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Specific inhibition of OKT8 binding to peripheral blood mononuclear cells by jacalin
C R Gattass1, I Ghobrial, M M Bunn-Moreno
1Institute of Biophysics, Federal University of Rio de Janeiro, Brasil.
Human T-specific monoclonal antibodies were used to study the interactions between the binding of jacalin to peripheral blood mononuclear cells (PBMC) and the immunoregulatory molecules displayed at the surface of T cells. Jacalin inhibits the binding of OKT8 (anti-CD8) to both fresh PBMC and jacalin-induced T cell blasts. In both cases the binding of anti-CD3 (OKT3) or anti-CD4 (OKT4) was not affected by the lectin. The effect of jacalin on OKT8 binding is abolished by 1-O-alpha-D-methylgalactopyranoside, suggesting its mediation by the lectin saccharide combining sites. Preincubation experiments indicated that the inhibitory effect of jacalin is due to a competition between the lectin and the monoclonal antibody. The effect of the lectin could also be reversed by increasing concentrations of the monoclonal antibody. Taken together this data demonstrates a specific inhibition of OKT8 (anti-CD8) binding by jacalin. This effect is mediated by the binding of the lectin to structures on the cell surface, perhaps the CD8 antigen. The data also points to the discovery of a new mitogen that could be useful for studying the physiological role of CD8 on T cell responses.
Human T-specific monoclonal antibodies were used to study the interactions between the binding of jacalin to peripheral blood mononuclear cells (PBMC) and the immunoregulatory molecules displayed at the surface of T cells. Jacalin inhibits the binding of OKT8 (anti-CD8) to both fresh PBMC and jacalin-induced T cell blasts. In both cases the binding of anti-CD3 (OKT3) or anti-CD4 (OKT4) was not affected by the lectin. The effect of jacalin on OKT8 binding is abolished by 1-O-alpha-D-methylgalactopyranoside, suggesting its mediation by the lectin saccharide combining sites. Preincubation experiments indicated that the inhibitory effect of jacalin is due to a competition between the lectin and the monoclonal antibody. The effect of the lectin could also be reversed by increasing concentrations of the monoclonal antibody. Taken together this data demonstrates a specific inhibition of OKT8 (anti-CD8) binding by jacalin. This effect is mediated by the binding of the lectin to structures on the cell surface, perhaps the CD8 antigen. The data also points to the discovery of a new mitogen that could be useful for studying the physiological role of CD8 on T cell responses.