Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P

被引：174

作者：

Beyer, WR

Pöpplau, D

Garten, W

von Laer, D

Lenz, O

机构：

[1] Univ Hamburg, Heinrich Pette Inst Expt Virol & Immunol, D-20251 Hamburg, Germany

[2] Georg Speyer Haus, D-60596 Frankfurt, Germany

[3] Univ Marburg, Inst Virol, D-35037 Marburg, Germany

来源：

JOURNAL OF VIROLOGY | 2003年 / 77卷 / 05期

关键词：

D O I：

10.1128/JVI.77.5.2866-2872.2003

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：2866 / 2872

页数：7

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