Inhibitor of endogenous human interferon-gamma

Abstract

The invention relates to an inhibitor of endogenous human interferon-gamma (hIFN-ϝ) in autoimmune diseases, especially in multiple sclerosis. More precisely, the invention relates to inactivated protein derivatives of the hIFN-ϝ with preserved affinity to the hIFN-ϝ receptor. The derivatives represent genetically modified variants of hIFN-ϝ, where the C-terminal part of the molecule is either deleted or replaced with a polypeptide sequence of another human protein and a recombinant hIFN-ϝ, inactivated by physical or chemical methods.

1 - 7 . (canceled) 
     
     
         8 . A method of inhibiting endogenous human interferon-gamma (hIFN-γ) comprising administering to a patient in need thereof an effective amount of an inactivated protein derivative of recombinant hIFN-γ characterized in that it represents a genetically modified or physically or chemically treated variant of hIFN-γ having preserved affinity to the hIFN-hIFN-γ receptor. 
     
     
         9 . The method of  claim 8  wherein inhibiting hIFN-γ is for the purpose of treating an autoimmune disease. 
     
     
         10 . The method of  claim 8  wherein inhibiting hIFN-γ is for the purpose of treating multiple sclerosis. 
     
     
         11 . The method of  claim 8  characterized in that the variant of hIFN-γ has a N-terminal primary structure coinciding with that of the human hIFN-γ. 
     
     
         12 . The method of  claim 8  characterized in that the variant of hIFN-γ is a genetically modified derivative of the hIFN-γ where the C-terminal part is truncated by 27 amino acids or replaced with a C-terminal fragment of another human protein. 
     
     
         13 . The method of  claim 8  characterized in that the variant of hIFN-γ is a hybrid protein hIFN-γ/hIFN-α where the C-terminal part corresponds to that of the hIFN-α. 
     
     
         14 . The method of  claim 8  characterized in that the variant of hIFN-γ is inactivated hIFN-γ obtained by UV irradiation of a recombinant human hIFN-γ at 290 nm. 
     
     
         15 . The method of  claim 9  characterized in that the variant of hIFN-γ has a N-terminal primary structure coinciding with that of the human hIFN-γ. 
     
     
         16 . The method of  claim 9  characterized in that the variant of hIFN-γ is a genetically modified derivative of the hIFN-γ where the C-terminal part is truncated by 27 amino acids or replaced with a C-terminal fragment of another human protein. 
     
     
         17 . The method of  claim 9  characterized in that the variant of hIFN-γ is a hybrid protein hIFN-γ/hIFN-α where the C-terminal part corresponds to that of the hIFN-α. 
     
     
         18 . The method of  claim 9  characterized in that the variant of hIFN-γ is inactivated hIFN-γ obtained by UV irradiation of a recombinant human hIFN-γ at 290 nm. 
     
     
         19 . The method of  claim 10  characterized in that the variant of hIFN-γ has a N-terminal primary structure coinciding with that of the human hIFN-γ. 
     
     
         20 . The method of  claim 10  characterized in that the variant of hIFN-γ is a genetically modified derivative of the hIFN-γ where the C-terminal part is truncated by 27 amino acids or replaced with a C-terminal fragment of another human protein. 
     
     
         21 . The method of  claim 10  characterized in that the variant of hIFN-γ is a hybrid protein hIFN-γ/hIFN-α where the C-terminal part corresponds to that of the hIFN-α. 
     
     
         22 . The method of  claim 10  characterized in that the variant of hIFN-γ is inactivated hIFN-γ obtained by UV irradiation of a recombinant human hIFN-γ at 290 nm.