The Z protein has been shown for several arenaviruses to serve as the viral matrix protein. As such, Z provides the principal force for the budding of virus particles and is capable of forming virus-like particles (VLPs) when expressed alone. For most arenaviruses, this activity has been shown to be linked to the presence of proline-rich late-domain motifs in the C terminus; however, for the New World arenavirus Tacaribe virus (TCRV), no such motif exists within Z. It was recently demonstrated that while TCRV Z is still capable of functioning as a matrix protein to induce the formation of VLPs, neither its ASAP motif, which replaces a canonical PT/SAP motif in related viruses, nor its YxxL motif is involved in budding, leading to the suggestion that TCRV uses a novel budding mechanism. Here we show that in comparison to its closest relative, Junin virus (JUNV), TCRV Z buds only weakly when expressed in isolation. While this budding activity is independent of the ASAP or YxxL motif, it is significantly enhanced by coexpression with the nucleoprotein (NP), an effect not seen with JUNV Z. Interestingly, both the ASAP and YxxL motifs of Z appear to be critical for the recruitment of NP into VLPs, as well as for the enhancement of T...Continue Reading
The Tacaribe arenavirus small zinc finger protein is required for both mRNA synthesis and genome replication
From the Centers for Disease Control and Prevention. Work-related injuries and illnesses associated with child labor--United States, 1993
An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm
The lymphocytic choriomeningitis virus RING protein Z associates with eukaryotic initiation factor 4E and selectively represses translation in a RING-dependent manner
From the Centers for Disease Control and Prevention. Fatal illnesses associated with a New World arenavirus--California, 1999-2000
Transcription and RNA replication of tacaribe virus genome and antigenome analogs require N and L proteins: Z protein is an inhibitor of these processes
Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P
Role of the virus nucleoprotein in the regulation of lymphocytic choriomeningitis virus transcription and RNA replication
Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected
Mechanisms for lymphocytic choriomeningitis virus glycoprotein cleavage, transport, and incorporation into virions
Characterization of the Lassa virus matrix protein Z: electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP)
Contribution of ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles
The signal peptide of the Junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex
Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis
Role of the stable signal peptide and cytoplasmic domain of G2 in regulating intracellular transport of the Junín virus envelope glycoprotein complex.
Genetic identification of Kodoko virus, a novel arenavirus of the African pigmy mouse (Mus Nannomys minutoides) in West Africa
Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains
Chapare virus, a newly discovered arenavirus isolated from a fatal hemorrhagic fever case in Bolivia.
Mapping of the tacaribe arenavirus Z-protein binding sites on the L protein identified both amino acids within the putative polymerase domain and a region at the N terminus of L that are critically involved in binding.
Efficient reverse genetics generation of infectious junin viruses differing in glycoprotein processing.
Host-species transferrin receptor 1 orthologs are cellular receptors for nonpathogenic new world clade B arenaviruses.
The RING domain and the L79 residue of Z protein are involved in both the rescue of nucleocapsids and the incorporation of glycoproteins into infectious chimeric arenavirus-like particles.
Mumps virus matrix, fusion, and nucleocapsid proteins cooperate for efficient production of virus-like particles.
Genetic detection and characterization of Lujo virus, a new hemorrhagic fever-associated arenavirus from southern Africa.
The z protein of the new world arenavirus tacaribe virus has bona fide budding activity that does not depend on known late domain motifs.
Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression
Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding.
Tsg101 is recruited by a late domain of the nucleocapsid protein to support budding of Marburg virus-like particles.
The C-terminal end of parainfluenza virus 5 NP protein is important for virus-like particle production and M-NP protein interaction
Cleavage of the Junin virus nucleoprotein serves a decoy function to inhibit the induction of apoptosis during infection
Conserved residues in Lassa fever virus Z protein modulate viral infectivity at the level of the ribonucleoprotein
A role for the C terminus of Mopeia virus nucleoprotein in its incorporation into Z protein-induced virus-like particles
The C-terminal region of lymphocytic choriomeningitis virus nucleoprotein contains distinct and segregable functional domains involved in NP-Z interaction and counteraction of the type I interferon response.
Tacaribe virus but not junin virus infection induces cytokine release from primary human monocytes and macrophages.
Identification of critical amino acids within the nucleoprotein of Tacaribe virus important for anti-interferon activity.
C-Terminal DxD-Containing Sequences within Paramyxovirus Nucleocapsid Proteins Determine Matrix Protein Compatibility and Can Direct Foreign Proteins into Budding Particles
Differential contributions of tacaribe arenavirus nucleoprotein N-terminal and C-terminal residues to nucleocapsid functional activity
The use of novel epitope-tagged arenaviruses reveals that Rab5c-positive endosomal membranes are targeted by the LCMV matrix protein
E3 Ligase ITCH Interacts with the Z Matrix Protein of Lassa and Mopeia Viruses and Is Required for the Release of Infectious Particles
The Integrity of the YxxL Motif of Ebola Virus VP24 Is Important for the Transport of Nucleocapsid-Like Structures and for the Regulation of Viral RNA Synthesis
Human BST-2/tetherin inhibits Junin virus release from host cells and its inhibition is partially counteracted by viral nucleoprotein
Absence of an N-Linked Glycosylation Motif in the Glycoprotein of the Live-Attenuated Argentine Hemorrhagic Fever Vaccine, Candid #1, Results in Its Improper Processing, and Reduced Surface Expression
Genomic characterization, phylogenetic position and in situ localization of a novel putative mononegavirus in Lepeophtheirus salmonis
A genome-wide siRNA screen identifies a druggable host pathway essential for the Ebola virus life cycle
[Molecular mechanisms of highly pathogenic viruses' replication and their applications for a novel drug discovery].
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.