ArticleNature communications2023
Cryo-EM structure of severe fever with thrombocytopenia syndrome virus.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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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.
The trial behind it
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Who cites it
40 citing papers in PubMed.
- A potent Gc neutralizing antibody reveals architecture-dependent bispecific protection against SFTSV.Emerging microbes & infections · 2026Article
- Evaluation of new adjuvants in enhancing the immune response to a candidate of Severe Fever with Thrombocytopenia Syndrome Virus vaccine.bioRxiv : the preprint server for biology · 2026Article
- Phylogeographic epidemiology of Dabie bandavirus in East Asia: divergent transmission networks and genotype‑linked clinical severity.Infectious diseases of poverty · 2026Article
- Genotype-Specific Amino Acid Signatures in the Gn/Gc Glycoprotein of Severe Fever with Thrombocytopenia Syndrome Virus Associated with Neurological Symptoms.Pathogens (Basel, Switzerland) · 2026Article
- Preparation and characterization of the affinity and neutralization abilities of human monoclonal antibodies against bunyavirus SFTSV glycoprotein C.Infectious medicine · 2026Article
- Phylogenetic and biological features of severe fever with thrombocytopenia syndrome virus from multi-species infections in eastern China.Microbiology spectrum · 2026Article
- Temperature-dependent infectious stability of Severe fever with thrombocytopenia syndrome virus.The Journal of veterinary medical science · 2026Article
- Human 3D liver spheroids support productive infection of a novel tick-borne phenuivirus.One health (Amsterdam, Netherlands) · 2026Article
- Unraveling the complexities: A comprehensive review of severe fever with thrombocytopenia syndrome and its associated complications.iScience · 2026Review
- Immune Cells at the Frontline of SFTSV Infection.Journal of microbiology and biotechnology · 2026Review
- Antibody engineering for SFTS treatment: frontier progress and translational challenges.Frontiers in microbiology · 2026Review
- Research progress on antiviral drugs and vaccines for severe fever with thrombocytopenia syndrome.Frontiers in immunology · 2026Review
- Multidimensional mechanisms of SFTSV-host interactions: viral protein functions, mFrontiers in cellular and infection microbiology · 2026Review
- Cryo-EM structure of the Rift Valley fever virus envelope protein in complex with a potent neutralization antibody.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A single-chain mRNA vaccine co-expressing GPC and NP provides complete protection against lethal Dabie bandavirus challenge in mice.Molecular therapy. Nucleic acids · 2025Article
- A viral codon usage strategy enhances antigen production and protection in SFTSV mRNA vaccination.NPJ vaccines · 2025Article
- Article
- Current status of severe fever with thrombocytopenia syndrome in China (Review).International journal of molecular medicine · 2025Review
- Recent Advances in Humoral Immunity Dysregulation in Severe Fever With Thrombocytopenia Syndrome Virus (SFTSV) Infection: A Systematic Review.Health science reports · 2025Article
- Sustained humoral immunity in the patients recovered from severe fever with thrombocytopenia syndrome.Tropical medicine and health · 2025Article
Corrections and comments
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Authors and funding
24 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The severe fever with thrombocytopenia syndrome virus (SFTSV) is a tick-borne human-infecting bunyavirus, which utilizes two envelope glycoproteins, Gn and Gc, to enter host cells. However, the structure and organization of these glycoproteins on virion surface are not yet known. Here we describe the structure of SFTSV determined by single particle reconstruction, which allows mechanistic insights into bunyavirus assembly at near-atomic resolution. The SFTSV Gn and Gc proteins exist as heterodimers and further assemble into pentameric and hexameric peplomers, shielding the Gc fusion loops by both intra- and inter-heterodimer interactions. Individual peplomers are associated mainly through the ectodomains, in which the highly conserved glycans on N914 of Gc play a crucial role. This elaborate assembly stabilizes Gc in the metastable prefusion conformation and creates some cryptic epitopes that are only accessible in the intermediate states during virus entry. These findings provide an important basis for developing vaccines and therapeutic drugs.
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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.