Correction: Activation of Notch-1 in oral epithelial cells by P. gingivalis triggers the expression of the antimicrobial protein PLA2-IIA

ABSTRACTTo protect against invading bacteria, oral epithelial cells appear to use two effector antimicrobial peptides (AMPs): calprotectin (S100A8-S100A9 heterodimer [S100A8/A9]) in the cytosol and cathelicidin antimicrobial protein (CAMP) in endosomes. We sought to learn whether innate immunity might be augmented benignly to increase resistance against invasive bacteria. Epithelial cells were transiently transfected with mRNA constructs containing either theCAMP,S100A8, andS100A9open reading frames,A8-IRES-A9(fusion sequence), orA8-nIRES-A9(fusion with native internal ribosome entry site [IRES] sequence). CAMP, S100A8, and S100A9 protein levels generally peaked between 16 and 44 h after mRNA transfection, depending on the construct; CAMP was processed to LL-37 over time. Following transfection with the respective mRNAs, CAMP and S100A8/A9 each independently increased resistance of epithelial cells to invasion byListeriaandSalmonellafor up to 48 h; tandem S100A8/A9 constructs were also effective. Cotransfection to express S100A8/A9 and CAMP together augmented resistance, but synergy was not seen. Independent of the new proteins produced, transfection reduced cell viability after 48 h by 20%, with only 2% attributable to apoptosis. Taken together, these results suggest that epithelial cell resistance to invasive pathogens can be augmented by transient transfection of antimicrobial mRNAs into epithelial cells.

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Faculty Opinions recommendation of From attachment to damage: defined genes of Candida albicans mediate adhesion, invasion and damage during interaction with oral epithelial cells.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.11552956.12602054 ◽

2011 ◽

Author(s):

Judith Berman ◽

Anja Forche

Keyword(s):

Candida Albicans ◽

Epithelial Cells ◽

Oral Epithelial Cells ◽

Oral Epithelial

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Assessment of the Effect of Complete Denture Adhesives on Oral Epithelial Cells’ DNA in Elderly Patients with Controlled Diabetes

Egyptian Dental Journal ◽

10.21608/edj.2018.77272 ◽

2018 ◽

Vol 64 (3) ◽

pp. 2747-2756

Author(s):

Noha El-Shaheed ◽

Amira Gomaa ◽

Ashraf Zakaria

Keyword(s):

Epithelial Cells ◽

Elderly Patients ◽

Complete Denture ◽

Oral Epithelial Cells ◽

Denture Adhesives ◽

Oral Epithelial

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Novel Aggregation Properties of Candida albicans Secreted Aspartyl Proteinase Sap6 Mediate Virulence in Oral Candidiasis

Infection and Immunity ◽

10.1128/iai.00282-15 ◽

2015 ◽

Vol 83 (7) ◽

pp. 2614-2626 ◽

Cited By ~ 35

Author(s):

Rohitashw Kumar ◽

Darpan Saraswat ◽

Swetha Tati ◽

Mira Edgerton

Keyword(s):

Candida Albicans ◽

Epithelial Cells ◽

Oral Candidiasis ◽

Oral Microbiome ◽

Proteinase Activity ◽

Adhesion Properties ◽

Content Type ◽

Oral Epithelial Cells ◽

Oral Epithelial ◽

Cell Cell

Candida albicans, a commensal fungus of the oral microbiome, causes oral candidiasis in humans with localized or systemic immune deficiencies. Secreted aspartic proteinases (Saps) are a family of 10 related proteases and are virulence factors due to their proteolytic activity, as well as their roles in adherence and colonization of host tissues. We found that mice infected sublingually withC. albicanscells overexpressing Sap6 (SAP6OE and a Δsap8strain) had thicker fungal plaques and more severe oral infection, while infection with the Δsap6strain was attenuated. These hypervirulent strains had highly aggregative colony structurein vitroand higher secreted proteinase activity; however, the levels of proteinase activity ofC. albicansSaps did not uniformly match their abilities to damage cultured oral epithelial cells (SCC-15 cells). Hyphal induction in cells overexpressing Sap6 (SAP6OE and Δsap8cells) resulted in formation of large cell-cell aggregates. These aggregates could be produced in germinated wild-type cells by addition of native or heat-inactivated Sap6. Sap6 bound only to germinated cells and increasedC. albicansadhesion to oral epithelial cells. The adhesion properties of Sap6 were lost upon deletion of its integrin-binding motif (RGD) and could be inhibited by addition of RGD peptide or anti-integrin antibodies. Thus, Sap6 (but not Sap5) has an alternative novel function in cell-cell aggregation, independent of its proteinase activity, to promote infection and virulence in oral candidiasis.

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