Molecular cloning, characterization and expression analysis of HSP60, HSP70 and HSP90 in the golden apple snail, Pomacea canaliculata

Yipeng Xu, Guowan Zheng, Shengzhang Dong, Guangfu Liu, Xiaoping Yu

Research output: Contribution to journalArticle

Abstract

The golden apple snail, Pomacea canaliculata, has strong tolerance to high temperature, facilitating its invasion in East and Southeast Asia. In the present study, three cDNAs encoding heat shock proteins (. PocaHSP60, PocaHSP70, PocaHSP90) in P. canaliculata were cloned and characterized. The PocaHSP60 cDNA was 2447bp, containing an ORF encoding a polypeptide of 574 amino acids. The PocaHSP70 cDNA was 2644bp, containing an ORF encoding a polypeptide of 643 amino acids. The PocaHSP90 cDNA was 2546bp, containing an ORF encoding a polypeptide of 726 amino acids. Genomic DNA analysis showed that PocaHSP60 had 11 introns in the coding region and PocaHSP90 had 7 introns but PocaHSP70 had no one. The expression changes of these three PocaHSPs in the gill, digestive gland, kidney and foot muscle of P.canaliculata exposed to high and low temperature were investigated. The results of quantitative PCR and western blotting showed that the expression level of PocaHSP90 was much higher than PocaHSP60 and PocaHSP70 at room temperature, and PocaHSP70 expression level was the lowest among them. After heat shock, PocaHSP70 expression increased rapidly, much more significantly than PocaHSP90 expression, and the effect of heat shock on the expression of PocaHSP70 and PocaHSP90 in the different tissues of P.canaliculata was not the same. Unlike PocaHSP70 and PocaHSP90, PocaHSP60 expression seemed not to be affected by heat shock, because its expression was moderately induced only in the foot muscle. However, cool shock had little effect on the expression change of above three PocaHSPs. These results indicated that HSPs might be related to the thermal resistance of P.canaliculata.

Original languageEnglish (US)
Pages (from-to)643-653
Number of pages11
JournalFish and Shellfish Immunology
Volume41
Issue number2
DOIs
StatePublished - Dec 1 2014
Externally publishedYes

Fingerprint

Pomacea canaliculata
Cloning
heat shock
Snails
Molecular Cloning
Malus
snail
heat stress
open reading frames
molecular cloning
Shock
polypeptides
Complementary DNA
Hot Temperature
Open Reading Frames
amino acids
amino acid
introns
Amino Acids
Introns

Keywords

  • Heat shock protein
  • HSP60
  • HSP70
  • HSP90
  • Pomacea canaliculata

ASJC Scopus subject areas

  • Aquatic Science
  • Environmental Chemistry
  • Medicine(all)

Cite this

Molecular cloning, characterization and expression analysis of HSP60, HSP70 and HSP90 in the golden apple snail, Pomacea canaliculata. / Xu, Yipeng; Zheng, Guowan; Dong, Shengzhang; Liu, Guangfu; Yu, Xiaoping.

In: Fish and Shellfish Immunology, Vol. 41, No. 2, 01.12.2014, p. 643-653.

Research output: Contribution to journalArticle

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abstract = "The golden apple snail, Pomacea canaliculata, has strong tolerance to high temperature, facilitating its invasion in East and Southeast Asia. In the present study, three cDNAs encoding heat shock proteins (. PocaHSP60, PocaHSP70, PocaHSP90) in P. canaliculata were cloned and characterized. The PocaHSP60 cDNA was 2447bp, containing an ORF encoding a polypeptide of 574 amino acids. The PocaHSP70 cDNA was 2644bp, containing an ORF encoding a polypeptide of 643 amino acids. The PocaHSP90 cDNA was 2546bp, containing an ORF encoding a polypeptide of 726 amino acids. Genomic DNA analysis showed that PocaHSP60 had 11 introns in the coding region and PocaHSP90 had 7 introns but PocaHSP70 had no one. The expression changes of these three PocaHSPs in the gill, digestive gland, kidney and foot muscle of P.canaliculata exposed to high and low temperature were investigated. The results of quantitative PCR and western blotting showed that the expression level of PocaHSP90 was much higher than PocaHSP60 and PocaHSP70 at room temperature, and PocaHSP70 expression level was the lowest among them. After heat shock, PocaHSP70 expression increased rapidly, much more significantly than PocaHSP90 expression, and the effect of heat shock on the expression of PocaHSP70 and PocaHSP90 in the different tissues of P.canaliculata was not the same. Unlike PocaHSP70 and PocaHSP90, PocaHSP60 expression seemed not to be affected by heat shock, because its expression was moderately induced only in the foot muscle. However, cool shock had little effect on the expression change of above three PocaHSPs. These results indicated that HSPs might be related to the thermal resistance of P.canaliculata.",
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AU - Yu, Xiaoping

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