Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
Authors:
- 1 December 1995
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 69 (12) , 8123-8126
Abstract
We have investigated the cleavages at the flavivirus capsid-prM protein junction in vitro. When expressed in the absence of the flavivirus proteinase, capsid and prM, which are separated by an internal signal sequence, exist as a membrane-spanning precursor protein. Here we show the induction of posttranslational signal peptidase cleavage of prM by trypsin cleavage of a cytoplasmic region of this precursor protein.Keywords
This publication has 31 references indexed in Scilit:
- Deletion Mutation in the Signal Anchor Domain Activates Cleavage of the Influenza Virus Neuraminidase, a Type II transmembrane ProteinJournal of General Virology, 1994
- Transport of Proteins Across the Endoplasmic Reticulum MembraneScience, 1992
- Proteolytic processing of a Murray Valley encephalitis virus non-structural polyprotein segment containing the viral proteinase: accumulation of a NS3-4A precursor which requires mature NS3 for efficient processingJournal of General Virology, 1992
- Processing of dengue virus type 2 structural proteins containing deletions in hydrophobic domainsArchives of Virology, 1992
- FLAVIVIRUS GENOME ORGANIZATION, EXPRESSION, AND REPLICATIONAnnual Review of Microbiology, 1990
- Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IV.Journal of Cell Biology, 1990
- Production of yellow fever virus proteins in infected cells: Identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antiseraVirology, 1990
- Analyses of the terminal sequences of west nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesisVirology, 1989
- The membrane-spanning segment of invariant chain (Iγ) contains a potentially cleavable signal sequenceCell, 1986
- Partial nucleotide sequence of the Murray Valley encephalitis virus genomeJournal of Molecular Biology, 1986