Molecular characterization of a transmembrane C-type lectin receptor gene from ayu (Plecoglossus altivelis) and its effect on the recognition of different bacteria by monocytes/macrophages

Zhang, Xueheng; Shi, Yu-Hong; Chen, Jiong

doi:10.1016/j.molimm.2015.05.009

Cited by 26 publications

(13 citation statements)

References 35 publications

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“…Headkidney-derived MO/MФ cells were also isolated and cultured as previously described (Zhang, Shi, & Chen, 2015). Briefly, the head-kidney leukocyte-enriched fraction was obtained with Ficoll-Hypaque PREMIUM (1.077 g/mL) (GE Healthcare, New Jersey, USA), following manufacturer protocol.…”

Section: Cell Preparationsmentioning

confidence: 99%

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Li¹,

Ding²,

Chen³

et al. 2018

Turk. J. Fish. Aquat. Sci.

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The MHC (major histocompatibility complex) class II family plays a major role in vertebrate immune systems and is normally found only on antigen-presenting cells. In this study, we identified the gene encoding the α (PaMHCIIα) chain of MHC class II molecules in ayu (Plecoglossus altivelis). Phylogenetic analysis showed that PaMHCIIα was tightly grouped with MHC class IIα in rainbow smelt (Osmerus mordax) and salmon. PaMHCIIα transcripts were detected in all tested tissues, with high levels in the spleen, head kidney, and gill; expression increased significantly upon Vibrio anguillarum infection. PaMHCIIα mRNA expression was also up-regulated in monocytes/macrophages (MO/MФ) after in vitro stimulation with V. anguillarum. We prepared antibodies for detecting N-glycosylation of PaMHCIIα or neutralizing PaMHCIIα on ayu MO/MФ. Western blot analysis showed that native PaMHCIIα was indeed N-glycosylated. Moreover, PaMHCIIα neutralization not only significantly inhibited ayu MO/MФ phagocytosis, but also reduced the ability of V. anguillarum to induce MO/MФ-cytokine expression. Overall, these findings reveal that the important role of PaMHCIIα against bacterial challenge, and it likely contributes to pathogen responsiveness in ayu MO/MФ.

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Section: Cell Preparationsmentioning

confidence: 99%

“…Finally, rPaMHCIIαex was inoculated into mice to produce antiserum. Antibody production and detection was performed as previously described (Zhang, Shi, & Chen, 2015).…”

Section: Prokaryotic Expression and Antibody Preparationmentioning

confidence: 99%

Untitled

Li¹,

Ding²,

Chen³

et al. 2018

Turk. J. Fish. Aquat. Sci.

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“…In particular, the primary function of CRD domain is to recognize antigens with carbohydrate residues located on the surface of pathogens. In previous studies, rPaCTLRC bound to LPS, PGN, D-mannose, D-galactose, L-fucose, and N-acetyl-D-glucosamine (GlcNAc), exhibiting a relative binding strength to D-mannose and PGN (23). rCaNTC could bind to polysaccharides, including LPS and PGN, exhibiting a dose-dependent manner (13).…”

Section: Discussionmentioning

confidence: 92%

“…rCaNTC displayed agglutinating activity against Gram-negative bacteria (E. coli and A. hydrophila) and Grampositive bacteria (S. aureus) in the presence of Ca 2+ (13). In ayu P. altivelis, rPaCTLRC agglutinated three Gram-positive bacteria (Listeria monocytogenes, S. aureus, and Streptococcus iniae) and four Gram-negative bacteria (A. hydrophila, E. coli, V. anguillarum, and V. parahaemolyticus) in vitro (23). CTLs are involved in host immune defense, and agglutinating activity against pathogens indicates the relative binding affinity of CTLs to pathogens.…”

Section: Discussionmentioning

confidence: 99%

Characterization and Functional Analysis of Two Transmembrane C-Type Lectins in Obscure Puffer (Takifugu obscurus)

Huang

Shi

et al. 2020

Front. Immunol.

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C-type lectins (CTLs) have received widespread attention in animal immune responses. In the present study, two CTLs (ToCTL1 and ToCTL2) were identified from obscure puffer Takifugu obscurus. The open reading frames of ToCTL1 and ToCTL2 were 687 and 1,380 bp, respectively. The predicted ToCTL1 and ToCTL2 proteins contained a single transmembrane region and one typical carbohydrate recognition domain (CRD). Quantitative real-time polymerase chain reaction detected ToCTL1 and ToCTL2 transcripts in all examined tissues, with high levels in the intestine and kidney, and their expression levels were remarkably altered upon Vibrio harveyi and Aeromonas hydrophila infection. The recombinant proteins ToCTL1-CRD and ToCTL2-CRD agglutinated the Gram-negative and Gram-positive bacteria in a Ca 2+-dependent manner. rToCTL1-CRD and rToCTL2-CRD exhibited evident binding activities against seven kinds of bacteria and polysaccharides (lipopolysaccharide and peptidoglycan) in a Ca 2+-independent manner. Moreover, rToCTL1-CRD and rToCTL2-CRD could inhibit the growth of four types of bacteria in vitro. These findings collectively demonstrated that ToCTL1 and ToCTL2 could be involved in host defense against bacterial infection in T. obscurus.

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“…At present, many fish CTLR genes have been identified, such as natural killer cell CTLR genes in cichlid fish ( Paralabidochromis chilotes ) and Nile tilapia ( Oreochromis niloticus ) [ 9 ], three kinds of CTLR (CTLR A, B, and C) genes in Atlantic salmon ( Salmo salar ) [ 10 ], lectin-like receptor genes in zebrafish ( Danio rerio ) [ 11 , 12 ], mannose receptor (MR) genes in blunt snout bream ( Megalobrama amblycephala ) and grass carp ( Ctenopharyngodon idella ) [ 13 , 14 ], and three CTLR-like genes in ayu ( Plecoglossus altivelis ) [ 15 , 16 , 17 ]. In ayu, a CTLR-like protein PaCD209L could bind Gram-negative and Gram-positive bacteria in the absence of Ca 2 + and plays a role in the regulation of the phagocytosis and bacterial killing of monocytes/macrophages (MO/Mϕ) [ 16 ], while another CTLR (PaCTLRC) agglutinates several Gram-negative and Gram-positive bacteria in a Ca 2+ -dependent manner [ 17 ]. Blunt snout bream MR has been found to mediate phagocytosis of bacteria in macrophages in a Ca 2+ -dependent manner [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

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

Ding

Chen

et al. 2015

IJMS

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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.

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Molecular characterization of a transmembrane C-type lectin receptor gene from ayu (Plecoglossus altivelis) and its effect on the recognition of different bacteria by monocytes/macrophages

Cited by 26 publications

References 35 publications

Untitled

Untitled

Characterization and Functional Analysis of Two Transmembrane C-Type Lectins in Obscure Puffer (Takifugu obscurus)

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

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