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Bradley L. Buster, Kirsten A. Mattes, W. Michael Scheld, Monoclonal Antibody-Mediated, Complement-Independent Binding of Human Tumor Necrosis Factor-α to Primate Erythrocytes via Complement Receptor 1, The Journal of Infectious Diseases, Volume 176, Issue 4, October 1997, Pages 1041–1046, https://doi.org/10.1086/516536
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Abstract
Monoclonal antibody (MAb)-based heteropolymers (HP) were used to simulate immune adherence. The HP is constructed by cross-linking MAbs that recognize complement receptor 1 (CR1) and tumor necrosis factor-α (TNF-α). 125I-labeled TNF-α was cocultured with either sheep, monkey, or human erythrocytes in the presence or absence of HP. Human erythrocytes demonstrated 63% ± 0 (mean ± SD) binding of 125I-labeled TNF-α, while binding of 125I-labeled TNF-α in the absence of HP was 4% ± 1% (P < .001). Monkey erythrocytes showed similar results, while sheep erythrocytes (which lack CR1) demonstrated low binding. The effect of HP binding on biologic activity of TNF-α was examined in an assay of stimulated human neutrophils. The HP completely inhibited the ability of TNF-α to prime neutrophils, occurring regardless of the presence or absence of erythrocytes but solely dependent on the addition of HP. Thus, the HP facilitated specific, saturable, and significant binding of 125I-labeled TNF-α to primate erythrocytes in vitro.
