Proteolytic degradation of human salivary MUC5B by dental biofilms.

Claes Wickström, Mark C Herzberg, David Beighton, Gunnel Svensater

Research output: Contribution to journalArticlepeer-review

52 Citations (SciVal)

Abstract

The degradation of complex substrates, like salivary mucins, requires an arsenal of glycosidases and proteases to sequentially degrade the oligosaccharides and polypeptide backbone. MUC5B is a complex oligomeric glycoprotein, heterogeneous in molecular mass (14-40 x 106 Da), with a diverse repertoire of oligosaccharides, differing in composition and charge. The aim of this study was to investigate whether proteolytic degradation of the mucin polypeptide backbone could be identified and if cooperation of dental biofilm bacteria was required. Cooperative bacterial-mediated proteolysis of MUC5B was determined by comparing individual and mixed consortia of strains isolated from supragingival plaque and freshly harvested supragingival plaque. Proteolytic activity was analyzed using fluorescent labelled substrate and by visualizing mucin degradation by SDS-PAGE. Dental plaque degraded the polypeptide backbone of the salivary MUC5B mucin. The mucin also was degraded by a specific consortium of isolated species from supragingival plaque, although individual species and other consortia did not. Select bacteria in supragingival dental plaque, therefore, cooperate as a consortium to proteolyze human salivary MUC5B and hydrolyze glycosides.
Original languageEnglish
JournalMicrobiology
Early online date2009 Jun 25
DOIs
Publication statusPublished - 2009

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Mucosal biology (013212033)

Subject classification (UKÄ)

  • Cell and Molecular Biology

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