ArticleNature structural & molecular biology2016
Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 80 citations in OpenAlex.
- Article
- Lymphocytic Choriomeningitis Virus Bearing GPC Mutations for Enhanced Tumor Tropism and Strong Anti-Tumor Activity.Viruses · 2026Article
- Structures of New World mammarenavirus glycoproteins as targets for antibody-mediated neutralization.Journal of virology · 2026Review
- Development and protective evaluation of mRNA vaccines encoding the glycoprotein precursor of lymphocytic choriomeningitis virus.Virus research · 2026Article
- Sulfated glycosaminoglycans inhibit LCMV entry and modulate antiviral immunity and pathology.EMBO molecular medicine · 2026Article
- Site-1 protease mediated GPC processing is required for persistence of LCMV Clone 13.Npj viruses · 2026Article
- Prediction of pre- and postfusion conformations of class I fusion proteins with AlphaFold2.PloS one · 2026Article
- Optimized arenaviruses with tumor-tropic mutations promote safe anti-tumor efficacy via sustainable immune modulatory properties.Cell reports. Medicine · 2025Article
- Molecular organization of the New World arenavirus spike glycoprotein complex.Nature microbiology · 2025Article
- In situ insights into antibody-mediated neutralization of a pre-fusion Junin virus glycoprotein complex.Cell reports · 2025Article
- Article
- Polyclonal B cells acquire LCMV antigens in a GP1-dependent manner.PLoS pathogens · 2025Article
- Architectural organization andJournal of virology · 2024Article
- Strategies of rational and structure-driven vaccine design for Arenaviruses.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2024Review
- High-Affinity-Mediated Viral Entry Triggers Innate Affinity Escape Resulting in Type I IFN Resistance and Impaired T Cell Immunity.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Article
- The underlying mechanisms of arenaviral entry through matriglycan.Frontiers in molecular biosciences · 2024Review
- Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity.PLoS pathogens · 2023Article
- Structural basis for antibody-mediated neutralization of lymphocytic choriomeningitis virus.Cell chemical biology · 2023Article
- The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1-GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1-GP2 complex of the prototypic arenavirus LCMV at 3.5 Å. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states.
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