A C-type lectin (LvCTL4) from Litopenaeus vannamei is a downstream molecule of the NF-κB signaling pathway and participates in antibacterial immune response. Issue 1 (March 2015)
- Record Type:
- Journal Article
- Title:
- A C-type lectin (LvCTL4) from Litopenaeus vannamei is a downstream molecule of the NF-κB signaling pathway and participates in antibacterial immune response. Issue 1 (March 2015)
- Main Title:
- A C-type lectin (LvCTL4) from Litopenaeus vannamei is a downstream molecule of the NF-κB signaling pathway and participates in antibacterial immune response
- Authors:
- Li, Haoyang
Chen, Yonggui
Li, Ming
Wang, Sheng
Zuo, Hongliang
Xu, Xiaopeng
Weng, Shaoping
He, Jianguo
Li, Chaozheng - Abstract:
- <abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">C-type lectins (CTLs) play multiple roles in innate immune defense against invading pathogens in both vertebrates and invertebrates. In this study, a new C-type lectin gene from pacific white shrimp <italic>Litopenaeus vannamei</italic> (designated as <italic>LvCTL4</italic>) was cloned by rapid amplification of the cDNA ends (RACE) method. The full-length cDNA of <italic>LvCTL4</italic> was 563 bp with open reading frame (ORF) of 471 bp encoding a polypeptide of 156 amino acids, including a putative signal sequence and a single C-type lectin-like domain (CTLD). The CTLD of 137 amino acid residues contained a mutated 'EPA' (Glu<sup>121</sup>-Pro<sup>122</sup>-Ala<sup>123</sup>) motif in the calcium-binding site 2 and three conserved disulfide bonds involved in structure maintenance. Tissue expression analysis showed <italic>LvCTL4</italic> was ubiquitously distributed with high levels in gill, intestine, epithelium and hepatopancreas. The expression of <italic>LvCTL4</italic> in gill was up-regulated in response to <italic>Vibrio parahaemolyticus</italic> challenge. RNAi knock-down of the <italic>LvCTL4</italic> gene significantly increased mortality after <italic>V. parahaemolyticus</italic> infection. A 103 bp 5′ flanking promoter sequence was obtained using the genome walking method and it contained a conserved NF-κB binding motif.<abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">C-type lectins (CTLs) play multiple roles in innate immune defense against invading pathogens in both vertebrates and invertebrates. In this study, a new C-type lectin gene from pacific white shrimp <italic>Litopenaeus vannamei</italic> (designated as <italic>LvCTL4</italic>) was cloned by rapid amplification of the cDNA ends (RACE) method. The full-length cDNA of <italic>LvCTL4</italic> was 563 bp with open reading frame (ORF) of 471 bp encoding a polypeptide of 156 amino acids, including a putative signal sequence and a single C-type lectin-like domain (CTLD). The CTLD of 137 amino acid residues contained a mutated 'EPA' (Glu<sup>121</sup>-Pro<sup>122</sup>-Ala<sup>123</sup>) motif in the calcium-binding site 2 and three conserved disulfide bonds involved in structure maintenance. Tissue expression analysis showed <italic>LvCTL4</italic> was ubiquitously distributed with high levels in gill, intestine, epithelium and hepatopancreas. The expression of <italic>LvCTL4</italic> in gill was up-regulated in response to <italic>Vibrio parahaemolyticus</italic> challenge. RNAi knock-down of the <italic>LvCTL4</italic> gene significantly increased mortality after <italic>V. parahaemolyticus</italic> infection. A 103 bp 5′ flanking promoter sequence was obtained using the genome walking method and it contained a conserved NF-κB binding motif. Dual-Luciferase assay showed both <italic>LvDorsal</italic> and <italic>LvRelish</italic> could up regulate the promoter activity of <italic>LvCTL4</italic>. This is the first report that a shrimp C-type lectin can be regulated by both <italic>LvDorsal</italic> and <italic>LvRelish</italic>. These findings provided novel insights into the regulation of shrimp CTLs expression.</p> </sec> </abstract> … (more)
- Is Part Of:
- Fish & shellfish immunology. Volume 43:Issue 1(2015:Mar.)
- Journal:
- Fish & shellfish immunology
- Issue:
- Volume 43:Issue 1(2015:Mar.)
- Issue Display:
- Volume 43, Issue 1 (2015)
- Year:
- 2015
- Volume:
- 43
- Issue:
- 1
- Issue Sort Value:
- 2015-0043-0001-0000
- Page Start:
- 257
- Page End:
- 263
- Publication Date:
- 2015-03
- Subjects:
- 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.2014.12.024 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3934.880000
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- 3695.xml