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Interactions of Streptococcus mutans glucosyltransferase B with lysozyme in solution and on the surface of hydroxyapatite

Cited 10 time in Web of Science Cited 9 time in Scopus
Authors
Kho, H.-S.; Vacca Smith, A.M.; Koo, H; Scott-Anne, K; Bowen, W.H
Issue Date
2005
Publisher
Karger
Citation
Caries Research 2005;39:411-416
Keywords
glucosyltransferase Blysozymeglucansaliva
Abstract
Several active enzymes have been identified as components of acquired enamel pellicle. In the present study, the interactions of Streptococcus mutans glucosyltransferase B (GtfB) with lysozyme in solution and on the surface of hydroxyapatite (HA) beads were studied. Experiments were also performed to investigate whether structural differences exist between glucans formed by GtfB enzyme in the presence or absence of lysozyme in solution and on the surface of HA. Hen egg-white lysozyme (HEWL) and saliva were used as the sources of lysozyme; lysozyme-depleted saliva was used as control. Lysozyme activity was significantly reduced when adsorbed onto HA beads compared with that in solution. The GtfB enzyme did not affect the activity of lysozyme in solution or that of adsorbed lysozyme onto HA. The presence of HEWL increased GtfB activity; bovine serum albumin had an even greater enhancing effect. Depletion of lysozyme from whole saliva increased GtfB activity in solution, but not on the surface of saliva-coated HA. The presence of lysozyme affected the amount of glucan formation by GtfB, but not the structure of glucans formed in solution and on the surface. Therefore, the interaction of lysozyme and GtfB enzymes on HA surface may modulate the formation of glucan and dental plaque.
ISSN
0008-6568
Language
English
URI
https://hdl.handle.net/10371/69671
DOI
https://doi.org/10.1159/000086849
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College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
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