ArticleJournal of virology2008
New world clade B arenaviruses can use transferrin receptor 1 (TfR1)-dependent and -independent entry pathways, and glycoproteins from human pathogenic strains are associated with the use of TfR1.
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 88 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
88 citing papers in PubMed, 117 citations in OpenAlex.
- Immunogenicity of recombinant vesicular stomatitis virus-vectored vaccines expressing the Machupo virus glycoprotein in different genome positions.Journal of virology · 2026Article
- Efficacy of an Fc-silent antibody targeting the apical domain of human transferrin receptor 1 in transgenic mouse models of Junín virus infection.Antiviral research · 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
- Comparison of Vaccine Platforms for Machupo Virus.Vaccines · 2026Article
- The placental battlefield: viral strategies and immune countermeasures.Frontiers in immunology · 2025Review
- The structure of the Lujo virus spike complex.Nature communications · 2024Article
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- Chapare virus infection and current perspectives on dentistry.Clinical oral investigations · 2024Review
- Novel Oliveros-like Clade CViruses · 2024Article
- An AAV capsid reprogrammed to bind human Transferrin Receptor mediates brain-wide gene delivery.bioRxiv : the preprint server for biology · 2023Article
- Structural and molecular biology of Sabiá virus.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity.PLoS pathogens · 2023Article
- Regulation of Stress-Activated Kinases in Response to Tacaribe Virus Infection and Its Implications for Viral Replication.Viruses · 2022Article
- Machupo Virus with Mutations in the Transmembrane Domain and Glycosylation Sites of the Glycoprotein Is Attenuated and Immunogenic in Animal Models of Bolivian Hemorrhagic Fever.Journal of virology · 2022Article
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- The late endosome-resident lipid bis(monoacylglycero)phosphate is a cofactor for Lassa virus fusion.PLoS pathogens · 2021Article
- Lassa Fever Virus Binds Matriglycan-A Polymer of Alternating Xylose and Glucuronate-On α-Dystroglycan.Viruses · 2021Review
28 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
7 authors at 1 institution in 1 country.
Funding
Abstract
Arenaviruses are rodent-borne viruses, with five members of the family capable of causing severe hemorrhagic fevers if transmitted to humans. To date, two distinct cellular receptors have been identified that are used by different pathogenic viruses, alpha-dystroglycan by Lassa fever virus and transferrin receptor 1 (TfR1) by certain New World clade B viruses. Our previous studies have suggested that other, as-yet-unknown receptors are involved in arenavirus entry. In the present study, we examined the use of TfR1 by the glycoproteins (GPs) from a panel of New World clade B arenaviruses comprising three pathogenic and two nonpathogenic strains. Interestingly, we found that TfR1 was only used by the GPs from the pathogenic viruses, with entry of the nonpathogenic strains being TfR1 independent. The pathogenic GPs could also direct entry into cells by TfR1-independent pathways, albeit less efficiently. A comparison of the abilities of TfR1 orthologs from different species to support arenavirus entry found that the human and feline receptors were able to enhance entry of the pathogenic strains, but that neither the murine or canine forms were functional. Since the ability to use TfR1 is a characteristic feature of the human pathogens, this interaction may represent an important target in the treatment of New World hemorrhagic fevers. In addition, the ability to use TfR1 may be a useful tool to predict the likelihood that any existing or newly discovered viruses in this family could infect humans.
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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.