Bacterial lectins, cell-cell recognition and infectious disease.
Numerous bacterial strains produce surface lectins, commonly in the form of fimbriae that are filamentous assemblies of protein subunits. Among the best characterized of these are the type 1 (mannose specific) fimbrial lectins of Escherichia coli that consist almost exclusively of one class of subunit with a molecular mass of 17 kDa. They possess an extended combining site corresponding to a trisaccharide and preferentially bind carbohydrate units of oligomannose or hybrid type. Type 1 fimbriae also possess a hydrophobic region close to the carbohydrate-binding site, since aromatic alpha-mannosides inhibit strongly (up to 1000-times more than methyl alpha-mannoside) the agglutination of yeasts by the bacteria and the adherence of the latter to pig ileal epithelial cells. The combining sites of type 1 fimbriae of the salmonellae and of other enteric bacteria are different from those of E. coli in that they are smaller and do not possess a hydrophobic region. The various bacterial surface lectins appear to function primarily in the initiation of infection by mediating bacterial adherence to epithelial cells, e.g. in the urinary and gastrointestinal tracts. The mannose specific lectins also act as recognition molecules in lectinophagocytosis (i.e. phagocytosis of the bacteria in the absence of opsonins) by mouse, rat and human peritoneal macrophages, and human polymorphonuclear leukocytes. Affinity chromatography of membrane lysates from human polymorphonuclear leukocytes on immobilized type 1 fimbrial lectin, using methyl alpha-mannoside as eluent, showed that glycoproteins with apparent molecular masses of 70-80, 100 and 150 kDa act as receptors for the bacteria. Inhibition experiments with monoclonal antibodies suggest that the glycoprotein bands of 100 and 150 kDa may be identical with the alpha and beta subunits of leukocyte complement receptors and adhesion glycoproteins involved in complement-mediated opsonophagocytosis. The systems described serve as a fine illustration for the biological role of lectin-carbohydrate interactions. Further studies of these systems will lead to a deeper understanding of the molecular basis of infectious diseases, and perhaps also to new approaches for their prevention.
D000818:Animals; D001424:Bacterial Infections / Q000503:physiopathology*; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000494:pharmacology; D002448:Cell Adhesion; D004848:Epithelium / Q000502:physiology; D004926:Escherichia coli / Q000502:physiology; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000502:physiology*; D005786:Gene Expression Regulation; D006384:Hemagglutination; D006801:Humans; D037102:Lectins / Q000037:antagonists & inhibitors / Q000502:physiology*; D008264:Macrophages / Q000378:metabolism; D010587:Phagocytosis; D011975:Receptors, Mitogen / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002241:Carbohydrates; D037102:Lectins; D011975:Receptors, Mitogen; C063055:fimbrillin; D036781:Fimbriae Proteins