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Avidin attachment to biotinylated amino groups of the erythrocyte membrane eliminates homologous restriction of both classical and alternative pathways of the complement
Author(s) -
Muzykantov Vladimir R.,
Smirnov Mikhail D.,
Klibanov Alexander L.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80002-c
Subject(s) - avidin , biotinylation , lysis , biotin , heterologous , classical complement pathway , biology , biochemistry , decay accelerating factor , microbiology and biotechnology , antibody , complement system , homologous chromosome , chemistry , immunology , gene
Lysis of avidin‐coated biotinylated sheep red blood cells (RBC) via the classical pathway of homologous (sheep) and heterologous (guinea pig) complement has been studied. The minimal surface density of avidin inducing antibody‐dependent lysis via the classical pathway is smaller than that inducing antibody‐independent lysis via the alternative pathway. Heterologous lysis via the classical pathway does not depend on the mode of avidin attachment: both biotinylation of membrane amino groups and insertion of biotinyl‐lipid into the membrane provide the same lysis of avidin‐coated RBCs by guinea pig serum in the presence of anti‐avidin antibody. Avidin‐free sheep RBC sensitized with hemolytic anti‐RBC antibody were lysed by guinea pig, but not by sheep serum, confirming high efficiency of homologous restriction of the complement. However, avidin‐coated RBCs were lysed by homologous serum in the presence of anti‐avidin antibody at low surface density of avidin attached. The elimination of the homologous restriction depends on the mode of avidin attachment: biotinylation of membrane amino groups provides antibodymediated lysis via the classical pathway of homologous complement, while insertion of biotinyl‐lipid does not provide lysis.