A rat monoclonal antibody against mouse α and β interferon of all molecular weight species

• Published in: Nature (London) 1982-04, Vol.296 (5858), p.664-665
• Main Authors: Kemler, R, Maeyer, E. De, Männel, Daniela, Cachard, A, Maeyer-Guignard, Jaqueline De
• Format: Article
• Language: English
• Subjects: Animals; Antibodies, Monoclonal - immunology; Antibody Specificity; Cross Reactions; Epitopes; Humanities and Social Sciences; Interferons - immunology; letter; Mice; Molecular Weight; multidisciplinary; Rats; Science; Science (multidisciplinary)
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/296664a0

Monoclonal antibodies have proven to be invaluable reagents for the characterization and purification of human interferons (IFN). Hybridoma lines secreting monospecific antibodies against human IFN- α and IFN- β have been isolated, and these antibodies have shown no cross-reactivity between the two interferons 1–4 . Murine interferons, when analysed by polyacrylamide gel electrophoresis, have two major migration patterns, one in the 28,000–35,000 (28–35 K) molecular weight ( M r ) region and the second in the 22 K region 5–8 . Based on some homology of the N-terminal amino acid sequence with human interferons, the 28 K and 35 K species are classified as mouse IFN- β and the 22 K species as mouse IFN- α 9 . Minor species have also been described but their relationship to IFN- α and IFN- β is unknown 10,11 . We have now established a stable hybridoma line secreting rat antibodies to mouse virus-induced interferon. The monoclonal antibodies are of the IgG class, with binding activity to all the different M r specied, as demonstrated in an enzyme-linked immunosorbent assay (ELISA) and by affinity chromatography. In addition, the antiviral activity of all the M r species was neutralized by the antibody but the neutralizing activity was much weaker than the binding activity. This indicates the presence of a common antigenic site for all mouse α and β interferon species.