Wheat germ agglutinin activates human T lymphocytes by stimulation of phosphoinositide hydrolysis

H. C. Clevers, A. de Bresser, H. Kleinveld, F. H. Gmelig-Meyling, R. E. Ballieux

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14 Citations (Scopus)


Recently, it has become evident that stimulated phosphoinositide (PI) hydrolysis plays a crucial role in early T lymphocyte activation. We have investigated the effects of the nonmitogenic lectin wheat germ agglutinin (WGA) on several parameters associated with PI hydrolysis in human T cells. It was found that WGA was as effective as anti-T3 antibody and PHA in producing a rise in cytosolic free Ca++ ((Ca++)(i)) in blood T cells and in cells of the T cell line CCRF-CEM. It was inferred that identical cells within the blood T cell preparation responded to each of the three agents, refuting the contention that WGA only stimulated a subfraction of circulating mature T lymphocytes. WGA-induced, but not PHA-induced rise in (Ca++)(i) could be blocked completely by N-acetyl-D-glucosamine, demonstrating that the sugar-binding characteristics of the lectin dictate its action on T lymphocytes. Anti-T3 antibody, PHA, and WGA all initiated inositol phosphate formation in blood T cells, indicating that each of the agents stimulated PI hydrolysis. The combination of WGA with nonmitogenic amounts of phorbol-12-myristate-13-acetate resulted in strong mitogenicity. It is concluded that WGA, like anti-T3 antibody and PHA, is a pan-T activator of PI hydrolysis.

Original languageEnglish
Pages (from-to)3180-3183
Number of pages4
JournalJournal of Immunology
Issue number9
Publication statusPublished - 1986
Externally publishedYes


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