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 ...Continue Reading
Construction of a recombinant bacterial human CD4 expression system producing a bioactive CD4 molecule.
Molecular organization of Junin virus S RNA: complete nucleotide sequence, relationship with other members of the Arenaviridae and unusual secondary structures.
Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
Costimulatory properties of the human CD4 molecule: enhancement of CD3-induced T cell activation by human immunodeficiency virus type 1 through viral envelope glycoprotein gp120
Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
Steric masking of a dilysine endoplasmic reticulum retention motif during assembly of the human high affinity receptor for immunoglobulin E
Kinetics and pH dependence of acid-induced structural changes in the lymphocytic choriomeningitis virus glycoprotein complex
Localization of Bunyamwera bunyavirus G1 glycoprotein to the Golgi requires association with G2 but not with NSm
Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation
Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike
Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus
Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus
Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
The viral transmembrane superfamily: possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor
Biosynthesis and cellular trafficking of the convertase SKI-1/S1P: ectodomain shedding requires SKI-1 activity
New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor
Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P
Membrane receptor trafficking: evidence of proximal and distal zones conferred by two independent endoplasmic reticulum localization signals
Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected
The MHC class II beta chain cytoplasmic tail overcomes the invariant chain p35-encoded endoplasmic reticulum retention signal
Mechanisms for lymphocytic choriomeningitis virus glycoprotein cleavage, transport, and incorporation into virions
A specific interaction of small molecule entry inhibitors with the envelope glycoprotein complex of the Junín hemorrhagic fever arenavirus.
Old World arenavirus infection interferes with the expression of functional alpha-dystroglycan in the host cell
Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains
Role of the stable signal peptide of Junín arenavirus envelope glycoprotein in pH-dependent membrane fusion
The major determinant of attenuation in mice of the Candid1 vaccine for Argentine hemorrhagic fever is located in the G2 glycoprotein transmembrane domain
Signal peptide requirements for lymphocytic choriomeningitis virus glycoprotein C maturation and virus infectivity
A novel zinc-binding domain is essential for formation of the functional Junín virus envelope glycoprotein complex.
Reverse genetics generation of chimeric infectious Junin/Lassa virus is dependent on interaction of homologous glycoprotein stable signal peptide and G2 cytoplasmic domains
Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication.
Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains
Bitopic membrane topology of the stable signal peptide in the tripartite Junín virus GP-C envelope glycoprotein complex
Substitutions in the glycoprotein (GP) of the Candid#1 vaccine strain of Junin virus increase dependence on human transferrin receptor 1 for entry and destabilize the metastable conformation of GP.
Dissection of the role of the stable signal peptide of the arenavirus envelope glycoprotein in membrane fusion.
Human endogenous retrovirus HERV-K(HML-2) encodes a stable signal peptide with biological properties distinct from Rec.
Uncoupling GP1 and GP2 expression in the Lassa virus glycoprotein complex: implications for GP1 ectodomain shedding.
Biochemical reconstitution of hemorrhagic-fever arenavirus envelope glycoprotein-mediated membrane fusion
Maturation cleavage within the ectodomain of Lassa virus glycoprotein relies on stabilization by the cytoplasmic tail
Innate immune response to arenaviral infection: a focus on the highly pathogenic New World hemorrhagic arenaviruses
Molecular determinants of Pichinde virus infection of guinea pigs--a small animal model system for arenaviral hemorrhagic fevers.
The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain
Characterization of virulence-associated determinants in the envelope glycoprotein of Pichinde virus.
Distinct requirements for signal peptidase processing and function in the stable signal peptide subunit of the Junín virus envelope glycoprotein
Epistastic Interactions within the Junín Virus Envelope Glycoprotein Complex Provide an Evolutionary Barrier to Reversion in the Live-Attenuated Candid#1 Vaccine
Myristoylation of the Arenavirus Envelope Glycoprotein Stable Signal Peptide Is Critical for Membrane Fusion but Dispensable for Virion Morphogenesis
The signal peptide of the mouse mammary tumor virus Rem protein is released from the endoplasmic reticulum membrane and accumulates in nucleoli
Biological Characterization of Conserved Residues within the Cytoplasmic Tail of the Pichinde Arenaviral Glycoprotein Subunit 2 (GP2)
The late endosome-resident lipid bis(monoacylglycero)phosphate is a cofactor for Lassa virus fusion.
Argentine Hemorrhagic Fever
Argentine hemorrhagic fever (AHF) is an endemo-epidemic disease caused by junín virus (JUNV), a member of the arenaviridae family. Discover the latest research on AHF here.