Reduction of phagocytosis, surface hydrophobicity and charge of Salmonella typhimurium 395 MR10 by reaction with secretory IgA (SIgA).
Binding of human colostral secretory IgA (SIgA) to Salmonella typhimurium 395 MR10 decreased the liability to hydrophobic interaction of the bacteria, as analysed by hydrophobic interaction chromatography on Octyl-Sepharose and partition in an aqueous polymer two-phase system consisting of dextran, poly(ethyleneglycol) (PEG) and poly-(ethyleneglycol)-palmitate (P--PEG). SIgA also reduced the negative charge of the bacteria. Treatment of the bacteria with centrifuged but not further fractionated colostrum added positive charge to the bacteria which was removed by treatment with pepsin. Colostral SIgA reduced the in vitro phagocytosis of S. typhimurium MR10 by polymorphonuclear leucocytes. The adhesion of the bacteria to cellulose membrane filters in the absence of phagocytes was also reduced after the interaction with SIgA. It is proposed that the binding of SIgA to bacterial surfaces has hydrophilic and anti-adhesive effects, which may serve to exclude antigen from mucosal surfaces.
D002462:Cell Membrane / Q000502:physiology; D002847:Chromatography, Agarose; D003126:Colostrum / Q000276:immunology; D007070:Immunoglobulin A / Q000276:immunology*; D007071:Immunoglobulin A, Secretory / Q000276:immunology*; D009504:Neutrophils / Q000276:immunology; D010587:Phagocytosis; D012486:Salmonella typhimurium / Q000276:immunology*; D013499:Surface Properties
D007070:Immunoglobulin A; D007071:Immunoglobulin A, Secretory