Effect of specific binding of human albumin, fibrinogen, and immunoglobulin G on surface characteristics of bacterial strains as revealed by partition experiments in polymer phase systems.
Four strains of gram-positive cocci with different combinations of positive binding of human proteins were investigated with respect to changes in physicochemical surface properties after specific protein binding. Staphylococcus aureus Cowan I, two group A beta-hemolytic streptococci, and one group G streptococcal strain were studied; they represented three different combinations of reactivity for human serum albumin, human immunoglobulin G, and fibrinogen. Using single-tube partition of bacterial cells in a dextran-polyethylene glycol system of constant polymer concentration but varying ionic compositions, it was possible to detect changes in the partition of bacteria after specific protein binding. There was a correlation between the binding of radiolabled human proteins to the bacterial strains and the effect of human proteins on the partition of the bacteria in the phase systems. Thus, the specific binding of proteins to the bacteria changes their physicochemical surface properties. These types of bacteria-protein interactions may play an important role in modulating host-parasite relationships.
D000818:Animals; D001665:Binding Sites; D001666:Binding Sites, Antibody; D001769:Blood; D002417:Cattle; D005340:Fibrinogen / Q000494:pharmacology*; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D011108:Polymers; D012709:Serum Albumin / Q000494:pharmacology*; D013211:Staphylococcus aureus / Q000502:physiology; D013291:Streptococcus / Q000502:physiology; D013499:Surface Properties
D007074:Immunoglobulin G; D011108:Polymers; D012709:Serum Albumin; D005340:Fibrinogen