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Signal peptide of Lassa virus glycoprotein GP‐C exhibits an unusual length
Author(s) -
Eichler Robert,
Lenz Oliver,
Strecker Thomas,
Garten Wolfgang
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00160-1
Subject(s) - lassa virus , signal peptide , cleavage (geology) , peptide , endoplasmic reticulum , biology , glycoprotein , peptide sequence , signal peptidase , lassa fever , protein subunit , microbiology and biotechnology , virology , virus , biochemistry , paleontology , fracture (geology) , gene
Lassa virus glycoprotein is synthesized as precursor GP‐C into the lumen of the endoplasmic reticulum and cleaved posttranslationally into the N‐terminal subunit GP‐1 and the C‐terminal subunit GP‐2 by subtilase SKI‐1/S1P. The N‐terminal portion of the primary translation product preGP‐C contains a signal peptide of unknown length. In order to demonstrate the signal peptide cleavage site, purified viral GP‐1 isolated from Lassa virus particles was N‐terminally sequenced as TSLYKGV, identical to amino acids 59–65 of GP‐C. Mutational analysis of the amino acid residues flanking the putative cleavage site led to non‐cleavable preGP‐C indicating that no other signal peptide cleavage site exists. Interestingly, GP‐C mutants with a non‐cleavable signal peptide were not further processed by SKI‐1/S1P. This observation suggests that the signal peptide cleavage is necessary for GP‐C maturation and hence for Lassa virus replication.