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

来源：

EMBO REPORTS | 2003年 / 4卷 / 11期

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

页码：1084 / 1088

页数：5

共 25 条

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