ArticleJournal of virology2003
Measles virus (MV) nucleoprotein binds to a novel cell surface receptor distinct from FcgammaRII via its C-terminal domain: role in MV-induced immunosuppression.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 81 citations in OpenAlex.
- TRIM21 Neutralizes Hazara Virus Using a Dual Mechanism of Nucleoprotein Caging and Ubiquitination.Viruses · 2026Article
- Cell surface RNA virus nucleocapsid proteins: a viral strategy for immunosuppression?Npj viruses · 2024Review
- Dimeric immunoglobulin A as a novel diagnostic marker of measles infection.Microbiology spectrum · 2024Article
- Cell surface nucleocapsid protein expression: A betacoronavirus immunomodulatory strategy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cell Surface Nucleocapsid Protein Expression: A Betacoronavirus Immunomodulatory Strategy.bioRxiv : the preprint server for biology · 2023Article
- The Role of Nucleoprotein in Immunity to Human Negative-Stranded RNA Viruses-Not Just Another Brick in the Viral Nucleocapsid.Viruses · 2022Review
- Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis.Progress in molecular biology and translational science · 2020Review
- Nucleolin (NCL) inhibits the growth of peste des petits ruminants virus.The Journal of general virology · 2020Article
- Peste des Petits Ruminants Virus Nucleocapsid Protein Inhibits Beta Interferon Production by Interacting with IRF3 To Block Its Activation.Journal of virology · 2019Article
- Modulation of Measles Virus NBiomolecules · 2018Review
- The Unstructured Paramyxovirus Nucleocapsid Protein Tail Domain Modulates Viral Pathogenesis through Regulation of Transcriptase Activity.Journal of virology · 2018Article
- Activation of Macrophages by Oligomeric Proteins of Different Size and Origin.Mediators of inflammation · 2018Article
- Article
- How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.Cellular and molecular life sciences : CMLS · 2017Review
- The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.Science advances · 2017Article
- Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.International journal of molecular sciences · 2015Article
- The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.The Journal of biological chemistry · 2013Article
- Nucleoprotein-RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopy.Journal of virology · 2011Article
- Measles virus-induced immunosuppression: from effectors to mechanisms.Medical microbiology and immunology · 2010Review
- Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.PloS one · 2010Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During acute measles virus (MV) infection, an efficient immune response occurs, followed by a transient but profound immunosuppression. MV nucleoprotein (MV-N) has been reported to induce both cellular and humoral immune responses and paradoxically to account for immunosuppression. Thus far, this latter activity has been attributed to MV-N binding to human and murine FcgammaRII. Here, we show that apoptosis of MV-infected human thymic epithelial cells (TEC) allows the release of MV-N in the extracellular compartment. This extracellular N is then able to bind either to MV-infected or uninfected TEC. We show that recombinant MV-N specifically binds to a membrane protein receptor, different from FcgammaRII, highly expressed on the cell surface of TEC. This new receptor is referred to as nucleoprotein receptor (NR). In addition, different Ns from other MV-related morbilliviruses can also bind to FcgammaRII and/or NR. We show that the region of MV-N responsible for binding to NR maps to the C-terminal fragment (N(TAIL)). Binding of MV-N to NR on TEC triggers sustained calcium influx and inhibits spontaneous cell proliferation by arresting cells in the G(0) and G(1) phases of the cell cycle. Finally, MV-N binds to both constitutively expressed NR on a large spectrum of cells from different species and to human activated T cells, leading to suppression of their proliferation. These results provide evidence that MV-N, after release in the extracellular compartment, binds to NR and thereby plays a role in MV-induced immunosuppression.
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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.