枯草杆菌蛋白酶SKI-1/S1P对淋巴细胞性脉络丛脑膜炎病毒糖蛋白的内切蛋白水解加工
Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P.
作者信息
Beyer Winfried R, Pöpplau Dennis, Garten Wolfgang, von Laer Dorothee, Lenz Oliver
机构信息
Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, D-20251 Hamburg, Germany.
出版信息
J Virol. 2003 Mar;77(5):2866-72. doi: 10.1128/jvi.77.5.2866-2872.2003.
Abstract
The envelope glycoprotein (GP) of lymphocytic choriomeningitis virus (LCMV) is posttranslationally cleaved into two subunits. We show here that this endoproteolytic processing is not required for transport to the cell surface but is essential for LCMV GP to mediate infectivity of pseudotyped retroviral vectors. By systematic mutational analysis of the LCMV GP cleavage site, we determined that the consensus motif R-(R/K/H)-L-(A/L/S/T/F)(265) is essential for the endoproteolytic processing. In agreement with the identified consensus motif, we show that the cellular subtilase SKI-1/S1P cleaves LCMV GP.
摘要
淋巴细胞性脉络丛脑膜炎病毒（LCMV）的包膜糖蛋白（GP）在翻译后被切割成两个亚基。我们在此表明，这种内切蛋白水解加工对于转运到细胞表面不是必需的，但对于LCMV GP介导假型逆转录病毒载体的感染性至关重要。通过对LCMV GP切割位点的系统突变分析，我们确定共有基序R-(R/K/H)-L-(A/L/S/T/F)(265)对于内切蛋白水解加工至关重要。与鉴定出的共有基序一致，我们表明细胞枯草杆菌蛋白酶SKI-1/S1P可切割LCMV GP。
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