Actinobacillus actinomycetemcomitans Serotype b Lipopolysaccharide Mediates Coaggregation with Fusobacterium nucleatum

Autor: Graciela Rosen, Monica Helcer, M. N. Sela, Ira Nisimov
Rok vydání: 2003
Předmět:
Zdroj: Infection and Immunity. 71:3652-3656
ISSN: 1098-5522
0019-9567
DOI: 10.1128/iai.71.6.3652-3656.2003
Popis: 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 β- 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.
Databáze: OpenAIRE