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Identification of Lassa virus glycoprotein signal peptide as a trans ‐acting maturation factor
Author(s) -
Eichler Robert,
Lenz Oliver,
Strecker Thomas,
Eickmann Markus,
Klenk HansDieter,
Garten Wolfgang
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400002
Subject(s) - lassa virus , signal peptide , signal peptidase , peptide , endoplasmic reticulum , glycoprotein , biology , biochemistry , cleavage (geology) , peptide sequence , microbiology and biotechnology , virus , virology , gene , paleontology , fracture (geology)
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 wild‐type 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.