2005 Volume 67 Issue 5 Pages 543-545
Two kinds of FeIFN-α consisting of 166 amino acids (aa) and 171 aa were expressed in Escherichia coli, and the purified proteins were tested for antiviral activity on homologous and heterologous animal cells. Crude FeIFN induced in feline cells revealed antiviral activity on both homologous and heterologous animal cells. In contrast, both types of recombinant FeIFN-α revealed antiviral activity only on the feline cells. All of the FeIFN-α subtypes showed high activity to vesicular stomatitis virus, and the three species of feline viruses belonging to different families.