ArticleJournal of virology2006
N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
153 citing papers in PubMed, 198 citations in OpenAlex.
- Relevance of potential endocytosis motifs in Cedar virus glycoprotein G for its biological activity.Journal of virology · 2026Article
- The Silent Spillover Threat: Nipah Virus Epidemiology, Pathogenesis, Clinical Manifestations, and Advances in Therapeutics and Vaccine Development.Microorganisms · 2026Review
- Prevalence, molecular characterization and phylogenetic analysis of Newcastle disease virus isolated from domestic poultry during 2019-2024 in Egypt.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Structure-Function Correlations of Commercial Fucoidan Extracts: Antioxidant, Antiviral, Antifungal, Antibacterial and Prebiotic Activities.Molecules (Basel, Switzerland) · 2026Article
- The Nipah virus threat in India: Epidemiological trends, risk drivers, and lessons for pandemic preparedness.PLoS pathogens · 2026Review
- Strategically engineering an oncolytic herpes simplex virus to improve systemic delivery.Molecular therapy. Oncology · 2026Article
- Sulfur-containing class of broad-spectrum antivirals improves influenza virus vaccine development.Nature communications · 2026Article
- Broad-spectrum synthetic carbohydrate receptors (SCRs) inhibit viral entry across multiple virus families.Science advances · 2025Article
- Nipah virus: pathogenesis, genome, diagnosis, and treatment.Applied microbiology and biotechnology · 2025Review
- Unveiling emerging threats: Langya and Mojiang-A dance with unfamiliar foes.Infectious diseases & immunity · 2025Review
- Herpes simplex virus 1 envelope glycoprotein C shields glycoprotein D to protect virions from entry-blocking antibodies.Journal of virology · 2025Article
- Multi-platform omics analysis of Nipah virus infection reveals viral glycoprotein modulation of mitochondria.Cell reports · 2025Article
- Replication-incompetent VSV-based vaccine elicits protective responses against SARS-CoV-2 and influenza virus.Science advances · 2025Article
- Glycosylation as a strategic mechanism for measles virus and mumps virus immune evasion.Frontiers in immunology · 2025Review
- A monoclonal antibody targeting the Nipah virus fusion glycoprotein apex imparts protection from disease.Journal of virology · 2024Article
- Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses.Science advances · 2024Article
- Bats generate lower affinity but higher diversity antibody responses than those of mice, but pathogen-binding capacity increases if protein is restricted in their diet.PLoS biology · 2024Article
- Herpes Simplex Virus 1 Envelope Glycoprotein C Shields Glycoprotein D to Protect Virions from Entry-Blocking Antibodies.bioRxiv : the preprint server for biology · 2024Article
- Characterization and application of recombinant Bovine Leukemia Virus Env protein.Scientific reports · 2024Article
- Structural Studies of Henipavirus Glycoproteins.Viruses · 2024Review
93 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 2 institutions in 1 country.
Funding
Abstract
Nipah virus (NiV) is a deadly emerging paramyxovirus. The NiV attachment (NiV-G) and fusion (NiV-F) envelope glycoproteins mediate both syncytium formation and viral entry. Specific N-glycans on paramyxovirus fusion proteins are generally required for proper conformational integrity and biological function. However, removal of individual N-glycans on NiV-F had little negative effect on processing or fusogenicity and has even resulted in slightly increased fusogenicity. Here, we report that in both syncytium formation and viral entry assays, removal of multiple N-glycans on NiV-F resulted in marked increases in fusogenicity (>5-fold) but also resulted in increased sensitivity to neutralization by NiV-F-specific antisera. The mechanism underlying the hyperfusogenicity of these NiV-F N-glycan mutants is likely due to more-robust six-helix bundle formation, as these mutants showed increased fusion kinetics and were more resistant to neutralization by a fusion-inhibitory reagent based on the C-terminal heptad repeat region of NiV-F. Finally, we demonstrate that the fusogenicities of the NiV-F N-glycan mutants were inversely correlated with the relative avidities of NiV-F's interactions with NiV-G, providing support for the attachment protein "displacement" model of paramyxovirus fusion. Our results indicate that N-glycans on NiV-F protect NiV from antibody neutralization, suggest that this "shielding" role comes together with limiting cell-cell fusion and viral entry efficiencies, and point to the mechanisms underlying the hyperfusogenicity of these N-glycan mutants. These features underscore the varied roles that N-glycans on NiV-F play in the pathobiology of NiV entry but also shed light on the general mechanisms of paramyxovirus fusion with host cells.
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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.