Secretory component mediates Candida albicans binding to epithelial cells

Objectives Candida albicans attaches to oral surfaces via a number of mechanisms including adherence mediated by salivary components adsorbed to the C. albicans cell surface. Our goal was to identify the salivary molecules involved. Materials and Methods Biotinylated salivary polypeptides that were...

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Published in:Oral diseases Vol. 22; no. 1; pp. 69 - 74
Main Authors: van der Wielen, PA, Holmes, AR, Cannon, RD
Format: Journal Article
Language:English
Published: Denmark Blackwell Publishing Ltd 01-01-2016
Wiley Subscription Services, Inc
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Summary:Objectives Candida albicans attaches to oral surfaces via a number of mechanisms including adherence mediated by salivary components adsorbed to the C. albicans cell surface. Our goal was to identify the salivary molecules involved. Materials and Methods Biotinylated salivary polypeptides that were bound by C. albicans were detected in extracts from washed, saliva‐treated yeast cells by polyacrylamide gel electrophoresis and electroblot or immunoblot transfer analysis and purified by electroelution. Purified material was tested for the ability to promote the adherence of radiolabelled C. albicans yeast cells to cultured epithelial monolayers. Results Three of the polypeptides bound by C. albicans cells were identified as components of secretory IgA, including secretory component. Using non‐denaturing polyacrylamide gel electrophoresis, we demonstrated that secretory component could be detected in its free form in saliva, and was bound by yeast cells. Secretory component which was purified by electroelution from non‐denaturing PAGE‐separated saliva, without detectable complete IgA, promoted adherence of yeast cells to cultured epithelial monolayers in a dose‐dependent fashion. Conclusion These results indicate that despite the inhibitory effect on adherence of IgA specific to C. albicans, IgA components, in particular secretory component, also promote binding to cultured epithelial monolayers.
Bibliography:ark:/67375/WNG-T4ZQMQVG-R
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istex:500EE62AD61BDBEBD83133917412866E5DD7BBF8
ArticleID:ODI12397
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1354-523X
1601-0825
DOI:10.1111/odi.12397