Relativity of an antigenic homology between human interferon-alpha 1 and interferon-alpha 2c.
Analysis of an antigenic relatedness between human interferon (IFN)-alpha 1 and IFN-alpha 2 was performed with mapped monoclonal antibodies raised to the respective subtypes. Antigenic properties of immunoreactive domains located in the N-terminal segments 30-67 of IFN-alpha 1 and IFN-alpha 2 were found distinct when compared by neutralization bioassay or ELISA. On the other hand, corresponding domains exhibited an unexpectedly high antigenic homology when tested by Western blot. We suppose that this relativity in antigenic relation lies in the various extent of denaturation of IFN-molecules in bioassay, ELISA and immunoblot. Structural differences of tested antigens may be responsible for a conformation-determined access of antibodies to the shared epitopes.
Csabayová
M
M
Institute of Virology, Slovak Academy of Sciences, Bratislava, Slovak Republic.
Kontseková
E
E
Kontsek
P
P
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D015153:Blotting, Western; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000235:genetics / Q000276:immunology; D006801:Humans; D007370:Interferon Type I / Q000235:genetics / Q000276:immunology*; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D011487:Protein Conformation; D011489:Protein Denaturation; D011994:Recombinant Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D000911:Antibodies, Monoclonal; D000939:Epitopes; D007370:Interferon Type I; D011994:Recombinant Proteins