Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Real-time monitoring of adherence of Streptococcus anginosus group bacteria to extracellular matrix decorin and biglycan proteoglycans in biofilm formation

Landrygan-Bakri, Janine, Wilson, Melanie J., Williams, David Wynne, Lewis, Michael Alexander Oxenham and Waddington, Rachel J. 2012. Real-time monitoring of adherence of Streptococcus anginosus group bacteria to extracellular matrix decorin and biglycan proteoglycans in biofilm formation. Research in Microbiology 163 (6-7) , pp. 436-447. 10.1016/j.resmic.2012.07.006

[img]
Preview
Text - Accepted Post-Print Version
Download (1MB) | Preview

Abstract

Members of the Streptococcus anginosus group (SAGs) are significant pathogens. However, their pathogenic mechanisms are incompletely understood. This study investigates the adherence of SAGs to the matrix proteoglycans decorin and biglycan of soft gingival and alveolar bone. Recombinant chondroitin 4-sulphate(C4S)-conjugated decorin and biglycan were synthesised using mammalian expression systems. C4S-conjugated decorin/biglycan and dermatan sulphate (DS) decorin/biglycan were isolated from ovine alveolar bone and gingival connective tissue, respectively. Using surface plasmon resonance, adherence of the SAGs S. anginosus, Streptococcus constellatus and Streptococcus intermedius to immobilised proteoglycan was assessed as a function of real-time biofilm formation. All isolates adhered to gingival proteoglycan, 59% percent of isolates adhered to alveolar proteoglycans, 70% to recombinant decorin and 76% to recombinant biglycan. Higher adherence was generally noted for S. constellatus and S. intermedius isolates. No differences in adherence were noted between commensal and pathogenic strains to decorin or biglycan. DS demonstrated greater adherence compared to C4S. Removal of the glycosaminoglycan chains with chondroitinase ABC resulted in no or minimal adherence for all isolates. These results suggest that SAGs bind to the extracellular matrix proteoglycans decorin and biglycan, with interaction mediated by the conjugated glycosaminoglycan chain.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Subjects: R Medicine > RK Dentistry
Uncontrolled Keywords: Streptococcus anginosus group; Decorin; Biglycan; Dermatan sulphate; Chondroitin 4-sulphate; Surface plasmon resonance
Publisher: Elsevier
ISSN: 0923-2508
Date of First Compliant Deposit: 30 March 2016
Last Modified: 10 Mar 2019 10:24
URI: http://orca.cf.ac.uk/id/eprint/36036

Citation Data

Cited 4 times in Google Scholar. View in Google Scholar

Cited 5 times in Scopus. View in Scopus. Powered By Scopus® Data

Cited 4 times in Web of Science. View in Web of Science.

Actions (repository staff only)

Edit Item Edit Item

Downloads

Downloads per month over past year

View more statistics