Richt J A, Fürbringer T, Koch A, Pfeuffer I, Herden C, Bause-Niedrig I, Garten W
Institut für Virologie, Giessen, Germany.
J Virol. 1998 May;72(5):4528-33. doi: 10.1128/JVI.72.5.4528-4533.1998.
Open reading frame IV (ORF-IV) of Borna disease virus (BDV) encodes a protein with a calculated molecular mass of ca. 57 kDa (p57), which increases after N glycosylation to 94 kDa (gp94). The unglycosylated and glycosylated proteins are proteolytically cleaved by the subtilisin-like protease furin. Furin most likely recognizes one of three potential cleavage sites, namely, an arginine at position 249 of the ORF-IV gene product. The furin inhibitor decRVKRcmk decreases the production of infectious BDV significantly, indicating that proteolytic cleavage of the gp94 precursor molecule is necessary for the full biological activity of the BDV glycoprotein.
博尔纳病病毒（BDV）的开放阅读框IV（ORF-IV）编码一种计算分子量约为57 kDa的蛋白质（p57），该蛋白经N-糖基化后分子量增加至94 kDa（gp94）。未糖基化和糖基化的蛋白质被枯草杆菌蛋白酶样蛋白酶弗林蛋白酶进行蛋白水解切割。弗林蛋白酶最有可能识别三个潜在切割位点之一，即ORF-IV基因产物第249位的精氨酸。弗林蛋白酶抑制剂decRVKRcmk显著降低感染性BDV的产生，这表明gp94前体分子的蛋白水解切割对于BDV糖蛋白的完全生物学活性是必需的。
