Carbohydrate exposure on salmonella and E. coli bacteria after reaction with antibody IgG and secretory IgA (SIgA) assessed with fluorescent lectins.

The carbohydrate moieties exposed on enterobacteria before and after antibody binding have been tested with fluorescent lectins. Salmonella typhimurium 395 MS (S-type) and its Rd-mutant MR10 were coated with hyperimmune anti-MS and anti-MR 10 IgG, respectively. MR 10 bacteria and Escherichia coli O86 bacteria were coated with human colostral secretory IgA (SIgA). There was a conspicuous binding of some of the lectins to untreated bacteria not always closely related to the sugar composition of the outer membrane lipopolysaccharide (LPS) or other known sugar residues. Antibody IgG and SIgA binding modified the affinity for the lectins. The binding of some lectins was reduced, presumably by masking the bacterial sugars. Antibody IgG binding to S. typhimurium MS and R 10 enhanced the affinity for RCA-I (Gal) and to a smaller extent for WGA (GlcNAc) which may be explained by exposure of IgG oligosaccharide. Antibody SIgA binding to S. typhimurium R 10 and E. coli O86 enhanced the affinity for the above lectins to a larger extent as well as for Con A (Man, Glc). The corresponding sugars N-acetylglucosamine, mannose and glucose are present in the carbohydrate chain of the secretory component as well as in IgA indicating that when SIgA antibody binds its sugar components are exposed.