ArticleEuropean journal of cell biology
Nipah virus fusion protein: Importance of the cytoplasmic tail for endosomal trafficking and bioactivity.
Article in European journal of cell biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- The Silent Spillover Threat: Nipah Virus Epidemiology, Pathogenesis, Clinical Manifestations, and Advances in Therapeutics and Vaccine Development.Microorganisms · 2026Review
- Nipah Virus Encephalitis: Pathogenetic Aspects and Current Therapeutic Strategies.Pathogens (Basel, Switzerland) · 2026Review
- Functional and antigenic constraints on the Nipah virus fusion protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Functional and antigenic constraints on the Nipah virus fusion protein.bioRxiv : the preprint server for biology · 2026Article
- Beyond Processing: Furin as a Central Hub in Viral Pathogenesis and Genetic Susceptibility.Biomolecules · 2025Review
- Unveiling emerging threats: Langya and Mojiang-A dance with unfamiliar foes.Infectious diseases & immunity · 2025Review
- Cell-Free Expression of Nipah Virus Transmembrane Proteins for Proteoliposome Vaccine Design.ACS nano · 2025Article
- Emerging Nipah Virus With Pandemic Potential and High Mortality Rates: Is the Scientific Community Learning From Former Pandemics?Reviews in medical virology · 2025Review
- Uncovering human kinase substrates in nipah proteome.Frontiers in bioinformatics · 2025Article
- An Updated Review on Nipah Virus Infection with a Focus on Encephalitis, Vasculitis, and Therapeutic Approaches.Current topics in medicinal chemistry · 2025Review
- Nipah virus: epidemiology, pathogenesis, treatment, and prevention.Frontiers of medicine · 2024Review
- Development of Fusion-Based Assay as a Drug Screening Platform for Nipah Virus Utilizing Baculovirus Expression Vector System.International journal of molecular sciences · 2024Article
- Aptamers: precision tools for diagnosing and treating infectious diseases.Frontiers in cellular and infection microbiology · 2024Review
- Genomic characterization, transcriptome analysis, and pathogenicity of the Nipah virus (Indian isolate).Virulence · 2023Article
- In silico designing of an epitope-based peptide vaccine cocktail against Nipah virus: an Indian population-based epidemiological study.Archives of microbiology · 2023Article
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- YLMY Tyrosine Residue within the Cytoplasmic Tail of Newcastle Disease Virus Fusion Protein Regulates Its Surface Expression to Modulate Viral Budding and Pathogenicity.Microbiology spectrum · 2021Article
- Article
- Predicting and designing therapeutics against the Nipah virus.PLoS neglected tropical diseases · 2019Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nipah virus (NiV) is a highly pathogenic paramyxovirus which encodes two surface glycoproteins: the receptor-binding protein G and the fusion protein F. As for all paramyxoviruses, proteolytic activation of the NiV-F protein is an indispensable prerequisite for viral infectivity. Interestingly, proteolytic activation of NiV-F differs principally from other paramyxoviruses with respect to protease usage (cathepsins instead of trypsin- or furin-like proteases), and the subcellular localization where cleavage takes place (endosomes instead of Golgi or plasma membrane). To allow efficient F protein activation needed for productive virus replication and cell-to-cell fusion, the NiV-F cytoplasmic tail contains a classical tyrosine-based endocytosis signal (Y525RSL) that we have shown earlier to be needed for F uptake and proteolytic activation. In this report, we furthermore revealed that an intact endocytosis signal alone is not sufficient for full bioactivity. The very C-terminus of the cytoplasmic tail is needed in addition. Deletions of more than four residues did not affect F uptake or endosomal cleavage but downregulated the surface expression, likely by delaying the intracellular trafficking through endosomal-recycling compartments. Given that the NiV-F cytoplasmic tail is needed for timely and correct intracellular trafficking, endosomal cleavage and fusion activity, the influence of tail truncations on NiV-mediated cell-to-cell fusion and on pseudotyping lentiviral vectors is discussed.
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