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  4. Epitopes recognized by neutralizing therapy-induced human anti-interferon-alpha antibodies are localized within the N-terminal functional domain of recombinant interferon-alpha2
 
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1996
Journal Article
Title

Epitopes recognized by neutralizing therapy-induced human anti-interferon-alpha antibodies are localized within the N-terminal functional domain of recombinant interferon-alpha2

Abstract
During prolonged recombinant interferon (rIFN)-alpha2 therapy, a minority of patients develop high-titer neutralizing IFN-alpha antibodies. Sera from nine IFN-alpha antibody-positive patients were studied to characterize the specificity of anti-IFN-alpha neutralizing antibodies by their ability to inhibit the anitviral and antiproliferative activity of differnet rIFN-alpha subtypes and rIFN-alpha1/alpha2 hybrids. These therapy-induced antibodies (TaB) were compared with IFN-alpha-specific autoantibodies (Aab) from two patients with systemic lupus erythematosus who had never received any exogenous IFN-alpha. Although IFN-alpha subtypes are closely related in structure, Tab inhibited the antiviral activity of only recombinant (r)IFN-alpha2 and rIFN-alpha6, but not or slightly that of rIFN-alpha1, -alpha7,-alpha9 and alpha14. Furthermore, of four different rIFN-alpha1/alpha2 hybrids tested, Tab inhibited only those which contained the N-terminal residues 17-64 of rIFN-alpha2.
Author(s)
Nolte, K.-U.
Günther, G.
Wussow, P. von
Journal
European Journal of Immunology  
DOI
10.1002/eji.1830260929
Additional full text version
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Language
English
ITA  
Keyword(s)
  • antigen

  • antigenic determinant

  • cancer

  • immunoglobulins

  • immunology

  • immunospecificity

  • interferon

  • interferon alpha

  • leukemia

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