Abstract：
:Tumor necrosis factor receptor 2 (TNFR2) is known to mediate immune suppression and tissue regeneration. Interestingly, the transmembrane form of tumor necrosis factor (tmTNF) is necessary to robustly activate TNFR2. To characterize the stoichiometry and composition of tmTNF during TNFR2 activation, we constructed differently oligomerized single chain TNF ligands (scTNF) comprised of three TNF homology domain (THD) protomers that mimic tmTNF. Using a variety of cellular and in vivo assays, we can show that higher oligomerization of the scTNF trimers results in more efficient TNF/TNFR2 clustering and subsequent signal transduction. Importantly, the three-dimensional orientation of the scTNF trimers impacts the bioactivity of the oligomerized scTNF ligands. Our data unravel the organization of tmTNF-mimetic scTNF ligands capable of robustly activating TNFR2 and introduce novel TNFR2 agonists that hold promise as therapeutics to treat a variety of diseases.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Fischer R,Marsal J,Guttà C,Eisler SA,Peters N,Bethea JR,Pfizenmaier K,Kontermann REdoi
10.1038/s41598-017-06993-4subject
Has Abstractpub_date
2017-07-26 00:00:00pages
6607issue
1issn
2045-2322pii
10.1038/s41598-017-06993-4journal_volume
7pub_type
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