Molecular Characterization and Biological Effects of a C-Type Lectin-Like Receptor in Large Yellow Croaker Larimichthys croceaReport as inadecuate




Molecular Characterization and Biological Effects of a C-Type Lectin-Like Receptor in Large Yellow Croaker Larimichthys crocea - Download this document for free, or read online. Document in PDF available to download.

1

Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China

2

Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Key Laboratory of Marine Genetic Resources of Fujian Province, Xiamen 361005, China

3

Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266071, China





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Academic Editors: Jun Li and Li Lin

Abstract The C-type lectin-like receptors CTLRs play important roles in innate immunity as one type of pattern recognition receptors. Here, we cloned and characterized a C-type lectin-like receptor LycCTLR from large yellow croaker Larimichthys crocea. The full-length cDNA of LycCTLR is 880 nucleotides long, encoding a protein of 215 amino acids. The deduced LycCTLR contains a C-terminal C-type lectin-like domain CTLD, an N-terminal cytoplasmic tail, and a transmembrane region. The CTLD of LycCTLR possesses six highly conserved cysteine residues C1–C6, a conserved WI-MGL motif, and two sugar binding motifs, EPD Glu-Pro-Asp and WYD Trp-Tyr-Asp. Ca2+ binding site 1 and 2 were also found in the CTLD. The LycCTLR gene consists of five exons and four introns, showing the same genomic organization as tilapia Oreochromis niloticus and guppy Poecilia retitculata CTLRs. LycCTLR was constitutively expressed in various tissues tested, and its transcripts significantly increased in the head kidney and spleen after stimulation with inactivated trivalent bacterial vaccine. Recombinant LycCTLR rLycCTLR protein produced in Escherichia coli BL21 exhibited not only the hemagglutinating activity and a preference for galactose, but also the agglutinating activity against two food-borne pathogenic bacteria E. coli and Bacillus cereus in a Ca2+-dependent manner. These results indicate that LycCTLR is a potential galactose-binding C-type lectin that may play a role in the antibacterial immunity in fish. View Full-Text

Keywords: large yellow croaker Larimichthys crocea; C-type lectin-like receptor; hemagglutination; bacterial agglutination; antibacterial immunity large yellow croaker Larimichthys crocea; C-type lectin-like receptor; hemagglutination; bacterial agglutination; antibacterial immunity





Author: Jingqun Ao 1,2, Yang Ding 1,2, Yuanyuan Chen 1,2, Yinnan Mu 1,2 and Xinhua Chen 1,2,3,*

Source: http://mdpi.com/



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