ArticleScientific reports2017
Cellular splicing factor UAP56 stimulates trimeric NP formation for assembly of functional influenza viral ribonucleoprotein complexes.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- Proteomic Analysis of Influenza.Advances in experimental medicine and biology · 2026Review
- Cellular hnRNP AB inhibits avian influenza virus RNA synthesis via blocking UAP56-mediated nuclear export of PB2 mRNA.Veterinary research · 2025Article
- Baculovirus 25K hijacks host UAP56 to facilitate nuclear export of viral mRNA in insect cells.Journal of virology · 2025Article
- Critical Cellular Functions and Mechanisms of Action of the RNA Helicase UAP56.Journal of molecular biology · 2024Review
- Host Cell Factors That Interact with Influenza Virus Ribonucleoproteins.Cold Spring Harbor perspectives in medicine · 2021Review
- Cellular mRNA export factor UAP56 recognizes nucleic acid binding site of influenza virus NP protein.Biochemical and biophysical research communications · 2020Article
- Amino Acid Mutations A286V and T437M in the Nucleoprotein Attenuate H7N9 Viruses in Mice.Journal of virology · 2020Article
- Assembly and remodeling of viral DNA and RNA replicons regulated by cellular molecular chaperones.Biophysical reviews · 2018Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influenza virus RNA genome exists as a ribonucleoprotein (RNP) complex by interacting with NP, one of virus-encoded RNA binding proteins. It is proposed that trimeric NP is a functional form, but it is not clear how trimeric NP is formed and transferred to RNA. UAP56, a cellular splicing factor, functions as a molecular chaperone for NP and is required for the replication-coupled RNP formation of newly synthesized viral genome, but the details of NP transfer to viral RNA by UAP56 is unclear. Here we found that UAP56 is complexed with trimeric NP, but not monomeric NP. Gel filtration analysis and atomic force microscopy analysis indicated that the complex consists of two trimeric NP connected by UAP56. We also found that UAP56 stimulates trimeric NP formation from monomeric NP even at physiological salt concentrations. Thus, UAP56 facilitates the transfer of NP to viral RNA since trimeric NP has higher RNA binding activity than monomeric NP. Further, UAP56 represses the binding of excess amount of NP to RNA possibly by transferring trimeric NP. Collectively, we propose that UAP56 stimulates viral RNP formation through promotion of the assembly of trimeric NP and is important for the structural integrity of NP-RNA complex.
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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.