Lassa virus is the causative agent of a hemorrhagic fever endemic in west Africa. The RNA genome of Lassa virus encodes the glycoprotein precursor GP-C, a nucleoprotein (NP), the viral polymerase L and a small protein Z (11 kDa). Here, we analyze the role of Z protein for virus maturation. We have recently shown that expression of Z protein in the absence of other viral proteins is sufficient for the release of enveloped Z-containing particles. In this study, we examined particles secreted into the supernatant of a stably Z protein-expressing CHO cell line by electron microscopy. The observed Z-induced virus-like particles did not significantly differ in their morphology and size from Lassa virus particles. Mutation of two proline-rich domains within Z which are known to drastically reduce the release of virus-like particles, had no effect on the cellular localization of the protein nor on its membrane-association. Furthermore, we present evidence that Z interacts with the NP. We assume that Z recruits NP to cellular membranes where virus assembly takes place. We conclude from our data that Lassa virus Z protein plays an essential role in Lassa virus maturation.
Biochemical and immunological evidence that the 11 kDa zinc-binding protein of lymphocytic choriomeningitis virus is a structural component of the virus
The completed sequence of lymphocytic choriomeningitis virus reveals a unique RNA structure and a gene for a zinc finger protein
The lymphocytic choriomeningitis virus RING protein Z associates with eukaryotic initiation factor 4E and selectively represses translation in a RING-dependent manner
Nucleocapsid incorporation into parainfluenza virus is regulated by specific interaction with matrix protein
RING finger Z protein of lymphocytic choriomeningitis virus (LCMV) inhibits transcription and RNA replication of an LCMV S-segment minigenome
VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment
Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4
Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected
Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis
Generation and analysis of infectious virus-like particles of uukuniemi virus (bunyaviridae): a useful system for studying bunyaviral packaging and budding
Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains
Incorporation of high levels of chimeric human immunodeficiency virus envelope glycoproteins into virus-like particles
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.
Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication.
A role for the C terminus of Mopeia virus nucleoprotein in its incorporation into Z protein-induced virus-like particles
Lassa virus-like particles displaying all major immunological determinants as a vaccine candidate for Lassa hemorrhagic fever
Reverse genetics generation of chimeric infectious Junin/Lassa virus is dependent on interaction of homologous glycoprotein stable signal peptide and G2 cytoplasmic domains
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.
D471G mutation in LCMV-NP affects its ability to self-associate and results in a dominant negative effect in viral RNA synthesis
Targeting of arenavirus RNA synthesis by a carboxamide-derivatized aromatic disulfide with virucidal activity
An antiviral disulfide compound blocks interaction between arenavirus Z protein and cellular promyelocytic leukemia protein.
The microtubule motor protein KIF13A is involved in intracellular trafficking of the Lassa virus matrix protein Z
The flexible C-terminal arm of the Lassa arenavirus Z-protein mediates interactions with multiple binding partners.
The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain
Strategies of highly pathogenic RNA viruses to block dsRNA detection by RIG-I-like receptors: hide, mask, hit
A cell-based luciferase assay amenable to high-throughput screening of inhibitors of arenavirus budding
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.
Conserved residues in Lassa fever virus Z protein modulate viral infectivity at the level of the ribonucleoprotein
Self-association of lymphocytic choriomeningitis virus nucleoprotein is mediated by its N-terminal region and is not required for its anti-interferon function.
A leucine residue in the C terminus of human parainfluenza virus type 3 matrix protein is essential for efficient virus-like particle and virion release
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.