ArticlePLoS pathogens2019
Nipah virus induces two inclusion body populations: Identification of novel inclusions at the plasma membrane.
Article in PLoS pathogens, 2019. 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, 63 citations in OpenAlex.
- Identification of Blood Flow Type and Position of Blood Barrier in the Fruit Bat Spleen.Anatomia, histologia, embryologia · 2026Article
- Antiviral drug discovery and development: challenges and future directions.Signal transduction and targeted therapy · 2026Review
- Identification of extracellular vesicle microRNAs as potential facilitators of interferon-alpha escape in Marek's disease virus infection.Frontiers in cellular and infection microbiology · 2026Article
- Coordinated interactions among Nipah virus N, P and M proteins drive formation of distinct inclusion bodies.The Journal of general virology · 2025Article
- Human metapneumovirus: understanding the molecular mechanisms and pathology of infection.Journal of virology · 2025Review
- The intracellular virus-host interface of henipaviruses.Journal of virology · 2025Review
- Construction of Minigenome Replicon of Nipah Virus and Investigation of Biological Activity.Viruses · 2025Article
- Visualization of Respiratory Syncytial Virus RNA Synthesis Sites by Ethynyl Uridine Labeling.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Paramyxovirus matrix proteins modulate host cell translation via exon-junction complex interactions in the cytoplasm.bioRxiv : the preprint server for biology · 2024Article
- Liquid-liquid phase inclusion bodies in acute and persistent parainfluenaza virus type 5 infections.The Journal of general virology · 2024Article
- A specific phosphorylation-dependent conformational switch in SARS-CoV-2 nucleocapsid protein inhibits RNA binding.Science advances · 2024Article
- Article
- Grass carp reovirus VP56 and VP35 induce formation of viral inclusion bodies for replication.iScience · 2024Article
- Negative and ambisense RNA virus ribonucleocapsids: more than protective armor.Microbiology and molecular biology reviews : MMBR · 2023Review
- Disruption of Ebola NPJournal of molecular biology · 2023Article
- Spatial and functional arrangement of Ebola virus polymerase inside phase-separated viral factories.Nature communications · 2023Article
- Nyamanini Virus Nucleoprotein and Phosphoprotein Organize Viral Inclusion Bodies That Associate with Host Biomolecular Condensates in the Nucleus.International journal of molecular sciences · 2023Article
- Nipah Virus Impairs Autocrine IFN Signaling by Sequestering STAT1 and STAT2 into Inclusion Bodies.Viruses · 2023Article
- Liquid Phase Partitioning in Virus Replication: Observations and Opportunities.Annual review of virology · 2022Review
- Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.Science advances · 2022Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of cytoplasmic inclusion bodies (IBs) is a hallmark of infections with non-segmented negative-strand RNA viruses (order Mononegavirales). We show here that Nipah virus (NiV), a bat-derived highly pathogenic member of the Paramyxoviridae family, differs from mononegaviruses of the Rhabdo-, Filo- and Pneumoviridae families by forming two types of IBs with distinct localizations, formation kinetics, and protein compositions. IBs in the perinuclear region form rapidly upon expression of the nucleocapsid proteins. These IBperi are highly mobile and associate with the aggresome marker y-tubulin. IBperi can recruit unrelated overexpressed cytosolic proteins but do not contain the viral matrix (M) protein. Additionally, NiV forms an as yet undescribed IB population at the plasma membrane (IBPM) that is y-tubulin-negative but contains the M protein. Infection studies with recombinant NiV revealed that IBPM require the M protein for their formation, and most likely represent sites of NiV assembly and budding. The identification of this novel type of plasma membrane-associated IBs not only provides new insights into NiV biology and may open new avenues to develop novel antiviral approaches to treat these highly pathogenic viruses, it also provides a basis for a more detailed characterization of IBs and their role in virus assembly and replication in infections with other Mononegavirales.
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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.