C8 binding protein bears I antigenic determinants
P Blaas-Mautner1, S Filsinger, B Berger
1Institut für Immunologie der Universität Heidelberg, Federal Republic of Germany.
Insights
The I antigen, a sugar sequence on red blood cells, is linked to C8 binding protein (C8bp). Removing the I antigen does not affect C8bp
Area of Science:
- Immunology
- Glycobiology
- Complement System
Background:
- C8 binding protein (C8bp) is a membrane glycoprotein on blood cells.
- C8bp inhibits C5b-9-mediated lysis in homologous systems.
- The I antigenic determinant is a sugar sequence found on adult human erythrocytes.
Purpose of the Study:
- To analyze the carbohydrate portion of C8bp.
- To determine if the I antigenic determinant is essential for C8bp function.
- To investigate the role of I antigen in homologous species restriction.
Main Methods:
- Analysis of the carbohydrate structure of C8bp.
- Enzymatic cleavage of the I antigenic determinant from C8bp using endo-beta-galactosidase (E.C. 3.2.2.103).
- Treatment of intact erythrocytes with endo-beta-galactosidase.
Main Results:
- C8bp was found to be associated with the I antigenic determinant.
- Enzyme treatment removed the I antigen from C8bp without affecting its inhibitory function.
- Treatment of erythrocytes removed I antigen but did not abolish resistance to homologous C5b-9 lysis.
Conclusions:
- The I antigen is associated with C8bp.
- The presence of the I antigen is not required for the homologous species restriction mediated by C8bp.
Abstract:
C8 binding protein (C8bp) is an integral membrane glycoprotein of peripheral blood cells, which inhibits the C5b-9-mediated lysis in a homologous system. In the present study, we analyzed the carbohydrate portion of the C8bp. We found that C8bp is associated with I antigenic determinant, a sugar sequence found on human erythrocytes of adults. To assess whether or not the sugar residues are essential for the C8bp function, I determinant was cleaved off from the isolated C8bp by endo-beta-galactosidase (E.C. 3.2.2.103) that hydrolyses internal beta-galactosidic-linked-N-acetyllactosamine residues. Enzyme treatment removed I-antigen, the inhibitory function of C8bp, however, was not affected. When intact erythrocytes were treated with endo-beta-galactosidase, I-antigen was lost and the lytic insusceptibility of human erythrocytes to homologous C5b-9 could not be abolished. Thus, I-antigen is associated with the C8bp, but its presence is not required for the homologous species restriction.
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