International Immunology · 1989 · 201 citations · 0 references
Life SciencesBiochemistryImmunologyInnate ImmunityMembrane BiochemistryMonoclonal AntibodiesAntibody CharacterizationAntibody-antigen RecognitionComplement RegulationComplement SystemProtein BindingCell Membrane BindingCell Membrane PhysiologyComplement-binding AntibodiesComplement-mediated Cell LysisComplement-targeted Monoclonal AntibodiesMonoclonal Antibody RecognitionTerminal Complement Pathway Inhibition
Neuraminidase-treated human erythrocytes become sensitive to haemolysis by heterologous serum via activation of the alternative complement pathway (ACP), while remaining insensitive to homologous serum because of the presence of inhibitors on the cell membrane. We obtained a monoclonal antibody which renders the neuraminidase-treated erythrocytes sensitive to haemolysis by homologous human serum via the ACP. This antibody reacts with a 20 KDa membrane glycoprotein which interferes with the terminal stage of complement action on cell membranes. The 20 KDa protein is anchored to the membrane via phosphatidylinositol.