ArticleJournal of virology2017
GRP78 Is an Important Host Factor for Japanese Encephalitis Virus Entry and Replication in Mammalian Cells.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed, 172 citations in OpenAlex.
- GRP78 dysregulation: A proposed molecular mechanism linking the tumor microenvironment to sepsis susceptibility in patients with cancer (Review).International journal of molecular medicine · 2026Review
- Identification of GRP78 as a novel host factor that facilitates zoonotic porcine deltacoronavirus internalization and replication via clathrin-mediated endocytosis.Journal of virology · 2026Article
- GRP78 promotes rabies virus entry through interacting with viral receptors.Journal of virology · 2026Article
- Downmodulation of cholesterol biosynthetic network governs activation of the innate immune response to Japanese encephalitis virus infection.Journal of virology · 2026Article
- Annexin A2 facilitates Japanese encephalitis virus replication by regulating endocytosis and intracellular transport in PK15 cells.Frontiers in microbiology · 2026Article
- Endophilin mediated endocytosis and epidermal growth factor receptor govern Japanese encephalitis virus entry and infection in neuronal cells.PLoS pathogens · 2025Article
- Advances and Challenges in Vaccination and Therapeutic Strategies Against Japanese Encephalitis Virus.Pathogens (Basel, Switzerland) · 2025Review
- HSPA5, a Host Cellular Heat-Shock Protein Required for Influenza a Virus Replication.International journal of molecular sciences · 2025Article
- Telmisartan, an anti-hypertensive drug, impedes JEV infection, possibly via the AT1/PPARγ axis.Microbiology spectrum · 2025Article
- Unraveling the complexities of neurotropic virus infection and immune evasion.Microbiology and molecular biology reviews : MMBR · 2025Review
- Transcriptomic response of mosquitoes to Japanese encephalitis virus and identification of its potential entry factors.Npj viruses · 2025Article
- Deciphering core genetic and pathway signatures of Japanese encephalitis virus using transcriptomics.Virusdisease · 2025Article
- LncRNAJournal of virology · 2025Article
- Increased expression of chaperone proteins in response to DENV 2 infection of Huh-7 liver cells.PloS one · 2025Article
- Screening and identification of protein interacting with goose astrovirus.Frontiers in cellular and infection microbiology · 2025Article
- Host Factor Rab4b PromotesMicroorganisms · 2024Article
- Hepatitis E Virus: What More Do We Need to Know?Medicina (Kaunas, Lithuania) · 2024Review
- SARS-CoV-2 Spike Protein-Derived Cyclic Peptides as Modulators of Spike Interaction with GRP78.Chembiochem : a European journal of chemical biology · 2024Article
- Sialic acids as attachment factors in mosquitoes mediating Japanese encephalitis virus infection.Journal of virology · 2024Article
- The interaction of GRP78 and Zika virus E and NS1 proteins occurs in a chaperone-client manner.Scientific reports · 2024Article
39 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Japanese encephalitis virus (JEV), a mosquito-borne flavivirus, is the leading cause of viral encephalitis in Southeast Asia with potential to become a global pathogen. Here, we identify glucose-regulated protein 78 (GRP78) as an important host protein for virus entry and replication. Using the plasma membrane fractions from mouse neuronal (Neuro2a) cells, mass spectroscopy analysis identified GRP78 as a protein interacting with recombinant JEV envelope protein domain III. GRP78 was found to be expressed on the plasma membranes of Neuro2a cells, mouse primary neurons, and human epithelial Huh-7 cells. Antibodies against GRP78 significantly inhibited JEV entry in all three cell types, suggesting an important role of the protein in virus entry. Depletion of GRP78 by small interfering RNA (siRNA) significantly blocked JEV entry into Neuro2a cells, further supporting its role in virus uptake. Immunofluorescence studies showed extensive colocalization of GRP78 with JEV envelope protein in virus-infected cells. This interaction was also confirmed by immunoprecipitation studies. Additionally, GRP78 was shown to have an important role in JEV replication, as treatment of cells post-virus entry with subtilase cytotoxin that specifically cleaved GRP78 led to a substantial reduction in viral RNA replication and protein synthesis, resulting in significantly reduced extracellular virus titers. Our results indicate that GRP78, an endoplasmic reticulum chaperon of the HSP70 family, is a novel host factor involved at multiple steps of the JEV life cycle and could be a potential therapeutic target.
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