ReviewViruses2012
The curious case of arenavirus entry, and its inhibition.
Review in Viruses, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
93 citing papers in PubMed, 139 citations in OpenAlex.
- Lassa Virus-A Persistent and Evolving Threat.Microorganisms · 2026Review
- Emerging Mammarenaviruses in Wildlife: Expanding Host Range and Implications.Animals : an open access journal from MDPI · 2026Review
- Understanding machupo virus: A neglected arenavirus with global health importance.World journal of virology · 2026Review
- Structures of New World mammarenavirus glycoproteins as targets for antibody-mediated neutralization.Journal of virology · 2026Review
- Genomic characterization of Sabiá virus in Brazil, 2019-2020: Implications for diagnostics, virus evolution, and receptor binding.PLoS neglected tropical diseases · 2026Article
- Polyclonal B cells acquire LCMV antigens in a GP1-dependent manner.PLoS pathogens · 2025Article
- Animal Models of Pathogenic New World Arenaviruses.Microorganisms · 2025Review
- Article
- Lassa virus protein-protein interactions as mediators of Lassa fever pathogenesis.Virology journal · 2025Review
- Pathogenesis of Chapare virus in cynomolgus macaques.EMI. Animal & environment · 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
- The structure of the Lujo virus spike complex.Nature communications · 2024Article
- Inactivated rabies-based Lassa fever virus vaccine candidate LASSARAB protects nonhuman primates from lethal disease.NPJ vaccines · 2024Article
- Identification of residues in Lassa virus glycoprotein 1 involved in receptor switch.Virologica Sinica · 2024Article
- Entry inhibitors as arenavirus antivirals.Frontiers in microbiology · 2024Review
- Article
- Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity.PLoS pathogens · 2023Article
- Deletion of the first glycosylation site promotes Lassa virus glycoprotein-mediated membrane fusion.Virologica Sinica · 2023Article
- The Feline Immunodeficiency Virus Envelope Signal Peptide Is a Tetherin Antagonizing Protein.mBio · 2023Article
- Vaccine Candidates against Arenavirus Infections.Vaccines · 2023Review
33 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
2 authors at 1 institution in 1 country.
Funding
Abstract
Arenaviruses comprise a diverse family of enveloped negative-strand RNA viruses that are endemic to specific rodent hosts worldwide. Several arenaviruses cause severe hemorrhagic fevers in humans, including Junín and Machupo viruses in South America and Lassa fever virus in western Africa. Arenavirus entry into the host cell is mediated by the envelope glycoprotein complex, GPC. The virion is endocytosed on binding to a cell-surface receptor, and membrane fusion is initiated in response to physiological acidification of the endosome. As with other class I virus fusion proteins, GPC-mediated membrane fusion is promoted through a regulated sequence of conformational changes leading to formation of the classical postfusion trimer-of-hairpins structure. GPC is, however, unique among the class I fusion proteins in that the mature complex retains a stable signal peptide (SSP) as a third subunit, in addition to the canonical receptor-binding and fusion proteins. We will review the curious properties of the tripartite GPC complex and describe evidence that SSP interacts with the fusion subunit to modulate pH-induced activation of membrane fusion. This unusual solution to maintaining the metastable prefusion state of GPC on the virion and activating the class I fusion cascade at acidic pH provides novel targets for antiviral intervention.
Indexed as
Identifiers
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.