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Production, Purification and Biological Properties of an Escherichia Coli-derived Recombinant Porcine Alpha Interferon

Francisco Borras-Cuesta

Institut National de la Recherche Agronomique, Laboratoire de Virologie et Immunologie Moléculaires, Centre de Recherches de Jouy-en-Josas, Domaine de Vilvert, 78350 Jouy-en-Josas, France

Recombinant plasmids for intracellular synthesis of mature porcine interferon alpha 1 (IFN-1) in Escherichia coli were constructed. High amounts of antiviral activity were obtained [up to 4 x 10⁵ international units (IU) per ml of bacterial culture]. Recombinant porcine IFN-1 (rIFN-1) 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 x 10⁷ to 10 x 10⁷ IU/mg MDBK cells. In vitro biological properties of this purified rIFN-1 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-1 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.

Present address: Universidad de Navarra, Facultad de Medicina, Dpto de Medicina Interna, Apartado 273, Pamplona, Spain.

Received 29 August 1989; accepted 26 January 1990.

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