作者: M A Horisberger , G K McMaster , H Zeller , M G Wathelet , J Dellis
DOI: 10.1128/JVI.64.3.1171-1181.1990
关键词:
摘要: Abstract The human protein p78 is induced and accumulated in cells treated with type I interferon or some viruses. It the homolog of mouse Mx involved resistance to influenza virus. A full-length cDNA clone encoding was cloned sequenced. contained an open reading frame 662 amino acids, corresponding a polypeptide predicted molecular weight 75,500, good agreement Mr 78,000 determined on sodium dodecyl sulfate gels for purified natural protein. The gene expressed vitro corresponded size, pI, antigenic determinant(s), NH2 terminus sequence second which encoded 633-amino-acid sharing 63% homology p78. This p78-related translated reticulocyte lysates where it shared determinant(s) putative 5' regulatory region 83 base pairs within promoter upstream presumed mRNA cap site conferred alpha (IFN-alpha) inducibility cat reporter gene. high levels IFN-alpha. In contrast, not at detectable levels. rate decay diploid after 24-h treatment IFN-alpha much slower than antiviral state against virus vesicular stomatitis virus, suggesting that probably mechanism. Furthermore, we showed these proteins, as well homologous protein, possess three consensus elements proper spacing, characteristic GTP-binding proteins.