Establishment of strongly neutralizing monoclonal antibody to human interleukin-6 and its epitope analysis.
Three monoclonal antibodies against human interleukin-6 were established and characterized. One antibody was shown to strongly neutralize both the Ig-inducing and hybridoma/plasmacytoma growth activity of interleukin-6. The results of its epitope analysis using protease treated interleukin-6 and immobilized antibody indicated that this neutralizing antibody binds to a peptide corresponding to Leu151-Lys171 of interleukin-6 molecule. Further analysis using synthetic peptides showed that a shorter peptide corresponding to Ala153-Thr162 can also inhibit the binding of the antibody to interleukin-6. These results suggest that this carboxyl-terminal region plays a crucial role in interleukin-6 functions.
Ida
N
N
Basic Research Laboratories, Toray Industries, Inc., Kamakura, Japan.
Sakurai
S
S
Hosaka
T
T
Hosoi
K
K
Kunitomo
T
T
Shimazu
T
T
Maruyama
T
T
Matsuura
Y
Y
Kohase
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000302:isolation & purification; D002851:Chromatography, High Pressure Liquid; D000939:Epitopes / Q000032:analysis* / Q000302:isolation & purification; D006801:Humans; D015850:Interleukin-6 / Q000032:analysis / Q000276:immunology*; D007700:Kinetics; D051379:Mice; D008807:Mice, Inbred BALB C / Q000276:immunology; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D010455:Peptides / Q000138:chemical synthesis; D011994:Recombinant Proteins / Q000032:analysis / Q000276:immunology
D000911:Antibodies, Monoclonal; D000939:Epitopes; D015850:Interleukin-6; D010455:Peptides; D011994:Recombinant Proteins