Peptide-mapping of three neutralizing epitopes into predicted biologically active sites of human interferon-alpha 2.
Immunologically less reactive but functionally relevant structures were identified on human interferon (IFN)-alpha 2 by three neutralizing monoclonal antibodies (mAb). The binding sites of these mAbs were mapped using a set of synthetic peptides that covered the amino acid sequence of two predicted biologically active segments in the regions 31-53 and 63-85 of IFN-alpha 2. We measured the capacity of fragments to inhibit the IFN-neutralizing activity of mAbs and located three linear epitopes around residues 42-53, 63-76 and 77-85 of the IFN-alpha 2 molecule.
Kontsek
P
P
Institute of Virology, Slovak Academy of Sciences, Bratislava.
Borecký
L
L
Zav'yalov
V P
VP
Maiorov
V A
VA
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001666:Binding Sites, Antibody; D002417:Cattle; D002460:Cell Line; D000939:Epitopes; D006801:Humans; D007370:Interferon Type I / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D010449:Peptide Mapping; D011994:Recombinant Proteins
D000911:Antibodies, Monoclonal; D000939:Epitopes; D007370:Interferon Type I; D010446:Peptide Fragments; D011994:Recombinant Proteins