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Infection and Immunity, September 2002, p. 5279-5282, Vol. 70, No. 9
0019-9567/02/$04.00+0 DOI: 10.1128/IAI.70.9.5279-5282.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Department of Preventive Dentistry, Kyushu University Faculty of Dental Science, Fukuoka 812-8582, Japan
Received 28 January 2002/ Returned for modification 9 April 2002/ Accepted 6 June 2002
The bovine lactoferrin molecule and relatively long lactoferrin fragments containing residues 473 to 538 strongly inhibited adherence of Streptococcus mutans to saliva-coated hydroxyapatite beads. Each cysteine residue in Lf411 (residues 473 to 538) was replaced by a serine residue, and the mutants Lf411-C481S and Lf411-C532S strongly inhibited S. mutans adherence. These results suggest that the functional domain of lactoferrin that binds to a salivary film lies in residues 473 to 538 and that the region might be concealed by disulfide bond formation between Cys481 and Cys532 in the Lf411 fragment.
This paper is dedicated to the memory of Toshihiko Koga.
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