ArticleNature communications2024
The low-density lipoprotein receptor promotes infection of multiple encephalitic alphaviruses.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 35 citations in OpenAlex.
- The residue 86 of the Getah virus E2 glycoprotein mediates both glycosaminoglycan- and LDLR-dependent infection.PLoS pathogens · 2026Article
- Clinical Manifestations and Immunological Impacts in Co-Infections and Sequential Infections of SARS-CoV-2 and Arboviruses.Current microbiology · 2026Review
- Review
- LRP4 is an entry receptor for multiple encephalitic alphaviruses.Nature communications · 2026Article
- Current status on encephalitic alphavirus vaccines development: Advances, challenges, and global health perspectives.Infectious medicine · 2026Review
- The low-density lipoprotein receptor LDLR mediates cellular entry of nonenveloped hepatitis A virus.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- VLDLR: A Multifunctional receptor in diverse pathophysiological processes.Cell communication and signaling : CCS · 2026Review
- Informed mutation of western equine encephalitis virus to heparan sulfate binding: Implications for rational design of alphavirus live attenuated vaccines.PLoS pathogens · 2026Article
- LRP1 facilitates Jamestown Canyon virus infection of neurons.Journal of virology · 2025Article
- Molecular basis of ApoER2-mediated Semliki Forest virus entry.Nature communications · 2025Article
- Western equine encephalitis virus: A comprehensive review of epidemics, transmission, hosts, and strategies for mitigation.Virulence · 2025Review
- LRP8 is an entry receptor for tick-borne encephalitis viruses.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Old World alphaviruses use distinct mechanisms to infect brain microvascular endothelial cells for neuroinvasion.Cell reports · 2025Article
- Cellular and molecular keys to entry: Mechanisms mediating Orthoflavivirus infection of the mosquito midgut.PLoS pathogens · 2025Article
- Unraveling the complexities of neurotropic virus infection and immune evasion.Microbiology and molecular biology reviews : MMBR · 2025Review
- Structural elucidation of a unique binding mode by an intact alphavirus human IgG molecule to a quaternary epitope.Nature communications · 2025Article
- Three positively charged binding sites on the eastern equine encephalitis virus E2 glycoprotein coordinate heparan sulfate- and protein receptor-dependent infection.Nature communications · 2025Article
- Basic patches on the E2 glycoprotein of eastern equine encephalitis virus influence viral vascular clearance and dissemination in mice.Journal of virology · 2025Article
- LDL receptor-mediated endocytosis ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Members of the low-density lipoprotein receptor (LDLR) family, including LDLRAD3, VLDLR, and ApoER2, were recently described as entry factors for different alphaviruses. However, based on studies with gene edited cells and knockout mice, blockade or abrogation of these receptors does not fully inhibit alphavirus infection, indicating the existence of additional uncharacterized entry factors. Here, we perform a CRISPR-Cas9 genome-wide loss-of-function screen in mouse neuronal cells with a chimeric alphavirus expressing the Eastern equine encephalitis virus (EEEV) structural proteins and identify LDLR as a candidate receptor. Expression of LDLR on the surface of neuronal or non-neuronal cells facilitates binding and infection of EEEV, Western equine encephalitis virus, and Semliki Forest virus. Domain mapping and binding studies reveal a low-affinity interaction with LA domain 3 (LA3) that can be enhanced by concatenation of LA3 repeats. Soluble decoy proteins with multiple LA3 repeats inhibit EEEV infection in cell culture and in mice. Our results establish LDLR as a low-affinity receptor for multiple alphaviruses and highlight a possible path for developing inhibitors that could mitigate infection and disease.
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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.