Identification of the small heat shock protein, HSP21, of shrimp Penaeus monodon and the gene expression of HSP21 is inactivated after white spot syndrome virus (WSSV) infection

Huang, Po Yu; Kang, Shih Ting; Chen, Wei Yu; Hsu, Tai Ching; Lo, Chu Fang; Liu, Kuan Fu; Chen, Li Li

doi:10.1016/j.fsi.2008.06.002

Cited by 52 publications

(38 citation statements)

References 22 publications

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“…PmHSP20 was detected in different healthy P. martensii organisms with highest expression in the hepatopancreas and lowest in the adductor muscle, hemocyte, gill, and foot (Figure 4). The expression pattern of PmHSP20 in tissues was somewhat similar to previously reported HSP20 expression patterns in the disk abalone (Wan et al, 2012), but different to those previously reported in shrimp (Huang et al, 2008), bloody clam, and razor clam (Bao et al, 2011;Zhang et al, 2013). It has been speculated that different species-or-origin or various tissue functions result in the different expression of sHSPs in tissues.…”

Section: Discussionsupporting

confidence: 71%

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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Section: Discussionsupporting

confidence: 71%

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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“…1 twofold dilution of the AccHsp27.6 protein solution; 2 fivefold dilution of the AccHsp27.6 protein solution; 3 tenfold dilution of the AccHsp27.6 protein solution; 4 positive control (kanamycin, 250 mg/ml); 5 negative control (the total protein from BL21 (DE3) E. coli, 0.5 mg/ml); 6 PBS; 7 the original concentrated solution of purified AccHsp27.6 protein (0.5 mg/ml) (Wu et al 2011); however, information concerning immunity and the potential role of the sHSPs is relatively limited and has emerged only recently. An sHSP gene from shrimp, Hsp21, was downregulated during a white spot syndrome viral infection, which might be related to host cell apoptosis (Huang et al 2008). The genome-wide analysis of host gene expression in silkworm cells infected with Bombyx mori nucleopolyhedrovirus revealed that the expression of Hsp20.1 was decreased to approximately 50% at 2 h post-infection, which suggested that silkworm Hsp20.1 is involved in anti-BmNPV immunity at the early phase of infection (Sagisaka et al 2010).…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning and characterization of Hsp27.6: the first reported small heat shock protein from Apis cerana cerana

Liu

Kang

et al. 2012

Cell Stress and Chaperones

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Small heat shock proteins (sHSPs) play an important role in the cellular defense of prokaryotic and eukaryotic organisms against a variety of internal and external stressors. In this study, a cDNA clone encoding a member of the α-crystallin/sHSP family, termed AccHsp27.6, was isolated from Apis cerana cerana. The full-length cDNA is 1,014 bp in length and contains a 708-bp open reading frame encoding a protein of 236 amino acids with a calculated molecular weight of 27.6 kDa and an isoelectric point of 7.53. Seven putative heat shock elements and three NF-κB binding sites were present in the 5′-flanking region, suggesting a possible function in immunity. A semi-quantitative RT-PCR analysis indicated that AccHsp27.6 was expressed in all tested tissues and at different developmental stages. Furthermore, expression of the AccHsp27.6 transcript was induced by exposure to heat shock, H 2 O 2 , a number of different chemicals (including SO 2 , formaldehyde, alcohol, acetone, chloroform, and the pesticides phoxime and acetamiprid), and the microbes Staphylococcus aureus and Micrococcus luteus. In contrast, the mRNA expression could be repressed by CO 2 , the pesticides pyriproxyfen and cyhalothrin, and the microbes Bacillus subtilis and Pseudomonas aeruginosa. Notably, the recombinant AccHsp27.6 protein exhibited significant in vitro molecular chaperone activity and antimicrobial activity. Taken together, these results suggest that AccHsp27.6 might play an important role in the response to abiotic and biotic stresses and in immune reactions.

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“…Citrate synthase (CS, from porcine heart, Sigma, Shanghai, China) aggregation was applied to identify chaperone activity; this procedure has been described in detail in a previous study (Huang et al 2008). Briefly, the aggregation level of CS was monitored in HEPES buffer (50 mM HEPES, pH 8.0, 25 mM NaCl, 0.5 mM DTT) at 45°C.…”

Section: Chaperone Activity Assaymentioning

confidence: 99%

“…Considering the enormous economic losses induced by environmental stressors in the shrimp industry, studies focusing on heat shock proteins have become increasingly popular because of the important roles these proteins play in resistance to stress (Cesar and Yang 2007;Cui et al 2010;Li et al 2012;Qian et al 2012). Unfortunately, only three Hsps, namely, Hsp90, Hsp70, and Hsp21, have been reported in P. monodon (Lo et al 2004;Huang et al 2008;Jiang et al 2009). In order to understand the mechanisms of stress tolerance and disease resistance of P. monodon better, we characterized the complete compelemantary DNA (cDNA) sequences of Hsp60 and its co-chaperonin, Hsp10, in this species and investigated the messenger RNA (mRNA) expression of the two genes when exposed to pH challenge, osmotic stress, and heavy metal.…”

Section: Introductionmentioning

confidence: 99%

Characterization and function analysis of Hsp60 and Hsp10 under different acute stresses in black tiger shrimp, Penaeus monodon

Shi

Zhao

et al. 2016

Cell Stress and Chaperones

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Heat shock proteins (Hsps) are a class of highly conserved proteins produced in virtually all living organisms from bacteria to humans. Hsp60 and Hsp10, the most important mitochondrial chaperones, participate in environmental stress responses. In this study, the full-length complementary DNAs (cDNAs) of Hsp60 (PmHsp60) and Hsp10 (PmHsp10) were cloned from Penaeus monodon. Sequence analysis showed that PmHsp60 and PmHsp10 encoded polypeptides of 578 and 102 amino acids, respectively. The expression profiles of PmHsp60 and PmHsp10 were detected in the gills and hepatopancreas of the shrimps under pH challenge, osmotic stress, and heavy metal exposure, and results suggested that PmHsp60 and PmHsp10 were involved in the responses to these stimuli. ATPase and chaperone activity assay indicated that PmHsp60 could slow down protein denaturation and that Hsp60/Hsp10 may be combined to produce a chaperone complex with effective chaperone and ATPase activities. Overall, this study provides useful information to help further understand the functional mechanisms of the environmental stress responses of Hsp60 and Hsp10 in shrimp.

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Identification of the small heat shock protein, HSP21, of shrimp Penaeus monodon and the gene expression of HSP21 is inactivated after white spot syndrome virus (WSSV) infection

Cited by 52 publications

References 22 publications

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

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

Molecular cloning and characterization of Hsp27.6: the first reported small heat shock protein from Apis cerana cerana

Characterization and function analysis of Hsp60 and Hsp10 under different acute stresses in black tiger shrimp, Penaeus monodon

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