Purification of 1F5 antigen that prevents complement attack on homologous cell membranes.
A mAb, 1F5, has the ability to cause hemolysis by human serum of human E treated with neuraminidase via the alternative C pathway. By Western blotting, this mAb reacts with a glycoprotein having a molecular mass of 20 kDa (1F5Ag). 1F5Ag was isolated from human E by affinity chromatography with mAb-coupled Sepharose. Purified 1F5Ag was then adsorbed to guinea pig E rendering them resistant to human C attack by both the classical and the alternative pathways. Furthermore, experiments with isolated C components revealed that 1F5Ag interferes with both homologous human C8 and C9 in the terminal stage of the C reaction, whereas it has little effect on hemolysis by rabbit C8 and C9. Therefore, 1F5Ag can be called HRF20, which stands for homologous restriction factor of 20 kDa.
Harada
R
R
Department of Microbiology, Fukuoka University School of Medicine, Japan.
Okada
N
N
Fujita
T
T
Okada
H
H
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000954:Antigens, Surface / Q000302:isolation & purification* / Q000502:physiology; D003167:Complement Activation; D003185:Complement C8 / Q000502:physiology; D003186:Complement C9 / Q000502:physiology; D004912:Erythrocytes / Q000032:analysis / Q000276:immunology*; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006461:Hemolysis; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D003185:Complement C8; D003186:Complement C9; D006026:Glycoside Hydrolases