Characterization and function analysis of Epinephelus coioides Hsp40 response to Vibrio alginolyticus and SGIV infection

Chen, He-Jia; Li, Pin-Hong; Yang, Yuanxiu; Xin, Xu; Ou, Yan; Wei, Jingguang; Huang, Youhua; Huang, Xiaohong; Qin, Qiwei; Sun, Hongyan

doi:10.1016/j.fsi.2021.09.030

Cited by 9 publications

(2 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This co-upregulation was greatest at CT max in the two highest acclimation temperature fishes, with lower fold-changes of these genes also differentially expressed at acclimation. In fishes, upregulation of hsp40 has mainly been documented in response to exposure to infection agents, including in Paralichthys olivaceus (olive flounder), Epinephelus coioides (orange-spotted grouper), Ictalurus punctatus (channel catfish), and Carassius auratus (Crucian carp) [40][41][42][43]. The mixed direction response (e.g., some subunits upregulated and others downregulated) we found in hsp40 subunit genes after acclimation is similar to that described in Channel Catfish liver following bacterial exposure [43].…”

Section: Discussionmentioning

confidence: 99%

Transcriptomic analyses of juvenile Striped Bass (Morone saxatilis) exposed to chronic and acute temperature change

Penny,

Pavey

2023

PLoS ONE

View full text Add to dashboard Cite

Striped Bass are economically important, migratory fishes, which occur across a wide range of latitudes. Given their wide-ranging nature, Striped Bass can cope with a broad range of environmental temperatures, yet the mechanisms underlying this ability have not been thoroughly described. Heat shock proteins (HSPs) are inducible molecular chaperones, which help mitigate protein damage resulting from increased temperatures. The importance of HSPs has been demonstrated in a number of fish species, but their role in Striped Bass is poorly understood. This study characterizes changes in gene expression in juvenile Striped Bass, following acute and chronic temperature change. Fish were acclimated to one of three temperatures (15, 25 or 30°C) and sampled at one of two treatments (control or after CTmax), following which we assessed differential gene expression and gene ontology in muscle. It is clear from our differential expression analyses that acclimation to warm temperatures elicits more robust changes to gene expression, compared to acute temperature increases. Our differential expression analyses also revealed induction of many different heat shock proteins, including hsp70, hsp90, hsp40 and other small HSPs, after both acute and chronic temperature increase in white muscle. Furthermore, the most consistent gene ontology pattern that emerged following both acclimation and CTmax was upregulation of transcripts involved in “protein folding”, which also include heat shock proteins. Gene ontology analyses also suggest changes to other processes after acclimation, including decreased growth pathways and changes to DNA methylation. Overall, these data suggest that HSPs likely play a major role in the Striped Bass’s ability to tolerate warm waters.

show abstract

Section: Discussionmentioning

confidence: 99%

Transcriptomic analyses of juvenile Striped Bass (Morone saxatilis) exposed to chronic and acute temperature change

Penny,

Pavey

2023

PLoS ONE

View full text Add to dashboard Cite

show abstract

“…The orange-spotted grouper is an important agricultural product in southern China and Southeast Asia [20]. However, in grouper farming, high intensification is usually accompanied by pathogenic disease outbreaks, like vibriosis, which reduce production dramatically [21].…”

Section: Introductionmentioning

confidence: 99%

Molecular and Functional Characterization of α Chain of Interleukin-15 Receptor (IL-15Rα) in Orange-Spotted Grouper (Epinephelus coioides) in Response to Vibrio harveyi Challenge

Zhang,

Wu,

Yang

et al. 2023

Animals

View full text Add to dashboard Cite

Interleukin-15 (IL15) is a proinflammatory cytokine that could induce the production of inflammatory cytokines. In this study, the α chain of the IL15 receptor of Epinephelus coioides (Ec-IL15Rα), a natural regulator of IL15, was identified, and immune response functions of fish were determined and characterized. Ec-IL15Rα contains a 720 bp open reading frame that encodes 239 amino acids, including four typical conserved cysteine residues with a highly conserved sushi domain. Ec-IL15Rα is closely related to Epinephelus lanceolatus and is the most clustered with teleost. Subcellular localization studies showed that Ec-IL15Rα was situated in the cytoplasm and cell membrane. Ec-IL15Rα was detected in 11 tissues, with the highest expression in the liver and blood. Meanwhile, the Ec-IL15Rα transcriptional levels substantially increased in nine tissues after Vibrio harveyi infection. Ec-IL15Rα was significantly up-regulated in HKLs by ConA, PHA, LPS and poly I:C stimulation. In vitro analysis, the recombinant protein of rEc-IL15Rα stimulates HKL proliferation and IL1R, IL6R, IL10, and IL16 expression. Challenge experiments revealed that IL15Rα protein showed an increase of 6.67–10% survival protection rate after V. harveyi infection. This study provides a better understanding of the immune protection of IL15Rα in vertebrate fish.

show abstract

Multiple isoforms of HSP70 and HSP90 required for betanodavirus multiplication in medaka cells

Zenke

Okinaka

2022

Arch Virol

View full text Add to dashboard Cite

Characterization and function analysis of Epinephelus coioides Hsp40 response to Vibrio alginolyticus and SGIV infection

Cited by 9 publications

References 31 publications

Transcriptomic analyses of juvenile Striped Bass (Morone saxatilis) exposed to chronic and acute temperature change

Transcriptomic analyses of juvenile Striped Bass (Morone saxatilis) exposed to chronic and acute temperature change

Molecular and Functional Characterization of α Chain of Interleukin-15 Receptor (IL-15Rα) in Orange-Spotted Grouper (Epinephelus coioides) in Response to Vibrio harveyi Challenge

Multiple isoforms of HSP70 and HSP90 required for betanodavirus multiplication in medaka cells

Contact Info

Product

Resources

About