A bivalent immunoadhesin of the human interferon-gamma receptor is an effective inhibitor of IFN-gamma activity.
J Interferon Cytokine Res
; 15(12): 1111-5, 1995 Dec.
Article
en En
| MEDLINE
| ID: mdl-8746794
ABSTRACT
We describe here the bioengineering of a bivalent IFN-gamma-RFc immunoadhesin consisting of the extracellular domain of the human IFN-gamma receptor alpha chain (IFN-gamma-R) fused to a human IgG1 Fc region (encoding hinge, CH2 and CH3 domain) that was efficiently expressed as a covalently linked homodimer in insect cells and purified in a one-step purification procedure. The IFN-gamma-RFc fusion protein exerted a 3-fold higher ligand binding affinity in binding competition studies in vitro compared with the monovalent extracellular IFN-gamma-R domain. In addition, the in vitro antagonistic activity of IFN-gamma-RFc, as determined by inhibition of IFN-gamma-induced virus protection and HLA-DR expression, was more than 30-fold higher in comparison with the monovalent soluble receptor. The described IFN-gamma-R immunoadhesin is a potential therapeutic reagent to interfere with the disease-promoting activities of IFN-gamma in several autoimmune diseases.
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Banco de datos:
MEDLINE
Asunto principal:
Antígenos CD
/
Interferón gamma
/
Inmunoadhesinas CD4
/
Receptores de Interferón
/
Estructura Terciaria de Proteína
Límite:
Animals
/
Humans
Idioma:
En
Año:
1995
Tipo del documento:
Article