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Int. J. Mol. Sci. 2015, 16(12), 29631-29642; doi:10.3390/ijms161226175

Molecular Characterization and Biological Effects of a C-Type Lectin-Like Receptor in Large Yellow Croaker (Larimichthys crocea)

1,2
,
1,2
,
1,2
,
1,2
and
1,2,3,*
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
*
Author to whom correspondence should be addressed.
Academic Editors: Jun Li and Li Lin
Received: 28 October 2015 / Revised: 28 November 2015 / Accepted: 1 December 2015 / Published: 10 December 2015
(This article belongs to the Special Issue Fish Molecular Biology)
View Full-Text   |   Download PDF [3822 KB, uploaded 10 December 2015]   |  

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
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Ao, J.; Ding, Y.; Chen, Y.; Mu, Y.; Chen, X. Molecular Characterization and Biological Effects of a C-Type Lectin-Like Receptor in Large Yellow Croaker (Larimichthys crocea). Int. J. Mol. Sci. 2015, 16, 29631-29642.

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