Molecular cloning and characterization of a C-type lectin in yellow catfish Tachysurus fulvidraco
Autor: | H. B. Zhang, Z. F. Wang, H. J. Dong, Y. Wang, X. Y. Cao, L. F. Hou, Fei Ke, G. W. Pan |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Signal peptide Lectin Lactose binding Aquatic Science Biology Tachysurus fulvidraco Molecular cloning biology.organism_classification Molecular biology 03 medical and health sciences CTL 030104 developmental biology Biochemistry C-type lectin biology.protein Ecology Evolution Behavior and Systematics Catfish |
Zdroj: | Journal of Fish Biology. 89:1692-1703 |
ISSN: | 0022-1112 |
DOI: | 10.1111/jfb.13080 |
Popis: | This study represents the first report of a C-type lectin (ctl) in yellow catfish Tachysurus fulvidraco. The complete sequence of ctl complementary (c)DNA consisted of 685 nucleotides. The open reading frame potentially encoded a protein of 177 amino acids with a calculated molecular mass of c.y 20.204 kDa. The deduced amino-acid sequence contained a signal peptide and a single carbohydrate recognition domain with four cysteine residues and GlnProAsp (QPD) and TrpAsnAsp (WND) motifs. Ctl showed the highest identity (56.0%) to the predicted lactose binding lectin from channel catfish Ictalurus punctatus. Quantitative real-time (qrt)-PCR analysis showed that ctl messenger (m)RNA was constitutively expressed in all examined tissues in normal fish, with high expression in trunk kidney and head kidney, which was increased following Aeromonas hydrophila challenge in a duration-dependent manner. Purified recombinant Ctl (rCtl) from Escherichia coli BL21 was able to bind and agglutinate Gram-positive and Gram-negative bacteria in a calcium-dependent manner. These results suggested that Ctl might be a C-type lectin of T. fulvidraco involved in innate immune responses as receptors (PRR). |
Databáze: | OpenAIRE |
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