ArticleNature microbiology2025
Molecular organization of the New World arenavirus spike glycoprotein complex.
Article in Nature microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed.
- Junín virus and Argentine haemorrhagic fever: Virology, pathogenesis, diagnosis, and prevention strategies.World journal of virology · 2026Review
- Immunogenicity of recombinant vesicular stomatitis virus-vectored vaccines expressing the Machupo virus glycoprotein in different genome positions.Journal of virology · 2026Article
- Emerging Mammarenaviruses in Wildlife: Expanding Host Range and Implications.Animals : an open access journal from MDPI · 2026Review
- Structures of New World mammarenavirus glycoproteins as targets for antibody-mediated neutralization.Journal of virology · 2026Review
- Target-driven machine learning-enabled virtual screening (TAME-VS) enables prioritization of AKR1C3 inhibitors.Communications chemistry · 2026Article
- Development and protective evaluation of mRNA vaccines encoding the glycoprotein precursor of lymphocytic choriomeningitis virus.Virus research · 2026Article
- Development of a Conditional Replication System Using a Lassa Virus Glycoprotein Complex-Encoding Retroviral Vector for Isolating Resistant Variants to Inhibitors in BSL-2.International journal of molecular sciences · 2026Article
- HIV infection reprogrammes CD4+ T cells for quiescence and entry into proviral latency.Nature microbiology · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Of the multiple arenaviruses that cause haemorrhagic fevers in the Americas, all lack reliable therapeutic options, and only one has a vaccine. The arenavirus glycoprotein complex (GPC) binds cellular receptors and mediates pH-dependent fusion of viral and host cell membranes during entry. GPC comprises GP1, GP2 and stable signal peptide (SSP) subunits. SSP remains associated with the mature glycoprotein complex and regulates pH-dependent membrane fusion through an unclear mechanism. We report cryo-EM structures of Junin virus and Machupo virus GPC stabilized in the prefusion conformation using an amino acid substitution in the transmembrane region of SSP at 3.0 Å and 2.9 Å resolution, respectively. Mutational analyses, cell-cell fusion assays and molecular dynamics simulations reveal how contacts in the membrane-proximal and transmembrane regions of GPC regulate pH-dependent membrane fusion. The structures may aid in the design of therapeutic antibody cocktails, small-molecule inhibitors and vaccines against arenaviruses.
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What OpenQuestion holds
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.