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J. Biol. Chem., Vol. 281, Issue 20, 13964-13971, May 19, 2006
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1123
4
From the
Biochemistry Department, University of Lausanne, CH-1066 Epalinges, Switzerland and BiogenIdec, Cambridge, Massachusetts 02142
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 species-specific (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, mouse APRIL exists as two different splice variants differing by a single amino acid. Although human APRIL does not interact with BAFF-R, the shorter variant of mouse APRIL exhibits weak but detectable binding to mouse BAFF-R.
Received for publication, February 17, 2006 , and in revised form, March 15, 2006.
* This work was supported by grants from the Swiss National Science Foundation, NCCR Molecular Oncology, and the CTI program (to P. S. and J. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 These authors contributed equally to this work.
2 Present address: Merck & Co, Inc., West Point, PA 19486.
3 Present address: University Medical Center, CH-1211 Geneva, Switzerland.
4 To whom correspondence should be addressed: Dept. of Biochemistry, University of Lausanne, Boveresses 155, CH-1066 Epalinges, Switzerland. Tel.: 41-21-692-5709; Fax: 41-21-692-5705; E-mail: pascal.schneider{at}unil.ch.
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