ArticleJournal of virology2008
pH-induced activation of arenavirus membrane fusion is antagonized by small-molecule inhibitors.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 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.
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Who cites it
69 citing papers in PubMed, 103 citations in OpenAlex.
- 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
- Phospho-activated non-muscle myosin IIA heavy chain supports different mechanisms of virus uptake.Journal of virology · 2025Article
- Molecular organization of the New World arenavirus spike glycoprotein complex.Nature microbiology · 2025Article
- Animal Models of Pathogenic New World Arenaviruses.Microorganisms · 2025Review
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- 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
- Hexestrol, an estrogen receptor agonist, inhibits Lassa virus entry.Journal of virology · 2024Article
- A Salt Bridge and Disulfide Bond within the Lassa Virus Fusion Domain Are Required for the Initiation of Membrane Fusion.ACS omega · 2024Article
- Entry inhibitors as arenavirus antivirals.Frontiers in microbiology · 2024Review
- Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity.PLoS pathogens · 2023Article
- 50 Years of Lassa Fever Research.Current topics in microbiology and immunology · 2023Article
- The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023Article
- Host-Associated Distribution of Two Novel Mammarenaviruses in Rodents from Southern Africa.Viruses · 2022Article
- Screening and Identification of Lassa Virus Entry Inhibitors from a Fragment-Based Drug Discovery Library.Viruses · 2022Article
- Lassa antiviral LHF-535 protects guinea pigs from lethal challenge.Scientific reports · 2022Article
- CD164 is a host factor for lymphocytic choriomeningitis virus entry.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The late endosome-resident lipid bis(monoacylglycero)phosphate is a cofactor for Lassa virus fusion.PLoS pathogens · 2021Article
- Second-Generation Live-Attenuated Candid#1 Vaccine Virus Resists Reversion and Protects against Lethal Junín Virus Infection in Guinea Pigs.Journal of virology · 2021Article
- Characterizing the Lassa Virus Envelope Glycoprotein Membrane Proximal External Region for Its Role in Fusogenicity.Virologica Sinica · 2021Article
- Screening of Botanical Drugs against Lassa Virus Entry.Journal of virology · 2021Article
9 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
4 authors at 2 institutions in 1 country.
Funding
Abstract
The arenavirus envelope glycoprotein (GPC) mediates viral entry through pH-induced membrane fusion in the endosome. This crucial process in the viral life cycle can be specifically inhibited in the New World arenaviruses by the small-molecule compound ST-294. Here, we show that ST-294 interferes with GPC-mediated membrane fusion by targeting the interaction of the G2 fusion subunit with the stable signal peptide (SSP). We demonstrate that amino acid substitutions at lysine-33 of the Junín virus SSP confer resistance to ST-294 and engender de novo sensitivity to ST-161, a chemically distinct inhibitor of the Old World Lassa fever virus. These compounds, as well as a broadly active inhibitor, ST-193, likely share a molecular target at the SSP-G2 interface. We also show that both ST-294 and ST-193 inhibit pH-induced dissociation of the G1 receptor-binding subunit from GPC, a process concomitant with fusion activation. Interestingly, the inhibitory activity of these molecules can in some cases be overcome by further lowering the pH used for activation. Our results suggest that these small molecules act to stabilize the prefusion GPC complex against acidic pH. The pH-sensitive interaction between SSP and G2 in GPC represents a robust molecular target for the development of antiviral compounds for the treatment of arenavirus hemorrhagic fevers.
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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.