Streptavidin‐induced lysis of homologous biotinylated erythrocytes Evidence against the key role of the avidin charge in complement activation via the alternative pathway

FEBS Letters

Smirnov, Michael D.¹  Samokhin, Gennady P.¹  Muzykantov, Vladimir R.¹ 

[1] Institute of Experimental Cardiology, USSR Cardiology Research Center, Moscow, USSR

关键词: Complement;    Avidin-biotin interaction;    Membrane modification;    APC;    alternative pathway of complement;    PBS;    phosphate-buffered saline;    VBS;    veronal-buffered saline;    DAF;    decay accelerating factor;    CR1;    complement receptor type 1;    HRF;    homologous restriction factor;    EA;    sheep erythrocytes sensitized by hemolytic antibody;   

DOI  :  10.1016/0014-5793(91)80216-P

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It is shown that non-covalent attachment of streptavidin, as well as of avidin, to biotinylated human erythrocytes induces homologous hemolysis by complement. Rabbit antiserum against human C3 is found to inhibit the lysis specifically as compared with non-immune rabbit serum. Efficiency of lysis inhibition is greater for avidin- and streptavidin-induced lysis of biotinylated human erythrocytes than for antibody-sentitized sheep erythrocytes. In contrast to positively charged avidin (pI II), streptavidin is a neutral protein. Hence, hemolysis of streptavidin-carrying erythrocytes is inconsistent with the suggestion on the crucial role of avidin charge in lysis. Membrane alterations (cross-linking and clusterization of biotinylated components) induced by avidin (streptavidin) seem to be a more plausible explanation for the lysis.

【 授权许可】

Unknown