Interactions of Streptococcus mutans Glucosyltransferase B with Lysozyme in Solution and on the Surface of HydroxyapatiteKho H.-S. · Vacca Smith A.M. · Koo H. · Scott-Anne K. · Bowen W.H.
University of Rochester, Center for Oral Biology, Rochester, New York, N.Y., USA
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.
Dr. Hong-Seop Kho
Department of Oral Medicine and Oral Diagnosis
College of Dentistry, Seoul National University
28-22 Yunkeun-Dong, Chongro-Ku, Seoul 110-744 (Korea)
Tel. +82 2 7602611, 3989, Fax +82 2 7449135, E-Mail email@example.com
Received: May 7, 2004
Accepted after revision: December 9, 2004
Number of Print Pages : 6
Number of Figures : 4, Number of Tables : 0, Number of References : 35
Vol. 39, No. 5, Year 2005 (Cover Date: September-October 2005)
Journal Editor: Shellis, R.P.(Bristol)
ISSN: 0008–6568 (print), 1421–976X (Online)
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