ArticleJournal of virology2011
Identification of two functional domains within the arenavirus nucleoprotein.
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 36 papers.
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Who cites it
36 citing papers in PubMed, 48 citations in OpenAlex.
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- Lassa virus protein-protein interactions as mediators of Lassa fever pathogenesis.Virology journal · 2025Review
- Alternative translation contributes to the generation of a cytoplasmic subpopulation of the Junín virus nucleoprotein that inhibits caspase activation and innate immunity.Journal of virology · 2024Article
- RNA to Rule Them All: Critical Steps in Lassa Virus Ribonucleoparticle Assembly and Recruitment.Journal of the American Chemical Society · 2023Article
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- Isolation of Reconstructed Functional Ribonucleoprotein Complexes of Machupo Virus.Journal of virology · 2021Article
- Molecular characterization of a new highly divergent Mobala related arenavirus isolated from Praomys sp. rodents.Scientific reports · 2021Article
- Distinct Molecular Mechanisms of Host Immune Response Modulation by Arenavirus NP and Z Proteins.Viruses · 2020Review
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- Role of the ERK1/2 Signaling Pathway in the Replication of Junín and Tacaribe Viruses.Viruses · 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
- Differential Immune Responses to New World and Old World Mammalian Arenaviruses.International journal of molecular sciences · 2017Review
- Myristoylation of the Arenavirus Envelope Glycoprotein Stable Signal Peptide Is Critical for Membrane Fusion but Dispensable for Virion Morphogenesis.Journal of virology · 2016Article
- Inhibition of Innate Immune Responses Is Key to Pathogenesis by Arenaviruses.Journal of virology · 2016Review
- Human hemorrhagic Fever causing arenaviruses: molecular mechanisms contributing to virus virulence and disease pathogenesis.Pathogens (Basel, Switzerland) · 2015Review
- Development of live-attenuated arenavirus vaccines based on codon deoptimization.Journal of virology · 2015Article
- Mapping of the interaction domains of the Crimean-Congo hemorrhagic fever virus nucleocapsid protein.The Journal of general virology · 2015Article
- Replication of boid inclusion body disease-associated arenaviruses is temperature sensitive in both boid and mammalian cells.Journal of virology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tacaribe virus (TCRV) belongs to the Arenaviridae family. Its bisegmented negative-stranded RNA genome encodes the nucleoprotein (N), the precursor of the envelope glycoproteins, the polymerase (L), and a RING finger matrix (Z) protein. The 570-amino-acid N protein binds to viral RNA, forming nucleocapsids, which are the template for transcription and replication by the viral polymerase. We have previously shown that the interaction between N and Z is required for assembly of infectious virus-like particles (VLPs) (J. C. Casabona et al., J. Virol. 83:7029-7039, 2009). Here, we examine the functional organization of TCRV N protein. A series of deletions and point mutations were introduced into the N-coding sequence, and the ability of the mutants to sustain heterotypic (N-Z) or homotypic (N-N) interactions was analyzed. We found that N protein displays two functional domains. By using coimmunoprecipitation studies, VLP incorporation assays, and double immunofluorescence staining, the carboxy-terminal region of N was found to be required for N-Z interaction and also necessary for incorporation of N protein into VLPs. Moreover, further analysis of this region showed that the integrity of a putative zinc-finger motif, as well as its amino-flanking sequence (residues 461 to 489), are critical for Z binding and N incorporation into VLPs. In addition, we provide evidence of an essential role of the amino-terminal region of N protein for N-N interaction. In this regard, using reciprocal coimmunoprecipitation analysis, we identified a 28-residue region predicted to form a coiled-coil domain (residues 92 to 119) as a newly recognized molecular determinant of N homotypic interactions.
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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.