ArticleProceedings of the National Academy of Sciences of the United States of America2011
X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 86 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.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
86 citing papers in PubMed, 123 citations in OpenAlex.
- In silico prioritization and cheminformatics identify structurally diverse small-molecule inhibitors of Lassa virus glycoprotein-mediated membrane fusion.SLAS discovery : advancing life sciences R & D · 2026Article
- Structures of New World mammarenavirus glycoproteins as targets for antibody-mediated neutralization.Journal of virology · 2026Review
- CD164 is an endolysomal host factor for entry of Clade A New World Arenaviruses.bioRxiv : the preprint server for biology · 2026Article
- Prediction of pre- and postfusion conformations of class I fusion proteins with AlphaFold2.PloS one · 2026Article
- Human endogenous retrovirus K (HERV-K) envelope structures in pre- and postfusion by cryo-EM.Science advances · 2025Article
- The Biological Characteristics and Mouse Model of Lassa Virus From the First Imported Case in China.MedComm · 2025Article
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- Architectural organization andJournal of virology · 2024Article
- Hexestrol, an estrogen receptor agonist, inhibits Lassa virus entry.Journal of virology · 2024Article
- Chapare virus infection and current perspectives on dentistry.Clinical oral investigations · 2024Review
- Understanding the Neurotrophic Virus Mechanisms and Their Potential Effect on Systemic Lupus Erythematosus Development.Brain sciences · 2024Review
- Cleavage-intermediate Lassa virus trimer elicits neutralizing responses, identifies neutralizing nanobodies, and reveals an apex-situated site-of-vulnerability.Nature communications · 2024Article
- The underlying mechanisms of arenaviral entry through matriglycan.Frontiers in molecular biosciences · 2024Review
- Envelope Recombination: A Major Driver in Shaping Retroviral Diversification and Evolution within the Host Genome.Viruses · 2023Review
- Design, Synthesis, and Biological Evaluation of Benzimidazole Derivatives as Potential Lassa Virus Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- Development of a new drug candidate for the inhibition of Lassa virus glycoprotein and nucleoprotein by modification of evodiamine as promising therapeutic agents.Frontiers in microbiology · 2023Article
- Review
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- Lassa virus glycoprotein complex review: insights into its unique fusion machinery.Bioscience reports · 2022Review
26 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issuedVonhrein, Clemens [corrected to Vonrhein, Clemens]
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arenaviruses are important agents of zoonotic disease worldwide. The virions expose a tripartite envelope glycoprotein complex at their surface, formed by the glycoprotein subunits GP1, GP2 and the stable signal peptide. This complex is responsible for binding to target cells and for the subsequent fusion of viral and host-cell membranes for entry. During this process, the acidic environment of the endosome triggers a fusogenic conformational change in the transmembrane GP2 subunit of the complex. We report here the crystal structure of the recombinant GP2 ectodomain of the lymphocytic choriomeningitis virus, the arenavirus type species, at 1.8-Å resolution. The structure shows the characteristic trimeric coiled coil present in class I viral fusion proteins, with a central stutter that allows a close structural alignment with most of the available structures of class I and III viral fusion proteins. The structure further shows a number of intrachain salt bridges stabilizing the postfusion hairpin conformation, one of which involves an aspartic acid that appears released from a critical interaction with the stable signal peptide upon low pH activation.
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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.