%0 Journal Article %A Lefèvre, François %A L’Haridon, René %A Borras-Cuesta, Francisco %A la Bonnardière, Claude %T Production, Purification and Biological Properties of an Escherichia Coli-derived Recombinant Porcine Alpha Interferon %D 1990 %J Journal of General Virology, %V 71 %N 5 %P 1057-1063 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-71-5-1057 %I Microbiology Society, %X Recombinant plasmids for intracellular synthesis of mature porcine interferon alpha 1 (IFN-α1) in Escherichia coli were constructed. High amounts of antiviral activity were obtained [up to 4 × 105 international units (IU) per ml of bacterial culture]. Recombinant porcine IFN-αl (rIFN-αl) was purified to homogeneity by monoclonal antibody immunoaffinity and was found to have the expected M r (17·5K) and N-terminal sequence (except for the apparent lack of an N-terminal methionine). Its specific antiviral activity was 5 × 107 to 10×l07 lU/mg MDBK cells. In vitro biological properties of this purified rIFN-α1 were compared to those of virus-induced porcine leukocyte interferon: the two interferons shared similar antigenic determinants and had the same ability to induce a cytocidal effect on primary cultures of pig kidney epithelial cells. However, rIFN-α1 was at least six times more active in inducing an antiviral state on homologous porcine cells. These properties are discussed in the light of a possible in vivo use of the purified recombinant molecule. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-71-5-1057