ArticleScientific reports2018
Trivalent soluble TNF Receptor, a potent TNF-α antagonist for the treatment collagen-induced arthritis.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Trimerized S expressed by modified vaccinia virus Ankara (MVA) confers superior protection against lethal SARS-CoV-2 challenge in mice.Journal of virology · 2024Article
- Biparatopic anti-PCSK9 antibody enhances the LDL-uptake in HepG2 cells.Scientific reports · 2024Article
- Computational design and engineering of self-assembling multivalent microproteins with therapeutic potential against SARS-CoV-2.Journal of nanobiotechnology · 2024Article
- An etanercept O-glycovariant with enhanced potency.Molecular therapy. Methods & clinical development · 2022Article
- Soluble forms of cytokine and growth factor receptors: mechanisms of generation and modes of action in the regulation of local and systemic inflammation.FEBS letters · 2022Review
- Metabolic Messengers: tumour necrosis factor.Nature metabolism · 2021Review
- Primary graft dysfunction after heart transplantation: a thorn amongst the roses.Heart failure reviews · 2019Review
- The Effect of Human Recombinant Tumor Necrosis Factor Receptor-2 on Reducing Inflammatory of Collagen -Induced Arthritis in Balb/c Mice.Iranian journal of biotechnology · 2019Article
- The Long Road Toward COVID-19 Herd Immunity: Vaccine Platform Technologies and Mass Immunization Strategies.Frontiers in immunologyReview
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tumor necrosis factor is a major pro-inflammatory cytokine which triggers various physiological consequences by binding to and trimerizing its receptors, and has been the single most sought-after drug target for intervening autoimmune diseases such as rheumatoid arthritis and psoriasis. However, current TNF-α blockers, including soluble receptor-Fc fusion and therapeutic antibodies, are all dimeric in structure, whereas their target TNF-α itself is homotrimeric in nature. Here we describe the development of a trivalent soluble TNF receptor and show that it is a more potent than the dimeric TNF receptor decoys in inhibiting TNF-α signaling both in vitro and in vivo. The process involves gene fusion between a soluble receptor TNFRII with a ligand binding domain and a trimerization tag from the C-propeptide of human collagen (Trimer-Tag), which is capable of self-assembly into a covalently linked trimer. We show that the homotrimeric soluble TNF receptor (TNFRII-Trimer) produced with such method is more potent in ligand binding kinetics and cell based bioassays, as well as more efficacious in attenuating collagen-induced arthritis (CIA) in a mouse model than its dimeric TNFRII-Fc counterpart. Thus, this work demonstrates the proof of concept of Trimer-Tag and provides a new platform for rational designs of next generation biologic drugs.
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