Mapping of the lectin-like activity of tumor necrosis factor

Rudolf Lucas, Stefan Magez, Robert De Leys, Lucie Fransen, Jean-Pierre Scheerlinck, Murielle Rampelberg, Erwin Sablon, Patrick De Baetselier

Research output: Contribution to journalArticle

165 Citations (Scopus)


Tumor necrosis factor (TNF), but not lymphotoxin (LT), is directly trypanolytic for salivarian trypanosomes. This activity was not blocked by soluble 55-kilodalton and 75-kilodalton TNF receptors, but was potently inhibited by N,N'-diacetylchitobiose, an oligosaccharide that binds TNF. Comparative sequence analysis of TNF and LT localized the trypanocidal region, and synthetic peptides were trypanolytic. TNF molecules in which the trypanocidal region was mutated or deleted retained tumoricidal activity. Thus, trypanosome-TNF interactions occur via a TNF domain, probably with lectin-like affinity, which is functionally and spatially distinct from the mammalian TNF receptor binding sites.
Original languageEnglish
Pages (from-to)814-817
Publication statusPublished - 1994

Bibliographical note

Science, 263, 814-817

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