Premium
Streptavidin‐induced lysis of homologous biotinylated erythrocytes Evidence against the key role of the avidin charge in complement activation via the alternative pathway
Author(s) -
Muzykantov Vladimir R.,
Smirnov Michael D.,
Samokhin Gennady P.
Publication year - 1991
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(91)80216-p
Subject(s) - biotinylation , avidin , streptavidin , lysis , hemolysis , biotin , chemistry , biochemistry , microbiology and biotechnology , biology , biophysics , immunology
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.