The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant protein
Background: Cyclophilin A (CypA), a receptor for the immunosuppressive agent cyclosporin A (CsA), is a cis-trans peptidyl-prolyl isomerase (PPIase) which accelerates the cis-trans isomerization of prolyl-peptide bonds and interacts with a variety of proteins to regulate their activities. Results: Th...
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Pontificia Universidad Católica de Valparaíso
2013
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oai:scielo:S0717-345820130002000022013-03-27The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant proteinWang,MengqiangZhang,DaoxiangWang,LinglingGai,YunchaoZhou,ZhiZhang,HuanSong,Linsheng antifungal activity cyclophilin A Eriocheir sinensis immune response PPIase activity Background: Cyclophilin A (CypA), a receptor for the immunosuppressive agent cyclosporin A (CsA), is a cis-trans peptidyl-prolyl isomerase (PPIase) which accelerates the cis-trans isomerization of prolyl-peptide bonds and interacts with a variety of proteins to regulate their activities. Results: The full-length cDNA of crab Eriocheir sinensis CypA (EsCypA) was cloned by EST and RACE technique. The complete sequence of EsCypA cDNA contained a 5' untranslated region (UTR) of 50 bp, a 3’ UTR of 233 bp with a polyA tail, and an open reading frame (ORF) of 495 bp encoding a polypeptide of 164 amino acids with the predicted molecular weight of 17.36 kDa. The deduced amino acid sequence of EsCypA contained two highly conserved signature sequences of peptidyl-prolyl cis-trans isomerase and a pro-isomerase domain. The mRNA transcripts of EsCypA were detectable in all the examined tissues, including haemocytes, gill, hepatopancreas, gonad, muscle and heart, with higher expression level in hepatopancreas and gonad. No significant difference in the relative mRNA expression level of EsCypA was observed during the whole course of bacteria challenge, whereas it was up-regulated during fungi challenge. The purified recombinant protein rEsCypA exhibited a significant PPIase activity and an antifungal activity. Conclusions: All these results indicated that it was a typical CypA member and potentially involved in the innate immune responses of crab.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.16 n.2 20132013-03-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000200002en10.2225/vol16-issue2-fulltext-5 |
| institution |
Scielo Chile |
| collection |
Scielo Chile |
| language |
English |
| topic |
antifungal activity cyclophilin A Eriocheir sinensis immune response PPIase activity |
| spellingShingle |
antifungal activity cyclophilin A Eriocheir sinensis immune response PPIase activity Wang,Mengqiang Zhang,Daoxiang Wang,Lingling Gai,Yunchao Zhou,Zhi Zhang,Huan Song,Linsheng The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant protein |
| description |
Background: Cyclophilin A (CypA), a receptor for the immunosuppressive agent cyclosporin A (CsA), is a cis-trans peptidyl-prolyl isomerase (PPIase) which accelerates the cis-trans isomerization of prolyl-peptide bonds and interacts with a variety of proteins to regulate their activities. Results: The full-length cDNA of crab Eriocheir sinensis CypA (EsCypA) was cloned by EST and RACE technique. The complete sequence of EsCypA cDNA contained a 5' untranslated region (UTR) of 50 bp, a 3’ UTR of 233 bp with a polyA tail, and an open reading frame (ORF) of 495 bp encoding a polypeptide of 164 amino acids with the predicted molecular weight of 17.36 kDa. The deduced amino acid sequence of EsCypA contained two highly conserved signature sequences of peptidyl-prolyl cis-trans isomerase and a pro-isomerase domain. The mRNA transcripts of EsCypA were detectable in all the examined tissues, including haemocytes, gill, hepatopancreas, gonad, muscle and heart, with higher expression level in hepatopancreas and gonad. No significant difference in the relative mRNA expression level of EsCypA was observed during the whole course of bacteria challenge, whereas it was up-regulated during fungi challenge. The purified recombinant protein rEsCypA exhibited a significant PPIase activity and an antifungal activity. Conclusions: All these results indicated that it was a typical CypA member and potentially involved in the innate immune responses of crab. |
| author |
Wang,Mengqiang Zhang,Daoxiang Wang,Lingling Gai,Yunchao Zhou,Zhi Zhang,Huan Song,Linsheng |
| author_facet |
Wang,Mengqiang Zhang,Daoxiang Wang,Lingling Gai,Yunchao Zhou,Zhi Zhang,Huan Song,Linsheng |
| author_sort |
Wang,Mengqiang |
| title |
The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant protein |
| title_short |
The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant protein |
| title_full |
The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant protein |
| title_fullStr |
The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant protein |
| title_full_unstemmed |
The molecular characterization of a cyclophilin A from Chinese mitten crab Eriocheir sinensis and the antifungal activity of its recombinant protein |
| title_sort |
molecular characterization of a cyclophilin a from chinese mitten crab eriocheir sinensis and the antifungal activity of its recombinant protein |
| publisher |
Pontificia Universidad Católica de Valparaíso |
| publishDate |
2013 |
| url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000200002 |
| work_keys_str_mv |
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| _version_ |
1718441869416857600 |