|Title||Mapping the lectin-like activity of tumor necrosis factor.|
|Publication Type||Journal Article|
|Year of Publication||1994|
|Authors||Lucas, R., S. Magez, R. De Leys, L. Fransen, J. P. Scheerlinck, M. Rampelberg, E. Sablon, and P. De Baetselier|
|Date Published||1994 Feb 11|
|Keywords||Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Disaccharides, Glucans, L Cells (Cell Line), Lectins, Lymphotoxin-alpha, Mice, Molecular Sequence Data, Mutation, Peptide Fragments, Receptors, Tumor Necrosis Factor, Trypanosoma brucei brucei, Tumor Necrosis Factor-alpha|
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.