THE POLYCLONAL ACTIVATION OF LYMPHOCYTES AND T-CELL MITOGENICITY BY A UNIQUE SIALIC-ACID-BINDING LECTIN FROM THE HEMOLYMPH OF ACHATINA-FULICA SNAIL

A unique sialic-acid-binding lectin, AchatininH, isolated from the hemolymph of Achatina fulica snail was found to be strongly mitogenic, as monitored by [3H]thymidine incorporation assay, to rat and human lymphocytes. However, the degree of mitogenic response varied with the type of cell population. As indicated, this lectin induced proliferation of purified T lymphocytes and rat thymocytes, whereas it was less mitogenic towards peripheral lymphocytes of pregnant rats and was not mitogenic towards B lymphocytes. Furthermore, the mitogenic response was inhibited by the sialic-acid-containing disaccharide, a strong inhibitor of this lectin. This suggests that lymphocyte cell surface molecules containing sialic acid residues are important for this interaction and may have a structure similar to that of AchatininH receptors. Although this lectin showed strong mitogenicity towards lymphocytes, it showed very weak leucoagglutination. Surprisingly, PHA-induced blastogenesis was inhibited by the same dose of AchatininH as caused mitogenic activity in resting lymphocyte culture. The degree of suppression was higher for the lymphocytes isolated from pregnant rat blood compared to the non-pregnant control. Since the 51Cr-uptake assay and the cell viability test results negate the potential cytotoxic activity of this protein, the immunosuppression induced in the presence of PHA by AchatininH may be the additive effect of two mitogens causing an increased cell-density-dependent arrest. AchatininH does not have complement-like activity, but induces potent polyclonal activation of B cells as measured by the reverse hemolytic plaque assay. © 1990.