ArticlePLoS pathogens2024
N-glycosylation of viral glycoprotein is a novel determinant for the tropism and virulence of highly pathogenic tick-borne bunyaviruses.
Article in PLoS pathogens, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The S32 amino acid deletion in the GP5 protein modulates the infectivity of porcine reproductive and respiratory syndrome virus.Virulence · 2026Article
- Comparison of the pathogenicity in type I interferon receptor deficient A129 mice and characterization of amino acid substitutions among severe fever with thrombocytopenia syndrome virus strains.The Journal of veterinary medical science · 2026Article
- Article
- SFTSV: a priority pathogen in need of a cure-reviewing the therapeutic.Archives of microbiology · 2026Review
- Research progress on emerging and important Tick-Borne pathogens.Frontiers in microbiology · 2026Review
- The roles of post-translational modifications in the pathogenesis of RNA viruses: allies or adversaries?Frontiers in microbiology · 2026Review
- The glycosylation variant at residue 381 of the spike protein contributes to virulence shifts in porcine epidemic diarrhea virus during both natural field transmission and laboratory cell passaging with poor cross-protection.Journal of virology · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Severe fever with thrombocytopenia syndrome (SFTS) virus, a tick-borne bunyavirus, causes a severe/fatal disease termed SFTS; however, the viral virulence is not fully understood. The viral non-structural protein, NSs, is the sole known virulence factor. NSs disturbs host innate immune responses and an NSs-mutant SFTS virus causes no disease in an SFTS animal model. The present study reports a novel determinant of viral tropism as well as virulence in animal models, within the glycoprotein (GP) of SFTS virus and an SFTS-related tick-borne bunyavirus. Infection with mutant SFTS viruses lacking the N-linked glycosylation of GP resulted in negligible usage of calcium-dependent lectins in cells, less efficient infection, high susceptibility to a neutralizing antibody, low cytokine production in macrophage-like cells, and reduced virulence in Ifnar-/- mice, when compared with wildtype virus. Three SFTS virus-related bunyaviruses had N-glycosylation motifs at similar positions within their GP and a glycan-deficient mutant of Heartland virus showed in vitro and in vivo phenotypes like those of the SFTS virus. Thus, N-linked glycosylation of viral GP is a novel determinant for the tropism and virulence of SFTS virus and of a related virus. These findings will help us understand the process of severe/fatal diseases caused by tick-borne bunyaviruses.
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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.