First characterization of three cyclophilin family proteins in the oyster, Crassostrea ariakensis Gould. (August 2016)
- Record Type:
- Journal Article
- Title:
- First characterization of three cyclophilin family proteins in the oyster, Crassostrea ariakensis Gould. (August 2016)
- Main Title:
- First characterization of three cyclophilin family proteins in the oyster, Crassostrea ariakensis Gould
- Authors:
- Xu, Ting
Xie, Jiasong
Yang, Shoubao
Ye, Shigen
Luo, Ming
Wu, Xinzhong - Abstract:
- Abstract: Cyclophilins (CyPs) are a family of proteins that bind the immunosuppressive agent cyclosporin A (CsA) with high-affinity and belong to one of the three superfamilies of peptidyl-prolyl cis-trans isomerases (PPIase). In this report, three cyclophilin genes (Ca-CyPs), including Ca-CyPA, Ca-CyPB and Ca-PPIL3, were identified from oyster, Crassostrea ariakensis Gould in which Ca-CyPA encodes a protein with 165 amino acid sequences, Ca-CyPB encodes a protein with 217 amino acid sequences and Ca-PPIL3 encodes a protein with 162 amino acid sequences. All of the three Ca-CyPs genes contain a typical CyP-PPIase domain with its signature sequences and Ca-CyPB contains an N-signal peptide sequences. Tissue distribution study revealed that Ca-CyPs were ubiquitously expressed in all examined tissues and the highest levels were observed in hemocytes. RLO incubation upregulated the mRNA expression levels of Ca-CyPs, indicating that three Ca-CyPs might be involved in oyster immune response against RLO infection. Highlights: We firstly identified three cyclophilins (Ca-CyPs), including Ca-CyPA, Ca-CyPB and Ca-PPIL3 from the oyster, C. ariakensis . All the Ca-CyPs contain a typical CyP-PPIase domain with its signature sequences and Ca-CyPB contains an N-signal peptide. Tissue distribution studies revealed that Ca-CyPs were expressed in all examined tissues with the highest levels in hemocytes. RLO incubation increased the expression levels of Ca-CyPs, indicating Ca-CyPs might beAbstract: Cyclophilins (CyPs) are a family of proteins that bind the immunosuppressive agent cyclosporin A (CsA) with high-affinity and belong to one of the three superfamilies of peptidyl-prolyl cis-trans isomerases (PPIase). In this report, three cyclophilin genes (Ca-CyPs), including Ca-CyPA, Ca-CyPB and Ca-PPIL3, were identified from oyster, Crassostrea ariakensis Gould in which Ca-CyPA encodes a protein with 165 amino acid sequences, Ca-CyPB encodes a protein with 217 amino acid sequences and Ca-PPIL3 encodes a protein with 162 amino acid sequences. All of the three Ca-CyPs genes contain a typical CyP-PPIase domain with its signature sequences and Ca-CyPB contains an N-signal peptide sequences. Tissue distribution study revealed that Ca-CyPs were ubiquitously expressed in all examined tissues and the highest levels were observed in hemocytes. RLO incubation upregulated the mRNA expression levels of Ca-CyPs, indicating that three Ca-CyPs might be involved in oyster immune response against RLO infection. Highlights: We firstly identified three cyclophilins (Ca-CyPs), including Ca-CyPA, Ca-CyPB and Ca-PPIL3 from the oyster, C. ariakensis . All the Ca-CyPs contain a typical CyP-PPIase domain with its signature sequences and Ca-CyPB contains an N-signal peptide. Tissue distribution studies revealed that Ca-CyPs were expressed in all examined tissues with the highest levels in hemocytes. RLO incubation increased the expression levels of Ca-CyPs, indicating Ca-CyPs might be involved in oyster immune response. … (more)
- Is Part Of:
- Fish & shellfish immunology. Volume 55(2016:Aug.)
- Journal:
- Fish & shellfish immunology
- Issue:
- Volume 55(2016:Aug.)
- Issue Display:
- Volume 55 (2016)
- Year:
- 2016
- Volume:
- 55
- Issue Sort Value:
- 2016-0055-0000-0000
- Page Start:
- 257
- Page End:
- 266
- Publication Date:
- 2016-08
- Subjects:
- Crassostrea ariakensis -- Rickettsia-like organism -- Cyclophilin -- Ca-CyPs -- Immune response
Fishes -- Immunology -- Periodicals
Shellfish -- Immunology -- Periodicals
Poissons -- Immunologie -- Périodiques
Crustacés -- Immunologie -- Périodiques
571.9617 - Journal URLs:
- http://www.sciencedirect.com/science/journal/10504648 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1050-4648;screen=info;ECOIP ↗
http://www.sciencedirect.com/science/journal/latest/10504648 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fsi.2016.05.037 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
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- British Library DSC - 3934.880000
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