ArticleJournal of virology2023
HSPA5 Promotes Attachment and Internalization of Porcine Epidemic Diarrhea Virus through Interaction with the Spike Protein and the Endo-/Lysosomal Pathway.
Article in Journal of virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 20 citations in OpenAlex.
- GPNMB promotes double-membrane vesicle accumulation and facilitates structural protein transport during PEDV infection.Virulence · 2026Article
- Neutralizing nanobodies against porcine epidemic diarrhea virus: discovery and characterization.BMC veterinary research · 2026Article
- Identification of GRP78 as a novel host factor that facilitates zoonotic porcine deltacoronavirus internalization and replication via clathrin-mediated endocytosis.Journal of virology · 2026Article
- The cholesterol transporter Niemann-Pick C1 facilitates the entry of porcine epidemic diarrhea coronavirus.Journal of virology · 2026Article
- A colloidal gold immunochromatographic test strip based on McAbs anti-S protein to detect porcine epidemic diarrhea virus.Microbiology spectrum · 2026Article
- MCL1 promotes porcine epidemic diarrhea virus replication by modulating arachidonic acid metabolic pathway.PLoS pathogens · 2026Article
- Cell entry mechanisms of porcine enteric coronaviruses.The Journal of biological chemistry · 2026Review
- Heat shock proteins at the crossroads of endosomal trafficking pathways.Cell biology and toxicology · 2025Review
- HSPA5, a Host Cellular Heat-Shock Protein Required for Influenza a Virus Replication.International journal of molecular sciences · 2025Article
- Cav1.2 facilitates the binding and internalisation of porcine epidemic diarrhoea virus.Veterinary research · 2025Article
- Heat Shock Protein 70 in Cold-Stressed Farm Animals: Implications for Viral Disease Seasonality.Microorganisms · 2025Review
- The biomechanical phenomena observed in the cell invasion pathway of porcine epidemic diarrhea virus: a review.Archives of virology · 2025Review
- Heat shock protein A1 inhibits the replication of foot-and-mouth disease virus by degrading viral RNA polymerase 3D through chaperone-mediated autophagy.Journal of virology · 2025Article
- Class B scavenger receptor resists WSSV replication by recognizing the viral lipid molecule and promoting phagocytosis.Journal of virology · 2025Article
- RNASEK interacting with PEDV structural proteins facilitates virus entry via clathrin-mediated endocytosis.Journal of virology · 2025Article
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- Proteomic Profile of Circulating Extracellular Vesicles in the Brain after Δ9-Tetrahydrocannabinol Inhalation.Biomolecules · 2024Article
- Cell-surface d-glucuronyl C5-epimerase binds to porcine deltacoronavirus spike protein facilitating viral entry.Journal of virology · 2024Article
- HSP70 positively regulates translation by interacting with the IRES and stabilizes the viral structural proteins VP1 and VP3 to facilitate duck hepatitis A virus type 1 replication.Veterinary research · 2024Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine epidemic diarrhea virus (PEDV) has caused huge economic losses to the global pig industry. The swine enteric coronavirus spike (S) protein recognizes various cell surface molecules to regulate viral infection. In this study, we identified 211 host membrane proteins related to the S1 protein by pulldown combined with liquid-chromatography tandem mass spectrometry (LC-MS/MS) analysis. Among these, heat shock protein family A member 5 (HSPA5) was identified through screening as having a specific interaction with the PEDV S protein, and positive regulation of PEDV infection was validated by knockdown and overexpression tests. Further studies verified the role of HSPA5 in viral attachment and internalization. In addition, we found that HSPA5 interacts with S proteins through its nucleotide-binding structural domain (NBD) and that polyclonal antibodies can block viral infection. In detail, HSPA5 was found to be involved in viral trafficking via the endo-/lysosomal pathway. Inhibition of HSPA5 activity during internalization would reduce the subcellular colocalization of PEDV with lysosomes in the endo-/lysosomal pathway. Together, these findings show that HSPA5 is a novel PEDV potential target for the creation of therapeutic drugs.
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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.