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Characterization of Mouse Monoclonal Antibodies to Human Interferon‐Gamma
Author(s) -
Yamamoto Yoko,
Miyata Keizo,
Ueda Masamichi,
Kawade Yoshimi,
Matsumoto Kayoko,
Tsukui Kazuo
Publication year - 1988
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1988.tb01394.x
Subject(s) - monoclonal antibody , epitope , antibody , biology , interferon gamma , radioimmunoassay , microbiology and biotechnology , neutralization , virology , biochemistry , immunology , in vitro
Mouse monoclonal antibodies (mAb) to human interferon‐gamma (HuIFN‐ γ ) were characterized. The mAbs studied—E4‐18, G4‐15, and SAT‐1—which are all IgGl‐type, reacted to all HuIFN‐ γ molecular species, both glycosylated and non‐glycosylated. Affinity constants calculated of E4‐18 and G4‐15 didn't have considerable differences for both kinds of HuIFN‐ γ (1–3 × 10 8 liter/mol), but SAT‐1 had a difference—a higher value (10 10 liter/mol) for the former than for the latter (8 × 10 8 liter/mol). In epitope specificity, the results suggested that E4‐18 and G4‐15 recognized an overlapped region remote from the region of SAT‐1. Competition experiment using synthetic peptides suggested that epitope of G4‐15 is around N9‐26 of the HuIFN‐ γ sequence. Those mAbs could be used for sandwich radioimmunoassay of HuIFN‐ γ using double mAbs in two combinations, one (G4‐15/E4‐18) based on dimer forms of HuIFN‐ γ and the other (SAT‐1/E4‐18) based on epitope difference. The mAbs are all neutralizing antibodies in which SAT‐1 neutralized at a lower concentration than did G4‐15, and at a much lower one than did E4‐18. The receptor binding of HuIFN‐ γ was inhibited by mAbs G4‐15 and SAT‐1. Efficacy of G4‐15 and SAT‐1 for the inhibition correspond with that for neutralization.