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Comparative structural analysis of the glycosylation of salivary and buccal cell proteins: innate protection against infection by C. albicans.
MedLine Citation:
PMID:  22833316     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Mucosal epithelial surfaces, such as line the oral cavity, are common sites of microbial colonization by bacteria, yeast and fungi. The microbial interactions involve adherence between the glycans on the host cells and the carbohydrate binding proteins of the pathogen. Saliva constantly bathes the buccal cells of the epithelial surface of the mouth and we postulate that the sugars on the salivary glycoproteins provide an innate host immune mechanism against infection by competitively inhibiting pathogen binding to the cell membranes. The structures of the N- and O- linked oligosaccharides on the glycoproteins of saliva and buccal cell membranes were analysed using capillary carbon LC-ESI MS/MS. The 190 glycan structures that were characterized were qualitatively similar, but differed quantitatively, between saliva and epithelial buccal cell membrane proteins. The similar relative abundance of the terminal glycan epitope structures (e.g ABO(H) blood group, sialylation and Lewis type antigens) on saliva and buccal cell membrane glycoproteins indicated that the terminal N- and O- linked glycan substructures in saliva could be acting as decoy binding receptors to competitively inhibit the attachment of pathogens to the surface of the oral mucosa. A flow cytometry based binding assay quantified the interaction between buccal cells and the commensal oral pathogen Candida albicans. Whole saliva and released glycans from salivary proteins inhibited the interaction of C. albicans with buccal epithelial cells, confirming the protective role of the glycans on salivary glycoproteins against pathogen infection.
Authors:
Arun V Everest-Dass; Dayong Jin; Morten Thaysen-Andersen; Helena Nevalainen; Daniel Kolarich; Nicolle H Packer
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-7-24
Journal Detail:
Title:  Glycobiology     Volume:  -     ISSN:  1460-2423     ISO Abbreviation:  -     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-7-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Chemistry and Biomolecular Sciences, Faculty of Science, Macquarie University, Sydney, NSW, Australia.
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