Mapping the lectin-like activity of tumor necrosis factor.

TitleMapping the lectin-like activity of tumor necrosis factor.
Publication TypeJournal Article
Year of Publication1994
AuthorsLucas, R., S. Magez, R. De Leys, L. Fransen, J. P. Scheerlinck, M. Rampelberg, E. Sablon, and P. De Baetselier
JournalScience
Volume263
Issue5148
Pagination814-7
Date Published1994 Feb 11
ISSN0036-8075
KeywordsAmino 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
Abstract

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.

Alternate JournalScience
PubMed ID8303299