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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
Immune adherence and staphylococcus protein A binding of soluble immune complexes produced by complement activation
Clinical and Experimental Immunology
|December 1, 1983
Summary
Complement influences antigen-antibody complex solubility and biological activity through classical and alternative pathways. Complement-reacted complexes bind to erythrocytes and staphylococcus protein A, with solubilized complexes showing greater immune adherence.
Area of Science:
- Immunology
- Biochemistry
- Complement System
Background:
- The complement system modulates antigen-antibody complex (IC) solubility via classical and alternative pathways.
- Classical pathway inhibits precipitate formation; alternative pathway solubilizes formed precipitates.
- Biological properties of complement-reacted ICs are not fully understood.
Purpose of the Study:
- To assess the biological properties of complement-reacted immune complexes (IC).
- To investigate the binding of ICs to staphylococcus protein A (SPA) and human erythrocytes.
- To determine how complement influences IC behavior and immune adherence.
Main Methods:
- Generated antigen-antibody complexes using BSA-anti-BSA.
- Reacted complexes with complement in normal and factor D-depleted human serum.
- Assessed binding of complement-reacted ICs to staphylococcus protein A (SPA) and human erythrocytes.
Main Results:
- Complement-reacted ICs bound to both human erythrocytes and SPA.
- ICs generated by solubilization showed greater immune adherence than those kept in solution.
- ICs in factor D-depleted serum exhibited enhanced erythrocyte binding compared to normal serum.
Conclusions:
- Complement-reacted immune complexes are not biologically inert.
- Complement function significantly impacts the properties and biological activity of ICs.
- Factors affecting complement pathways influence IC behavior, particularly immune adherence.
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