Identification of Lassa virus glycoprotein signal peptide as a trans-acting maturation factor

被引:122
作者
Eichler, R [1 ]
Lenz, O [1 ]
Strecker, T [1 ]
Eickmann, M [1 ]
Klenk, HD [1 ]
Garten, W [1 ]
机构
[1] Univ Marburg, Inst Virol, D-35037 Marburg, Germany
关键词
D O I
10.1038/sj.embor.7400002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lassa virus glycoprotein is translated as a precursor (pre-GP-C) into the lumen of the endoplasmic reticulum and is cotranslationally cleaved into the signal peptide and GP-C, before GP-C is proteolytically processed into its subunits GP1 and GP2. The signal peptide of pre-GP-C comprises 58 amino acids. The substitution of Lassa virus pre-GP-C signal peptide with another signal peptide still mediates translocation and the release of signal peptide but abolishes the proteolytic cleavage of GP-C into GP1 and GP2. Remarkably, cleavage of GP-C from these hybrid pre-GP-C substrates was restored on coexpression of the wildtype pre-GP-C signal peptide, indicating that the signal peptide functions as a trans-acting factor to promote Lassa virus GP-C processing. To our knowledge, this is the first report on a signal peptide that is essential for proteolytic processing of a secretory pathway protein.
引用
收藏
页码:1084 / 1088
页数:5
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