Avidin attachment to biotinylated erythrocytes induces homologous lysis via
the alternative pathway of complement
VR Muzykantov, MD Smirnov and GP Samokhin
Institute of Experimental Cardiology, USSR Cardiology Research Center,
Moscow.
Noncovalent attachment of avidin to the membrane of prebiotinylated red
blood cells (RBCs) induces lysis via the alternative pathway of complement
(APC). Lysis is not species-dependent; RBCs from humans, rabbits, rats, and
sheep were lysed with both autologous and all heterologous sera. Both
biotinylated and native cells were not lysed. Lysis was observed at an
avidin surface density of about 10(5) molecules per cell. Acylation of
avidin prevents lysis and decreases the positive charge of the avidin.
Lysis depends on the length of the cross-linking agent used for the biotin
attachment to the membrane. An increase in the length of the cross-linking
agent was accompanied by an enhancement of the lysis and the agglutination
titer of biotinylated RBCs in a solution of avidin. It is suggested that
avidin attachment induces some transformations of the cell membrane that
lead to the conversion from "APC nonactivator" cells to "APC activator"
cells. The interaction of avidin with membrane APC-restrictors
(decay-accelerating factors, type 1 receptor for complement, homologous
restriction factor, and others), the charge of avidin, and its
cross-linking ability in lysis are discussed. It is proposed that membrane
rearrangement induced by multipoint avidin attachment to biotinylated
membrane is the main reason for avidin-induced elimination of APC
restriction.
Volume 78,
Issue 10,
pp. 2611-2618,
11/15/1991
Copyright © 1991 by The American Society of Hematology
