TY - JOUR
T1 - Mapping the lectin-like activity of tumor necrosis factor
AU - Lucas, Rudolf
AU - Magez, Stefan
AU - De Leys, Robert
AU - Fransen, Lucie
AU - Scheerlinck, Jean Pierre
AU - Rampelberg, Murielle
AU - Sablon, Erwin
AU - De Baetselier, Patrick
PY - 1994/2/11
Y1 - 1994/2/11
N2 - 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.
AB - 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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U2 - 10.1126/science.8303299
DO - 10.1126/science.8303299
M3 - Article
C2 - 8303299
AN - SCOPUS:0028218545
SN - 0036-8075
VL - 263
SP - 814
EP - 817
JO - Science
JF - Science
IS - 5148
ER -