Journal article
Lactoferrin inhibits Porphyromonas gingivalis proteinases and has sustained biofilm inhibitory activity
SG Dashper, Y Pan, PD Veith, YY Chen, ECY Toh, SW Liu, KJ Cross, EC Reynolds
Antimicrobial Agents and Chemotherapy | Published : 2012
DOI: 10.1128/AAC.05100-11
Abstract
Porphyromonas gingivalis is a bacterial pathogen associated with chronic periodontitis that results in destruction of the tooth's supporting tissues. The major virulence determinants of P. gingivalis are its cell surface Arg- and Lys-specific cysteine proteinases, RgpA/B and Kgp. Lactoferrin (LF), an 80-kDa iron-binding glycoprotein found in saliva and gingival crevicular fluid, is believed to play an important role in innate immunity. In this study, bovine milk LF displayed proteinase inhibitory activity against P. gingivalis whole cells, significantly inhibiting both Arg- and Lys-specific proteolytic activities. LF inhibited the Arg-specific activity of purified RgpB, which lacks adhesin d..
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Funding Acknowledgements
This project was supported by MG Nutritionals, Murray Goulburn Co-operative Ltd., Victoria, Australia.