medicine

Abstract

BACKGROUND: E-cadherin (E-Cad) is a 120-kDa adhesive protein found in adherens junctions of the digestive tract epithelium. We tested the ability of two Candida strains to degrade human E-Cad in the Candida virulence factor perspective. MATERIALS AND METHODS: We set out to study oral mucosal E-Cad degradation by clinical and reference strains of Candida albicans and Candida glabrata. We also included hyphal and secreted aspartic proteinase (Sap) mutants of C. albicans to test the effect of yeast/hyphal transition on the ability to degrade E-Cad. The tests were performed at pH 4 and pH 6 to determine the effect of local tissue acidity on the activation of Saps. The C. albicans strains used were: CCUG 32723; clinical strain SC5314 which is known to be strongly invasive; hyphal mutants of SC5314: HLC52 (efg1/efg1), HLC54 (cph1/cph1 efg1/efg1) and JKC19 (cph1/cph1); clinical strain B1134; Sap 1-3 and Sap 4-6 mutants of SC5314. The C. glabrata strains used were ATCC 90030, and the clinical strains 5WT and G212. RESULTS: The sonicated yeast cells of C. albicans JKC19 and SC5314, both in hyphal form, degraded E-Cad at pH 4. The 10x concentrated growth media of the strains HLC-52, HLC-54, 32723 and B1134; all in yeast form, caused degradation at pH 4, HLC-52 and HLC-54 also at pH 6. The C. glabrata strains did not degrade E-Cad. CONCLUSIONS: pH is a strain dependent triggering factor in activating yeast or hyphal form related Candida Saps in degrading epithelial cell associated E-Cads.

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Crossref · 10.1111/j.1600-0714.2009.00866.x

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  • C. glabrata could not degrade the E-Cadherin protein present in the adherens junctions of the oral mucosal epithelium.

    “Similarly, C. glabrata could neither degrade the E-Cadherin protein present in the adherens junctions of the oral mucosal epithelium [135] nor invade the reconstituted human oral epithelium in vitro [130].”

    From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [135]

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Authors
Pärnänen, P., Meurman, J. H., Samaranayake, L., & Virtanen, I.
Affiliations
  • University of Helsinki (FI)
  • University of Hong Kong (HK)
Corresponding author
Pärnänen, Pirjo
Venue
Journal of Oral Pathology & Medicine
Publisher
Wiley
Published
2010-03
Volume
39
Issue
3
Pages
275-278
ISSN
  • 0300-9777 (ISSN-L)
  • 0904-2512
  • 1600-0714
OpenAlex
W1973074732
Cited by
28
References
22
Citations by year
2026: 1 · 2025: 2 · 2024: 1 · 2023: 2 · 2022: 5 · 2021: 2 · 2020: 3 · 2019: 1 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 3
FWCI
1.65
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Oral Pathology and Medicine (publishedVersion)
  • PubMed (publishedVersion)
  • The HKU Scholars Hub (University of Hong Kong) (submittedVersion)
Funders
  • Helsingin ja Uudenmaan Sairaanhoitopiiri
  • Suomen Hammaslääkäriliitto
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
E-cadherin degradation, Candida albicans, Candida glabrata, secreted aspartic proteinases, oral keratinocytes, hyphal morphology, yeast-to-hypha transition, adherens junctions, fungal virulence factors, oral candidiasis
MeSH terms
Candida albicans, Cell Adhesion, Cell Line, Epithelial Cells, Fungal Proteins, Humans, Hydrogen-Ion Concentration, Mouth Mucosa, Virulence, Keratinocytes, Cadherins, Aspartic Acid Endopeptidases, Hyphae, Candida glabrata

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