ArticlePLoS pathogens2016
Crystal Structure of Glycoprotein C from a Hantavirus in the Post-fusion Conformation.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- Prefusion-stabilized Hantaan virus glycoprotein nucleic acid vaccine elicits potent neutralizing antibody responses via germinal center activation.Nature communications · 2026Article
- Interactions Between Hantavirus Nucleoprotein and Glycoproteins: A Quantitative Fluorescence Microscopy Study.Viruses · 2025Article
- Puumala orthohantavirus: prevalence, biology, disease, animal models and recent advances in therapeutics development and structural biology.Frontiers in immunology · 2025Review
- Production and Purification of Hantavirus Glycoproteins in Drosophila melanogaster S2 Cells.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Expression and Purification of RVFV Glycoprotein C for Structural Studies Using Baculovirus Expression System.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Rift Valley Fever Virus-Infection, Pathogenesis and Host Immune Responses.Pathogens (Basel, Switzerland) · 2023Review
- Mechanistic basis for potent neutralization of Sin Nombre hantavirus by a human monoclonal antibody.Nature microbiology · 2023Article
- Structural and mechanistic basis of neutralization by a pan-hantavirus protective antibody.Science translational medicine · 2023Article
- Antigenic mapping and functional characterization of human New World hantavirus neutralizing antibodies.eLife · 2023Article
- Pseudotyped Viruses for Orthohantavirus.Advances in experimental medicine and biology · 2023Article
- Evolution and activation mechanism of the flavivirus class II membrane-fusion machinery.Nature communications · 2022Article
- Human antibody recognizing a quaternary epitope in the Puumala virus glycoprotein provides broad protection against orthohantaviruses.Science translational medicine · 2022Article
- Cryo-EM structure of glycoprotein C from Crimean-Congo hemorrhagic fever virus.Virologica Sinica · 2022Article
- Structural basis of synergistic neutralization of Crimean-Congo hemorrhagic fever virus by human antibodies.Science (New York, N.Y.) · 2022Article
- Article
- Review
- The Bunyavirales: The Plant-Infecting Counterparts.Viruses · 2021Review
- Broad and potently neutralizing monoclonal antibodies isolated from human survivors of New World hantavirus infection.Cell reports · 2021Article
- Differential pathogenesis between Andes virus strains CHI-7913 and Chile-9717869in Syrian Hamsters.Journal of virology · 2021Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Hantaviruses are important emerging human pathogens and are the causative agents of serious diseases in humans with high mortality rates. Like other members in the Bunyaviridae family their M segment encodes two glycoproteins, GN and GC, which are responsible for the early events of infection. Hantaviruses deliver their tripartite genome into the cytoplasm by fusion of the viral and endosomal membranes in response to the reduced pH of the endosome. Unlike phleboviruses (e.g. Rift valley fever virus), that have an icosahedral glycoprotein envelope, hantaviruses display a pleomorphic virion morphology as GN and GC assemble into spikes with apparent four-fold symmetry organized in a grid-like pattern on the viral membrane. Here we present the crystal structure of glycoprotein C (GC) from Puumala virus (PUUV), a representative member of the Hantavirus genus. The crystal structure shows GC as the membrane fusion effector of PUUV and it presents a class II membrane fusion protein fold. Furthermore, GC was crystallized in its post-fusion trimeric conformation that until now had been observed only in Flavi- and Togaviridae family members. The PUUV GC structure together with our functional data provides intriguing evolutionary and mechanistic insights into class II membrane fusion proteins and reveals new targets for membrane fusion inhibitors against these important pathogens.
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