ArticlePLoS pathogens2020
Marine medaka heat shock protein 90ab1 is a receptor for red-spotted grouper nervous necrosis virus and promotes virus internalization through clathrin-mediated endocytosis.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 78 citations in OpenAlex.
- Small heat shock and J-domain proteins direct defense against areca palm velarivirus 1 by degrading coat protein via autophagy.Nature communications · 2026Article
- Marine medaka PKCα promotes red-spotted grouper nervous necrosis virus entry by orchestrating MYL3-mediated macropinocytosis and cofilin-dependent actin remodeling.Journal of virology · 2026Article
- Nervous necrosis virus capsid protein functions as a SUMO E3 ligase to activate MAVS-dependent NF-κB signaling.Cellular and molecular life sciences : CMLS · 2026Article
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- Characterizing Marine Medaka (Animals : an open access journal from MDPI · 2024Article
- Nectin1 is a pivotal host factor involved in attachment and entry of red-spotted grouper nervous necrosis virus in the early stages of the viral life cycle.Journal of virology · 2024Article
- Molecular Mechanism of pH-Induced Protrusion Configuration Switching in Piscine Betanodavirus Implies a Novel Antiviral Strategy.ACS infectious diseases · 2024Article
- The laminin receptor is a receptor forJournal of virology · 2024Article
- Slc43a2Science China. Life sciences · 2024Article
- HSP90AB1 Is a Host Factor Required for Transmissible Gastroenteritis Virus Infection.International journal of molecular sciences · 2023Article
- In vitro infection efficiency of nervous necrosis virus alters depending on amount of viral particles adsorbed onto cells.Scientific reports · 2023Article
- Ring Finger Protein 34 Facilitates Nervous Necrosis Virus Evasion of Antiviral Innate Immunity by Targeting TBK1 and IRF3 for Ubiquitination and Degradation in Teleost Fish.Journal of virology · 2023Article
- Role of heat shock protein 90 as an antiviral target for swine enteric coronaviruses.Virus research · 2023Article
- Cells and Fugu Response to Capsid of BFNNV Genotype.Viruses · 2023Article
- An aquatic virus exploits the IL6-STAT3-HSP90 signaling axis to promote viral entry.PLoS pathogens · 2023Article
- Identification of B-Cell Epitopes on Capsid Protein Reveals Two Potential Neutralization Mechanisms in Red-Spotted Grouper Nervous Necrosis Virus.Journal of virology · 2023Article
- Hsp90 Regulates GCRV-II Proliferation by Interacting with VP35 as Its Receptor and Chaperone.Journal of virology · 2022Article
- Multiple isoforms of HSP70 and HSP90 required for betanodavirus multiplication in medaka cells.Archives of virology · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nervous necrosis virus (NNV) can infect many species of fish and causes serious acute or persistent infection. However, its pathogenic mechanism is still far from clear. Specific cellular surface receptors are crucial determinants of the species tropism of a virus and its pathogenesis. Here, the heat shock protein 90ab1 of marine model fish species marine medaka (MmHSP90ab1) was identified as a novel receptor of red-spotted grouper NNV (RGNNV). MmHSP90ab1 interacted directly with RGNNV capsid protein (CP). Specifically, MmHSP90ab1 bound to the linker region (LR) of CP through its NM domain. Inhibition of MmHSP90ab1 by HSP90-specific inhibitors or MmHSP90ab1 siRNA caused significant inhibition of viral binding and entry, whereas its overexpression led to the opposite effect. The binding of RGNNV to cultured marine medaka hMMES1 cells was inhibited by blocking cell surface-localized MmHSP90ab1 with anti-HSP90β antibodies or pretreating virus with recombinant MmHSP90ab1 or MmHSP90ab1-NM protein, indicating MmHSP90ab1 was an attachment receptor for RGNNV. Furthermore, we found that MmHSP90ab1 formed a complex with CP and marine medaka heat shock cognate 70, a known NNV receptor. Exogenous expression of MmHSP90ab1 independently facilitated the internalization of RGNNV into RGNNV impenetrable cells (HEK293T), which was blocked by chlorpromazine, an inhibitor of clathrin-dependent endocytosis. Further study revealed that MmHSP90ab1 interacted with the marine medaka clathrin heavy chain. Collectively, these data suggest that MmHSP90ab1 is a functional part of the RGNNV receptor complex and involved in the internalization of RGNNV via the clathrin endocytosis pathway.
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