ArticleFrontiers in microbiology2020
Heat Shock Protein Member 8 Is an Attachment Factor for Infectious Bronchitis Virus.
Article in Frontiers in microbiology, 2020. 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, 27 citations in OpenAlex.
- Monoclonal antibodies target conserved S1mBio · 2026Article
- HSPA5 induces autophagy targeting VP2 through the PERK-eIF2α signaling pathway to inhibit SVA replication.Journal of virology · 2026Article
- In-Depth Molecular Dynamics Simulations Reveal Ligand-Induced Modulations of the HSPA8-SARS-CoV-2 Spike Protein Interaction.International journal of molecular sciences · 2026Article
- Genes Encoding Heat Shock Proteins Are Associated with Risk and Clinical Course of Severe COVID-19: A Pilot Study.International journal of molecular sciences · 2025Article
- Article
- Characterization of bi-segmented and tri-segmented recombinant Pichinde virus particles.Journal of virology · 2024Article
- Mechanism and complex roles of HSC70/HSPA8 in viral entry.Virus research · 2024Review
- Cell-surface d-glucuronyl C5-epimerase binds to porcine deltacoronavirus spike protein facilitating viral entry.Journal of virology · 2024Article
- C1QTNF5 is a novel attachment factor that facilitates the entry of influenza A virus.Virologica Sinica · 2024Article
- A missense mutation in theFrontiers in neuroscience · 2024Article
- Review
- Expression of HSPA14 in patients with acute HIV-1 infection and its effect on HIV-1 replication.Frontiers in immunology · 2023Article
- Single-cell RNA-sequencing data analysis reveals a highly correlated triphasic transcriptional response to SARS-CoV-2 infection.Communications biology · 2022Article
- Heat Shock Protein Member 8 (HSPA8) Is Involved in Porcine Reproductive and Respiratory Syndrome Virus Attachment and Internalization.Microbiology spectrum · 2022Article
- Review
- Biologic correlates of beneficial convalescent plasma therapy in a COVID-19 patient reveal disease resolution mechanisms.medRxiv : the preprint server for health sciences · 2022Article
- The relation between avian coronaviruses and SARS-CoV-2 coronavirus.Frontiers in microbiology · 2022Review
- The Role of Chicken Prolactin, Growth Hormone and Their Receptors in the Immune System.Frontiers in microbiology · 2022Review
- Longitudinal Analysis of Biologic Correlates of COVID-19 Resolution: Case Report.Frontiers in medicine · 2022Article
- Anticancer Properties and Mechanism of Action of Oblongifolin C, Guttiferone K and Related Polyprenylated Acylphloroglucinols.Natural products and bioprospecting · 2021Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although infectious bronchitis virus (IBV) is the first coronavirus identified, little is known about which membrane protein of host cells could interact with IBV spike protein and facilitate the infection by the virus. In this study, by using a monoclonal antibody to the S1 protein of IBV M41 strain, we found that heat shock protein member 8 (HSPA8) could interact with spike protein of IBV. HSPA8 was found to be present on the cell membrane and chicken tissues, with highest expression level in the kidney. Results of co-IP and GST-pull-down assays indicated that the receptor binding domain (RBD) of IBV M41 could interact with HSPA8. The results of binding blocking assay and infection inhibition assay showed that recombinant protein HSPA8 and antibody to HSPA8 could inhibit IBV M41 infection of chicken embryonic kidney (CEK) cells. Further, we found that HSPA8 interacted with the N-terminal 19-272 amino acids of S1 of IBV Beaudette, H120 and QX strains and HSPA8 from human and pig also interacted with IBV M41-RBD. Finally the results of binding blocking assay and infection inhibition assay showed that recombinant HSPA8 protein and antibody to HSPA8 could inhibit IBV Beaudette strain infection of Vero cells that were treated with heparanase to remove heparan sulfate from the cell surface. Taken together, our results indicate that HSPA8 is a novel host factor involved in IBV infection.
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