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Interactions of Tumor Necrosis Factor (TNF) and TNF Receptor Family Members in the Mouse and Human by Claudia Bossen; Karine Ingold; Aubry Tardivel; Jean-Luc Bodmer; Olivier Gaide; Sylvie Hertig; Christine Ambrose; Jürg Tschopp; Pascal Schneider is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Ligands of the tumor necrosis factor superfamily (TNFSF) (4 -1BBL, APRIL, BAFF, CD27L, CD30L, CD40L, EDA1, EDA2, FasL, GITRL, LIGHT, lymphotoxin ␣, lymphotoxin ␣␤, OX40L, RANKL, TL1A, TNF, TWEAK, and TRAIL) bind members of the TNF receptor superfamily (TNFRSF). A comprehensive survey of ligand-receptor interactions was performed using a flow cytometry-based assay. All ligands engaged between one and five receptors, whereas most receptors only bound one to three ligands. The receptors DR6, RELT, TROY, NGFR, and mouse TNFRH3 did not interact with any of the known TNFSF ligands, suggesting that they either bind other types of ligands, function in a ligand-independent manner, or bind ligands that remain to be identified. The study revealed that ligand-receptor pairs are either cross-reactive between human and mouse (e.g. Tweak/Fn14, RANK/ RANKL), strictly species-specific (GITR/GITRL), or partially speciesspecific (e.g. OX40/OX40L, CD40/CD40L). Interestingly, the receptor binding patterns of lymphotoxin ␣ and ␣␤ are redundant in the human but not in the mouse system. Ligand oligomerization allowed detection of weak interactions, such as that of human TNF with mouse TNFR2. In addition,

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Author

Claudia Bossen; Karine Ingold; Aubry Tardivel; Jean-Luc Bodmer; Olivier Gaide; Sylvie Hertig; Christine Ambrose; Jürg Tschopp; Pascal Schneider

Publisher

Elsevier BV

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)