title: Sialic acid as receptor of Bacteroides fragilis lectin-like adhesin.
abstract: It was observed that sialic acid and macromolecules rich in this sugar were able to inhibit the hemagglutination activity (HA) of Bacteroides fragilis strains in low concentrations. Reversion of the HA and also of the adsorption to beads of Sepharose coupled to bovine submaxillary mucin, by this sugar residue corroborated the recognition capacity of the bacterial lectin-like adhesin. However, when erythrocytes were treated with clostridial neuraminidase, an increase in the HA of some strains was observed. Protease treatment of erythrocytes abolished the HA, indicating that cell receptors of B. fragilis are probably a glycoprotein moiety.
authors: Instituto de Microbiologia, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Ilha do Fundão, Brasil.
authors: R M
authors: RM
authors: Domingues
authors: S M
authors: SM
authors: Cavalcanti
authors: A F
authors: AF
authors: Andrade
authors: M C
authors: MC
authors: Ferreira
mesh_terms: D018829:Adhesins, Bacterial; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism*; D001441:Bacteroides fragilis / Q000378:metabolism*; D006388:Hemagglutinins / Q000378:metabolism; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000494:pharmacology; D011975:Receptors, Mitogen / Q000187:drug effects / Q000378:metabolism*; D012794:Sialic Acids / Q000032:analysis* / Q000378:metabolism
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D006388:Hemagglutinins; D011975:Receptors, Mitogen; D012794:Sialic Acids; C063910:adhesin, Bacteroides; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid