Molecular characterization, expression analysis, and bactericidal activity of the derivative peptides of TFPI-1 and TFPI-2 in half-smooth tongue sole, Cynoglossus semilaevis. (November 2016)
- Record Type:
- Journal Article
- Title:
- Molecular characterization, expression analysis, and bactericidal activity of the derivative peptides of TFPI-1 and TFPI-2 in half-smooth tongue sole, Cynoglossus semilaevis. (November 2016)
- Main Title:
- Molecular characterization, expression analysis, and bactericidal activity of the derivative peptides of TFPI-1 and TFPI-2 in half-smooth tongue sole, Cynoglossus semilaevis
- Authors:
- Zhao, Xin-peng
He, Shu-wen
Yue, Bin
Wang, Guang-hua
Zhang, Min - Abstract:
- Abstract: Tissue factor pathway inhibitors (TFPIs) are Kunitz-type serine protease inhibitors that reversibly regulate the blood coagulation induced by tissue factor. TFPI family contain two members, TFPI-1 and TFPI-2. Recent studies have shown TFPI-1 and TFPI-2 also play important roles in innate immunity, however, the potential function of teleost TFPI are very limited. In this study, we characterized two TFPI (CsTFPI-1 and CsTFPI-2) molecules from half-smooth tongue sole ( Cynoglossus semilaevis ), examined their tissue distributions and expression patterns under pathogens stimulation as well as investigated the antibacterial activity of the C-terminal peptides. Quantitative real time RT-PCR analysis showed that constitutive CsTFPI-1 expression occurred, in increasing order, in head kidney, intestine, brain, spleen, liver, skin, gills, heart, and muscle; CsTFPI-2 was expressed, in increasing order, in the gills, intestine, skin, head kidney, liver, brain, spleen, muscle, and heart. Under Vibrio anguillarum, Streptococcus agalactiae and fish megalocytivirus stimulation, both CsTFPI-1 and CsTFPI-2 expression increased significantly in a manner that depended on the pathogen, tissue type, and infection stage, which suggested CsTFPI-1 and CsTFPI-2 play important roles in anti-bacterial and anti-viral infection. Finally, C-terminal peptides of CsTFPI-1 and CsTFPI-2, were synthesized and proved to have antibacterial effect against Micrococcus luteus that were independent of hostAbstract: Tissue factor pathway inhibitors (TFPIs) are Kunitz-type serine protease inhibitors that reversibly regulate the blood coagulation induced by tissue factor. TFPI family contain two members, TFPI-1 and TFPI-2. Recent studies have shown TFPI-1 and TFPI-2 also play important roles in innate immunity, however, the potential function of teleost TFPI are very limited. In this study, we characterized two TFPI (CsTFPI-1 and CsTFPI-2) molecules from half-smooth tongue sole ( Cynoglossus semilaevis ), examined their tissue distributions and expression patterns under pathogens stimulation as well as investigated the antibacterial activity of the C-terminal peptides. Quantitative real time RT-PCR analysis showed that constitutive CsTFPI-1 expression occurred, in increasing order, in head kidney, intestine, brain, spleen, liver, skin, gills, heart, and muscle; CsTFPI-2 was expressed, in increasing order, in the gills, intestine, skin, head kidney, liver, brain, spleen, muscle, and heart. Under Vibrio anguillarum, Streptococcus agalactiae and fish megalocytivirus stimulation, both CsTFPI-1 and CsTFPI-2 expression increased significantly in a manner that depended on the pathogen, tissue type, and infection stage, which suggested CsTFPI-1 and CsTFPI-2 play important roles in anti-bacterial and anti-viral infection. Finally, C-terminal peptides of CsTFPI-1 and CsTFPI-2, were synthesized and proved to have antibacterial effect against Micrococcus luteus that were independent of host serum. Take together, these results indicate that CsTFPI-1 and CsTFPI-2 play important roles in antimicrobial immunity of this fish. Highlights: Two TFPI homologues (CsTFPI-1 and CsTFPI-2) were characterized. Both CsTFPI-1 and CsTFPI-2 distributed ubiquitously in tongue sole tissues. Both CsTFPI-1 and CsTFPI-2 could be induced by bacterial or viral pathogens. C-terminal peptides of CsTFPI-1 and CsTFPI-2 displayed antibacterial activity that were independent of host serum. … (more)
- Is Part Of:
- Fish & shellfish immunology. Volume 58(2016:Nov.)
- Journal:
- Fish & shellfish immunology
- Issue:
- Volume 58(2016:Nov.)
- Issue Display:
- Volume 58 (2016)
- Year:
- 2016
- Volume:
- 58
- Issue Sort Value:
- 2016-0058-0000-0000
- Page Start:
- 563
- Page End:
- 571
- Publication Date:
- 2016-11
- Subjects:
- Cynoglossus semilaevis -- TFPI-1 -- TFPI-2 -- Expression -- C-terminal peptides -- Antibacterial activity
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.2016.10.003 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3934.880000
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