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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Production, purification and biological properties of an Escherichia coli-derived recombinant porcine alpha interferon.

Recombinant plasmids for intracellular synthesis of mature porcine interferon alpha 1 (IFN-alpha 1) in Escherichia coli were constructed. High amounts of antiviral activity were obtained [up to 4 x 10(5) international units (IU) per ml of bacterial culture]. Recombinant porcine IFN-alpha 1 (rIFN-alpha 1) was purified to homogeneity by monoclonal antibody immunoaffinity and was found to have the expected Mr (17.5K) and N-terminal sequence (except for the apparent lack of an N-terminal methionine). Its specific antiviral activity was 5 x 10(7) to 10 x 10(7) IU/mg MDBK cells. In vitro biological properties of this purified rIFN-alpha 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-alpha 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.[1]

References

  1. Production, purification and biological properties of an Escherichia coli-derived recombinant porcine alpha interferon. Lefèvre, F., L'Haridon, R., Borras-Cuesta, F., La Bonnardière, C. J. Gen. Virol. (1990) [Pubmed]
 
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