Cloning and expression of heat shock protein 70 gene in the haemocytes of pearl oyster (Pinctada fucata, Gould 1850) responding to bacterial challenge

Wang, Zhongliang; Wu, Zaohe; Jian, Jichang; Lu, Yue

doi:10.1016/j.fsi.2008.10.011

Cited by 77 publications

(37 citation statements)

References 52 publications

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“…They are soluble intracellular chaperones present in all organisms from prokaryotes to eukaryotes [6,7]. Most Hsps are constitutively expressed under normal physiological conditions, however, their expression is up-regulated by various physiological stressors, such as high temperature, toxins, osmotic stress, ultraviolet and gamma radiation, certain chemicals and drugs, hypoxia, glucose deprivation, and microbial infection that could potentially damage the cellular and molecular structures in the cells [8,9]. Hsps perform essential biological functions under both normal and stressful conditions such as assisting in the folding of nascent proteins, translocation of these proteins between cell organelles, assembly and disassembly of multi-subunit complexes, refolding or degradation of denatured proteins due to stresses, dissolution of pathological protein aggregates, and other processes enhancing the survival of normal and diseased cells and tissues [10].…”

Section: Introductionmentioning

confidence: 99%

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Baruah

Ranjan

Sorgeloos

et al. 2010

Fish & Shellfish Immunology

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a b s t r a c tThe Hsp70 class of heat shock proteins (Hsps) has been implicated at multiple points in the immune response of both vertebrates and invertebrates. This class of chaperones is highly conserved in both sequence and structure, from prokaryotes to higher eukaryotes. In view of their high degree of homology, it was assumed that these Hsp70 proteins derived either from the prokaryotes or eukaryotes would have similar functions, especially in relation to their protective ability in a challenge assay. To verify this, we compared two evolutionary diverse Hsp70s, Artemia Hsp70 and Escherichia coli Hsp70 equivalent DnaK (each overproduced in E.coli), for their ability to protect Artemia against Vibrio challenge. Results showed that Artemia fed with E. coli producing Artemia Hsp70 or DnaK proteins, as assessed by immune-probing in western blots, survived better in a Vibrio challenge assay. The observed effects could be due to enhancement of the Artemia immune system as phenoloxidase activity was found to be increased by these proteins. These two Hsp70 proteins exhibit a high degree of homology, particularly in the peptidebinding domain (the putative innate immunity-activating portion) with 59.6% identity, indicating that the observed protective capacity of homologous or heterologous Hsp70 proteins might reside within this peptide-binding domain.

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Section: Introductionmentioning

confidence: 99%

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Baruah

Ranjan

Sorgeloos

et al. 2010

Fish & Shellfish Immunology

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“…(Pinctada fucata) (Wang et al, 2009). LPS is believed to be an endotoxin because it constitutes the outer leaflet of the outer membrane of most gram-negative bacteria (Wang and Quinn, 2010).…”

Section: Discussionmentioning

confidence: 99%

“…It is primarily cultured to develop the pearls that are known as "South China Sea Pearls" (Zhao et al, 2012). However, a high mortality in juvenile, mother, and operational cultured pearl oysters has been frequently observed in recent years , resulting in a severe reduction in seawater pearls (Wang et al, 2009). To date the cause of the mass oyster mortalities has not been elucidated; however, it has been suggested that the causes are connected with multiple factors such as the degradation of water quality, pathogens, and stock degeneration caused by inbreeding (Song et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Monitoring the response pattern of pearl oysters to environmental challenges might help us to further understand the stress resistance mechanisms in pearl shells, provide assistance in determining appropriate biomarkers to assess environmental impact, and establish treatment strategies for disease control (Wang et al, 2009). To date, several HSP20 gene sequences isolated from mollusc species have been identified, analyzed, and made available in GenBank, including those of Cyclina sinensis (AET13647.1) and Meretrix meretrix (AFK80359.1) .…”

Section: Introductionmentioning

confidence: 99%

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Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii

Lei¹,

Wu²,

Liang³

et al. 2016

Genet. Mol. Res.

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ABSTRACT. Small heat shock proteins (HSPs) are molecular chaperones with ATP-independent properties. They are involved in a variety of physiological and stress processes. In this study, the full-length HSP 20 (HSP20) from Pinctada martensii, designated as PmHSP20, was obtained from hemocytes using rapid amplification of cDNA ends technology. The PmHSP20 cDNA was 952 bp in length, containing an open reading frame of 534 bp that encoded 177-amino acid residues, with an isoelectric point of 5.86 and molecular weight of 20.24 kDa. The sequence of this deduced polypeptide contained typical structure and function domains conserved in the HSP20 family, providing evidence that PmHSP20 belongs to the HSP20 family. The PmHSP20 mRNA expression levels were detected in various tissues of P. martensii and in hemocytes after challenges with the bacteria Vibrio harveyi and lipopolysaccharide (LPS) using quantitative realtime polymerase chain reaction amplification. The results indicated that PmHSP20 is constitutively expressed in all tissues tested and might be involved in the immune response. The upregulation of PmHSP20 after V. harveyi and LPS challenge suggests that PmHSP20 plays an important role in anti-bacterial immunity. Studies on PmHSP20 are a valuable resource to further explore the immune system in pearl oysters and might enhance our knowledge of molluscan innate immunity.

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“…ROS mtHSP75 (Jönsson and Schill, 2007), mtHSP75 (Gao et al, 2008). mtHSP75 (Wang et al, 2009). Poly I:C blood kidney BsmtHSP75 .…”

Section: 재료 및 방법mentioning

confidence: 99%

Characterization of Mitochondrial Heat Shock Protein 75 (mtHSP75) of the Big-belly Seahorse Hippocampus abdominalis

Ko¹,

Wan²,

Lee³

et al. 2015

Korean Journal of Fisheries and Aquatic Sciences

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Cloning and expression of heat shock protein 70 gene in the haemocytes of pearl oyster (Pinctada fucata, Gould 1850) responding to bacterial challenge

Cited by 77 publications

References 52 publications

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii

Characterization of Mitochondrial Heat Shock Protein 75 (mtHSP75) of the Big-belly Seahorse Hippocampus abdominalis

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