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Infection and Immunity, June 2003, p. 3652-3656, Vol. 71, No. 6
0019-9567/03/$08.00+0 DOI: 10.1128/IAI.71.6.3652-3656.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Department of Oral Biology, Hebrew University-Hadassah Faculty of Dental Medicine, Jerusalem, Israel
Received 6 February 2003/ Returned for modification 25 February 2003/ Accepted 24 March 2003
Purified Actinobacillus actinomycetemcomitans serotype b lipopolysaccharide (LPS) was found to be able to bind Fusobacterium nucleatum cells and to inhibit binding of F. nucleatum to A. actinomycetemcomitans serotype b. Sugar binding studies showed that the requirements for binding of A. actinomycetemcomitans serotype b LPS to the F. nucleatum lectin are the presence of a metal divalent ion, an axial free hydroxyl group at position 4, and free equatorial hydroxyl groups at positions 3 and 6 of D-galactose, indicating that the ß-N-acetyl-D-galactosamine in the serotype b LPS trisaccharide repeating unit is the monosaccharide residue recognized by the F. nucleatum lectin. These data strongly suggest that A. actinomycetemcomitans serotype b LPS is one of the receptors responsible for the lactose-inhibitable coaggregation of A. actinomycetemcomitans to fusobacteria.
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