Conformational changes in pH2-treated human interferon-alpha 2 detected with monoclonal antibodies.
Monoclonal antibodies allowed to demonstrate the existence of alternative antigenic forms of the same molecule as of human interferon (IFN)-alpha 2. Exposure of recombinant IFN to pH 2, although not affecting its bioactivity, induced structural modulation of molecular surface. The antigenic structure of IFN-alpha 2 appeared to be built of the acid-stable and acid-labile epitopes. In general, the acid-stable sites determined subtype-specific antigenic properties of the protein, whereas the acid-labile determinants were responsible for antigenic characteristics shared by some other human IFNs. Acidification of IFN-alpha 2 to pH 2 for at least 1-2 h resulted in simultaneous structural rearrangement of all acid-labile sites.
Kúdela
O
O
Institute of Virology, Slovak Academy of Sciences, Bratislava, Slovak Republic.
Kontseková
E
E
Csabayová
M
M
Záhorová
K
K
Kontsek
P
P
D000911:Antibodies, Monoclonal; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D016898:Interferon-alpha / Q000737:chemistry* / Q000276:immunology; D007700:Kinetics; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D000939:Epitopes; D016898:Interferon-alpha