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Molecular characterization and functional activity of Prx1 in grass carp (Ctenopharyngodon idella).

Authors :
Zhu, Denghui
Li, Yangyang
Huang, Rong
Luo, Lifei
Chen, Liangming
Fu, Peipei
He, Libo
Li, Yongming
Liao, Lanjie
Zhu, Zuoyan
Wang, Yaping
Source :
Fish & Shellfish Immunology. Jul2019, Vol. 90, p395-403. 9p.
Publication Year :
2019

Abstract

Peroxiredoxin (Prx) family are known as an important antioxidant enzyme as the first line of defense against oxidative damage, and also involved in immune responses following viral and bacterial infection. Here, a full-length Prx1 cDNA sequence (CiPrx1) was cloned from grass carp (Ctenopharyngodon idella), which was 1029 bp, including a 5′-terminal untranslated region (UTR) of 121 bp, a 3′-UTR of 272 bp, an open reading frame of 600 bp encoding 199 amino acids with molecular weight of 22.21 kDa and isoelectric point of 6.30. CiPrx1 shares 80.8–99% protein sequence similarity with Prx1 of other fishes. The conserved peroxidase catalytic center "FYPLDFTFVCPTEI" and "GEVCPA" were observed in the sequence of CiPrx1; this indicated that it was a member of 2-Cys Prx. Subcellular localization of CiPrx1 was only strongly distributed in the cytoplasm. Quantitative real-time PCR (RT-qPCR) assays revealed that CiPrx1 mRNA was ubiquitously detected in all tested tissues, and the expression was comparatively high in liver, gill and spleen. Further, the expression of CiPrx1 can be induced by grass carp reovirus (GCRV), lipopolysaccharide (LPS) and polyinosinic:polycytidylic acid (Poly I:C) infection in the different tissues. Moreover, the recombinant CiPrx1 (rCiPrx1) protein was found a potential antioxidant enzyme, that could inhibit DNA damage from oxidants. Altogether, our results imply that CiPrx1 is associated with defending against virus and bacteria pathogens and oxidants in grass carp. • Peroxiredoxin 1 from grass carp was cloned and characterized. • CiPrx1 mRNAs was ubiquitously detected in all tested tissues. • The expression of CiPrx1 can be induced by GCRV, LPS and Poly I:C infection in the different tissues. • Subcellular localization of Prx1-pEGFP was only strongly distributed in the cytoplasm. • The antioxidant activity of the recombinant rCiPrx1 was assessed by mixed-function oxidase assay. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10504648
Volume :
90
Database :
Academic Search Index
Journal :
Fish & Shellfish Immunology
Publication Type :
Academic Journal
Accession number :
136646947
Full Text :
https://doi.org/10.1016/j.fsi.2019.04.302