Heat shock 70 kDa protein cognate 5 involved in WSSV toleration of Litopenaeus vannamei

Yuan, Kai; Yuan, Fenghua; He, Honghui; Bi, Haitao; Weng, Shaoping; He, Jianguo; Chen, Yihong

doi:10.1016/j.dci.2017.02.003

Cited by 33 publications

(17 citation statements)

References 34 publications

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“…In addition, HSC70-5 was shown to exhibit high sequence similarity with HSC70-5 in the beetle Ointhophagus taurus (82% identity) and was induced by heat stress in a manner that was similar to the recently discovered P . vannamei HSC70-5 15 . In S2 cells, Lv HSC70-5 has been shown to localise in mitochondria, where it functions as the regulator of mitochondrial morphology and cellular homeostasis 15,16 .…”

Section: Discussionmentioning

confidence: 99%

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Sequence and expression analysis of HSP70 family genes in Artemia franciscana

Junprung

Norouzitallab

Vos

et al. 2019

Sci Rep

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Thus far, only one gene from the heat shock protein 70 ( HSP70 ) family has been identified in Artemia franciscana . Here, we used the draft Artemia transcriptome database to search for other genes in the HSP70 family. Four novel HSP70 genes were identified and designated heat shock cognate 70 ( HSC70 ), heat shock 70 kDa cognate 5 ( HSC70-5 ), Immunoglobulin heavy-chain binding protein (BIP) , and hypoxia up-regulated protein 1 ( HYOU1 ). For each of these genes, we obtained nucleotide and deduced amino acid sequences, and reconstructed a phylogenetic tree. Expression analysis revealed that in the juvenile state, the transcription of HSP70 and HSC70 was significantly ( P < 0.05) higher in a population of A . franciscana selectively bred for increased induced thermotolerance (TF12) relative to a control population (CF12). Following non-lethal heat shock treatment at the nauplius stage, transcription of HSP70 , HSC70 , and HSC70-5 were significantly ( P < 0.05) up-regulated in TF12. In contrast, transcription of the other HSP70 family members in A . franciscana ( BIP , HYOU1 , and HSPA4 ) showed no significant ( P > 0.05) induction. Gene expression analysis demonstrated that not all members of the HSP70 family are involved in the response to heat stress and selection and that especially altered expression of HSC70 plays a role in a population selected for increased thermotolerance.

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Section: Discussionmentioning

confidence: 99%

“…vannamei HSC70-5 15 . In S2 cells, Lv HSC70-5 has been shown to localise in mitochondria, where it functions as the regulator of mitochondrial morphology and cellular homeostasis 15,16 . We also identified BIP in this study; this was very similar to heat shock protein cognate 3 of Chelax destructor (88% identity).…”

Section: Discussionmentioning

confidence: 99%

Sequence and expression analysis of HSP70 family genes in Artemia franciscana

Junprung

Norouzitallab

Vos

et al. 2019

Sci Rep

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“…In Metapenaeus ensis , HSC70 (the constitutive form of HSP70) was found to be a negative regulator of vitellogenesis (Chan et al, 2014). In L. vannamei , HSP10 , HSP27 , HSP30 , HSP60 , HSP70 and HSP90 mRNA were consistently or specifically expressed in response to thermal or pH stress, heavy metal exposure (Qian et al, 2012), and bacterial or viral infection (Junprung et al, 2017; Yuan et al, 2017); HSP70 promoted post-larval tolerance to heat, ammonia and metals (Sung et al, 2018), and HSC70 reduced protein aggregation and mortality after viral infection (Yuan et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Heat Shock Protein 40 (HSP40) in Pacific White Shrimp (Litopenaeus vannamei): Molecular Cloning, Tissue Distribution and Ontogeny, Response to Temperature, Acidity/Alkalinity and Salinity Stresses, and Potential Role in Ovarian Development

Chen

Lin

et al. 2018

Front. Physiol.

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Heat shock proteins (HSPs), a family of conserved proteins that are produced by cells in response to stresses, are known as molecular chaperones with a range of housekeeping and cellular protective functions. The 40 kD heat shock protein (HSP40) is a co-chaperone for HSP70 in the regulation of ATP hydrolysis. Unlike its well-documented cofactor HSP70, little is currently known regarding the biological functions of HSP40 in crustacean species such as penaeid shrimp. In the present study, the cDNA encoding HSP40 (Lv-HSP40) was identified from the Pacific white shrimp Litopenaeus vannamei, a highly significant commercial culture species. The structural organization indicates that Lv-HSP40 belongs to the type-I HSP40s. The muscle, gill, and hepatopancreas are the main sites of Lv-HSP40 transcript expression. Within these tissues, Lv-HSP40 mRNA were predominantly exhibited in the myocytes, epithelial cells and hepatopancreatic cells, respectively. Under acute thermal stress in the culture environment, Lv-HSP40 transcript levels are significantly induced in these three tissues, while low pH stress only upregulates Lv-HSP40 mRNA in the hepatopancreas and gill. During ontogenesis, Lv-HSP40 transcript levels are high at early embryonic stages and drop sharply at late embryonic and early larval stages. The ovary is another major organ of Lv-HSP40 mRNA expression in female shrimp, and Lv-HSP40 transcripts were mainly presented in the follicle cells but only weekly detected in the oocytes. Ovarian Lv-HSP40 mRNA levels increase continuously during gonadal development. Silencing of the Lv-HSP40 gene by RNA interference may effectively delay ovarian maturation after unilateral eyestalk ablation. The roles of Lv-HSP40 in ovarian development are speculated to be independent of its cofactor HSP70, and the vitellogenesis factor vitellogenin (Vg) and vitellogenin receptor (VgR). Our study, as a whole, provides new insights into the roles of HSP40 in multiple physiological processes in L. vannamei: (1) HSP40 is a responding factor during stressful conditions; and (2) HSP40 participates in embryonic and ovarian development.

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“…Heat shock protein (HSP) is a family of proteins that ubiquitously distribute and highly conserve, behaving as molecular chaperones and exerting a protective effect against various stimuli [ 82 – 84 ]. The stimuli include heat shock, ultraviolet light, infection, inflammation, and cellular toxins.…”

Section: Discussionmentioning

confidence: 99%

“…In L . vannamei , down-regulation Heat shock 70 kDa protein cognate 5 (LvHSC70-5) could increase the cumulative mortality after WSSV infection and LvHSC70-5 contribute to WSSV toleration [ 84 ]. The HSP21 and HSP70 were found in our transcriptome data and changed significantly.…”

Section: Discussionmentioning

confidence: 99%

A transcriptome study on Macrobrachium nipponense hepatopancreas experimentally challenged with white spot syndrome virus (WSSV)

Zhao

Sun

et al. 2018

PLoS ONE

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White spot syndrome virus (WSSV) is one of the most devastating pathogens of cultured shrimp, responsible for massive loss of its commercial products worldwide. The oriental river prawn Macrobrachium nipponense is an economically important species that is widely farmed in China and adult prawns can be infected by WSSV. However, the molecular mechanisms of the host pathogen interaction remain unknown. There is an urgent need to learn the host pathogen interaction between M. nipponense and WSSV which will be able to offer a solution in controlling the spread of WSSV. Next Generation Sequencing (NGS) was used in this study to determin the transcriptome differences by the comparison of control and WSSV-challenged moribund samples, control and WSSV-challenged survived samples of hepatopancreas in M. nipponense. A total of 64,049 predicted unigenes were obtained and classified into 63 functional groups. Approximately, 4,311 differential expression genes were identified with 3,308 genes were up-regulated when comparing the survived samples with the control. In the comparison of moribund samples with control, 1,960 differential expression genes were identified with 764 genes were up-regulated. In the contrast of two comparison libraries, 300 mutual DEGs with 95 up-regulated genes and 205 down-regulated genes. All the DEGs were performed GO and KEGG analysis, overall a total of 85 immune-related genes were obtained and these gene were groups into 13 functions and 4 KEGG pathways, such as protease inhibitors, heat shock proteins, oxidative stress, pathogen recognition immune receptors, PI3K/AKT/mTOR pathway, MAPK signaling pathway and Ubiquitin Proteasome Pathway. Ten genes that valuable in immune responses against WSSV were selected from those DEGs to furture discuss the response of host to WSSV. Results from this study contribute to a better understanding of the immune response of M. nipponense to WSSV, provide information for identifying novel genes in the absence of genome of M. nipponense. Furthermore, large number of transcripts obtained from this study could provide a strong basis for future genomic research on M. nipponense.

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Heat shock 70 kDa protein cognate 5 involved in WSSV toleration of Litopenaeus vannamei

Cited by 33 publications

References 34 publications

Sequence and expression analysis of HSP70 family genes in Artemia franciscana

Sequence and expression analysis of HSP70 family genes in Artemia franciscana

Heat Shock Protein 40 (HSP40) in Pacific White Shrimp (Litopenaeus vannamei): Molecular Cloning, Tissue Distribution and Ontogeny, Response to Temperature, Acidity/Alkalinity and Salinity Stresses, and Potential Role in Ovarian Development

A transcriptome study on Macrobrachium nipponense hepatopancreas experimentally challenged with white spot syndrome virus (WSSV)

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