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Science 11 February 1994: Vol. 263. no. 5148, pp. 814 - 817 DOI: 10.1126/science.8303299
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Articles
Science, Vol 263, Issue 5148, 814-817
Copyright © 1994 by American Association for the Advancement of Science
Mapping the lectin-like activity of tumor necrosis factor
R Lucas,
S Magez,
R De Leys,
L Fransen,
JP Scheerlinck,
M Rampelberg,
E Sablon,
and
P De Baetselier
Laboratory of Cellular Immunology, University of Brussels, Sint-Genesius-Rode, Belgium.
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.
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