ArticleJournal of virology2011
Molecular determinants of arenavirus Z protein homo-oligomerization and L polymerase binding.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 41 citations in OpenAlex.
- Characterization of conserved residues in the mammarenavirus matrix protein Z using novel Lassa virus life cycle modelling assays.Scientific reports · 2026Article
- Article
- Structural and molecular biology of Sabiá virus.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Lassa Virus Genetics.Current topics in microbiology and immunology · 2023Article
- Review
- Isolation of Reconstructed Functional Ribonucleoprotein Complexes of Machupo Virus.Journal of virology · 2021Article
- Structure of Machupo virus polymerase in complex with matrix protein Z.Nature communications · 2021Article
- Structural basis for recognition and regulation of arenavirus polymerase L by Z protein.Nature communications · 2021Article
- Cryo-EM structures of Lassa and Machupo virus polymerases complexed with cognate regulatory Z proteins identify targets for antivirals.Nature microbiology · 2021Article
- An Antiviral Drug Screening Platform with a FRET Biosensor for Measurement of Arenavirus Z Assembly.Cell structure and function · 2020Article
- A single mutation (V64G) within the RING Domain of Z attenuates Junin virus.PLoS neglected tropical diseases · 2020Article
- NEDD4 family ubiquitin ligases associate with LCMV Z's PPXY domain and are required for virus budding, but not via direct ubiquitination of Z.PLoS pathogens · 2019Article
- Biochemical characterization of the Lassa virus L protein.The Journal of biological chemistry · 2019Article
- Virus⁻Host Interactions Involved in Lassa Virus Entry and Genome Replication.Pathogens (Basel, Switzerland) · 2019Review
- Mammarenaviral Infection Is Dependent on Directional Exposure to and Release from Polarized Intestinal Epithelia.Viruses · 2018Article
- Design of peptide-based epitope vaccine and further binding site scrutiny led to groundswell in drug discovery against Lassa virus.3 Biotech · 2018Article
- The use of novel epitope-tagged arenaviruses reveals that Rab5c-positive endosomal membranes are targeted by the LCMV matrix protein.The Journal of general virology · 2018Article
- Review ofFrontiers in microbiology · 2018Article
- Baseline mapping of Lassa fever virology, epidemiology and vaccine research and development.NPJ vaccines · 2018Review
- Arenavirus Quasispecies and Their Biological Implications.Current topics in microbiology and immunology · 2016Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The arenavirus Z is a zinc-binding RING protein that has been implicated in multiple functions during the viral life cycle. These roles of Z involve interactions with viral and cellular proteins that remain incompletely understood. In this regard, Z inhibits viral RNA transcription and replication through direct interaction with the viral L polymerase. Here, we defined the L-binding domain of Tacaribe virus (TCRV) Z protein and the structural requirements mediating Z homo-oligomerization. By using site-directed mutagenesis, coimmunoprecipitation, and functional assays, we showed that residues R37, N39, W44, L50, and Y57, located around the zinc coordination site I, play a critical role in the Z-L interaction. We also found that Z protein from either TCRV or the pathogenic Junin virus (JUNV) self-associates into oligomeric forms in mammalian cells. Importantly, mutation of the myristoylation site, the strictly conserved residue G at position 2, severely impaired the ability of both TCRV Z and JUNV Z to self-interact as well as their capacity to accumulate at the plasma membrane, strongly suggesting that Z homo-oligomerization is associated with its myristoylation and cell membrane targeting. In contrast, disruption of the RING structure or substitution of W44 or N39, which are critical for L protein recognition, did not affect Z self-binding. Overall, the data presented here indicate that homo-oligomerization is not a requirement for Z-L interaction or Z-mediated polymerase activity inhibition.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.