ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed, 117 citations in OpenAlex.
- A potent Gc neutralizing antibody reveals architecture-dependent bispecific protection against SFTSV.Emerging microbes & infections · 2026Article
- Preparation and characterization of the affinity and neutralization abilities of human monoclonal antibodies against bunyavirus SFTSV glycoprotein C.Infectious medicine · 2026Article
- Exploring SNPs in viral entry-related protein genes and their association with severe fever with thrombocytopenia syndrome virus infection risk.Microbiology spectrum · 2026Article
- Effectiveness of lignans against severe fever with thrombocytopenia syndrome virus infection.Virologica Sinica · 2026Article
- Recombinant Dabie bandavirus as a bivalent vaccine platform inducing protective immunity against intracellular pathogens and cancer.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Structural basis for recognition of Rift Valley fever virus Gn protein by a human neutralizing monoclonal antibody with a kappa light chain.PLoS pathogens · 2026Article
- Antibody engineering for SFTS treatment: frontier progress and translational challenges.Frontiers in microbiology · 2026Review
- Article
- Weakened invasion of severe fever with thrombocytopenia syndrome bunyavirus beneficial to its immune escape by multi-site mutation of glycoprotein.Molecular genetics and genomics : MGG · 2025Article
- Current status of severe fever with thrombocytopenia syndrome in China (Review).International journal of molecular medicine · 2025Review
- Identification of Licoflavone C as a cap-dependent endonuclease inhibitor against severe fever with thrombocytopenia syndrome virus.Acta pharmacologica Sinica · 2025Article
- Article
- Research Progress on the Gc Proteins of Akabane Virus.Veterinary sciences · 2025Review
- Article
- The Role of Orthobunyavirus Glycoprotein Gc in the Viral Life Cycle: From Viral Entry to Egress.Molecules (Basel, Switzerland) · 2025Review
- Article
- N6-methyladenosine RNA modification promotes Severe Fever with Thrombocytopenia Syndrome Virus infection.PLoS pathogens · 2024Article
- Adenovirus type 5-expressing Gn induces better protective immunity than Gc against SFTSV infection in mice.NPJ vaccines · 2024Article
- Bispecific antibodies targeting two glycoproteins on SFTSV exhibit synergistic neutralization and protection in a mouse model.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification and characterization of three monoclonal antibodies targeting the SFTSV glycoprotein and displaying a broad spectrum recognition of SFTSV-related viruses.PLoS neglected tropical diseases · 2024Article
20 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
8 authors at 2 institutions in 1 country.
Funding
Abstract
An emergent viral pathogen termed severe fever with thrombocytopenia syndrome virus (SFTSV) is responsible for thousands of clinical cases and associated fatalities in China, Japan, and South Korea. Akin to other phleboviruses, SFTSV relies on a viral glycoprotein, Gc, to catalyze the merger of endosomal host and viral membranes during cell entry. Here, we describe the postfusion structure of SFTSV Gc, revealing that the molecular transformations the phleboviral Gc undergoes upon host cell entry are conserved with otherwise unrelated alpha- and flaviviruses. By comparison of SFTSV Gc with that of the prefusion structure of the related Rift Valley fever virus, we show that these changes involve refolding of the protein into a trimeric state. Reverse genetics and rescue of site-directed histidine mutants enabled localization of histidines likely to be important for triggering this pH-dependent process. These data provide structural and functional evidence that the mechanism of phlebovirus-host cell fusion is conserved among genetically and patho-physiologically distinct viral pathogens.
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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.