On the physical-chemical effect of colostral antibody binding to Escherichia coli O 86.
Sensitization of Escherichia coli O 86 with colostrum or purified colostral sIgA antibody produces a physical-chemical change of the bacterial surface detectable as a change in partition in dextran-polyethylene glycol polymer two-phase systems. Sensitization with colostrum or sIgA reduces affinity for the dextran-rich phase. In contrast immune serum, IgG and complement increase the affinity for that phase. The results are compatible with the hypothesis that hydrophilic particles, e.g. certain strains of bacteria, are less liable to attachment to and phagocytosis by animal cells than hydrophobic particles, e.g. other bacterial strains. Sensitization with secretory IgA enhances the hydrophilicity thereby making possible an escape mechanism operating at the mucosal surfaces.
D000017:ABO Blood-Group System; D000906:Antibodies / Q000302:isolation & purification; D001666:Binding Sites, Antibody; D055598:Chemical Phenomena; D002621:Chemistry; D003126:Colostrum / Q000276:immunology; D003911:Dextrans; D004912:Erythrocytes / Q000276:immunology; D004926:Escherichia coli / Q000276:immunology*; D006801:Humans; D007070:Immunoglobulin A; D007071:Immunoglobulin A, Secretory; D010587:Phagocytosis; D011092:Polyethylene Glycols
D000017:ABO Blood-Group System; D000906:Antibodies; D003911:Dextrans; D007070:Immunoglobulin A; D007071:Immunoglobulin A, Secretory; D011092:Polyethylene Glycols