Functioning of the stable signal peptide of the pCloDF13-encoded bacteriocin release protein

1991 ◽  
Vol 5 (2) ◽  
pp. 393-399 ◽  
Author(s):  
J. Luirink ◽  
B. Duim ◽  
J. W. L. Gier ◽  
B. Oudega
Keyword(s):  
Signal Peptide ◽  
Bacteriocin Release Protein ◽  
Stable Signal

scholarly journals Role of the Stable Signal Peptide and Cytoplasmic Domain of G2 in Regulating Intracellular Transport of the Junín Virus Envelope Glycoprotein Complex

2006 ◽  
Vol 80 (11) ◽  
pp. 5189-5198 ◽  
Author(s):  
Sudhakar S. Agnihothram ◽  
Joanne York ◽  
Jack H. Nunberg
Keyword(s):  
Cell Surface ◽  
Signal Peptide ◽  
Envelope Glycoprotein ◽  
Intracellular Transport ◽  
Cytoplasmic Domain ◽  
Virus Envelope ◽  
Quality Control Process ◽  
C Complex ◽  
Stable Signal

ABSTRACT Enveloped viruses utilize the membranous compartments of the host cell for the assembly and budding of new virion particles. In this report, we have investigated the biogenesis and trafficking of the envelope glycoprotein (GP-C) of the Junín arenavirus. The mature GP-C complex is unusual in that it retains a stable signal peptide (SSP) as an essential component in association with the typical receptor-binding (G1) and transmembrane fusion (G2) subunits. We demonstrate that, in the absence of SSP, the G1-G2 precursor is restricted to the endoplasmic reticulum (ER). This constraint is relieved by coexpression of SSP in trans, allowing transit of the assembled GP-C complex through the Golgi and to the cell surface, the site of arenavirus budding. Transport of a chimeric CD4 glycoprotein bearing the transmembrane and cytoplasmic domains of G2 is similarly regulated by SSP association. Truncations to the cytoplasmic domain of G2 abrogate SSP association yet now permit transport of the G1-G2 precursor to the cell surface. Thus, the cytoplasmic domain of G2 is an important determinant for both ER localization and its control through SSP binding. Alanine mutations to either of two dibasic amino acid motifs in the G2 cytoplasmic domain can also mobilize the G1-G2 precursor for transit through the Golgi. Taken together, our results suggest that SSP binding masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP-C complex is transported for virion assembly. This quality control process points to an important role of SSP in the structure and function of the arenavirus envelope glycoprotein.

scholarly journals Human endogenous retrovirus HERV-K(HML-2) encodes a stable signal peptide with biological properties distinct from Rec

Retrovirology ◽  
2009 ◽  
Vol 6 (1) ◽  
pp. 17 ◽  
Author(s):  
Alessia Ruggieri ◽  
Esther Maldener ◽  
Marlies Sauter ◽  
Nikolaus Mueller-Lantzsch ◽  
Eckart Meese ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Biological Properties ◽  
Endogenous Retrovirus ◽  
Human Endogenous Retrovirus ◽  
Stable Signal

scholarly journals The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain

Virology ◽  
2013 ◽  
Vol 436 (1) ◽  
pp. 127-133 ◽  
Author(s):  
Dominique J. Burri ◽  
Antonella Pasquato ◽  
Joel Ramos da Palma ◽  
Sebastien Igonet ◽  
Michael B.A. Oldstone ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Envelope Glycoprotein ◽  
Proteolytic Processing ◽  
Old World ◽  
Stable Signal

scholarly journals Bitopic Membrane Topology of the Stable Signal Peptide in the Tripartite Junín Virus GP-C Envelope Glycoprotein Complex

2007 ◽  
Vol 81 (8) ◽  
pp. 4331-4337 ◽  
Author(s):  
Sudhakar S. Agnihothram ◽  
Joanne York ◽  
Meg Trahey ◽  
Jack H. Nunberg
Keyword(s):  
Membrane Fusion ◽  
Signal Peptide ◽  
Envelope Glycoprotein ◽  
Lipid Membrane ◽  
Critical Role ◽  
Membrane Topology ◽  
Single Amino Acid ◽  
Fusion Activity ◽  
C Complex ◽  
Stable Signal

ABSTRACT The stable signal peptide (SSP) of the GP-C envelope glycoprotein of the Junín arenavirus plays a critical role in trafficking of the GP-C complex to the cell surface and in its membrane fusion activity. SSP therefore may function on both sides of the lipid membrane. In this study, we have investigated the membrane topology of SSP by confocal microscopy of cells treated with the detergent digitonin to selectively permeabilize the plasma membrane. By using an affinity tag to mark the termini of SSP in the properly assembled GP-C complex, we find that both the N and C termini reside in the cytosol. Thus, SSP adopts a bitopic topology in which the C terminus is translocated from the lumen of the endoplasmic reticulum to the cytoplasm. This model is supported by (i) the presence of two conserved hydrophobic regions in SSP (hφ1 and hφ2) and (ii) our previous demonstration that lysine-33 in the ectodomain loop is essential for pH-dependent membrane fusion. Moreover, we demonstrate that the introduction of a charged side chain or single amino acid deletion in the membrane-spanning hφ2 region significantly diminishes SSP association in the GP-C complex and abolishes membrane fusion activity. Taken together, our results suggest that bitopic membrane insertion of SSP is centrally important in the assembly and function of the tripartite GP-C complex.

scholarly journals Mapping the Landscape of the Lymphocytic Choriomeningitis Virus Stable Signal Peptide Reveals Novel Functional Domains

2007 ◽  
Vol 81 (11) ◽  
pp. 5649-5657 ◽  
Author(s):  
April A. Saunders ◽  
Joey P. C. Ting ◽  
Jeffrey Meisner ◽  
Benjamin W. Neuman ◽  
Mar Perez ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Lymphocytic Choriomeningitis ◽  
Lymphocytic Choriomeningitis Virus ◽  
Surface Glycoprotein ◽  
Functional Domains ◽  
In Vitro Mutagenesis ◽  
Glycoprotein Precursor ◽  
Virus Surface ◽  
Stable Signal

ABSTRACT The stable signal peptide (SSP) of the lymphocytic choriomeningitis virus surface glycoprotein precursor has several unique characteristics. The SSP is unusually long, at 58 amino acids, and contains two hydrophobic domains, and its sequence is highly conserved among both Old and New World arenaviruses. To better understand the functions of the SSP, a panel of point and deletion mutants was created by in vitro mutagenesis to target the highly conserved elements within the SSP. We were also able to confirm critical residues required for separate SSP functions by trans-complementation. Using these approaches, it was possible to resolve functional domains of the SSP. In characterizing our SSP mutants, we discovered that the SSP is involved in several distinct functions within the viral life cycle, beyond translocation of the viral surface glycoprotein precursor into the endoplasmic reticulum lumen. The SSP is required for efficient glycoprotein expression, posttranslational maturation cleavage of GP1 and GP2 by SKI-1/S1P protease, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.

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