期刊
AQUACULTURE
卷 545, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.aquaculture.2021.737195
关键词
Oreochromis niloticus; RBL-1; Agglutination; Streptococcus agalactiae; Aeromonas hydrophila
资金
- National Natural Science Foundation of China [31902396, 31972818]
- Natural Science Foundation of Guangdong Province (Guangdong Natural Science Foundation) [2019A1515012065]
- China Postdoctoral Science Foundation [2019 M652942]
- Open Foundation of Guangdong Provincial Key Laboratory of Pathogenic Biology and Epidemiology for Aquatic Economic Animals [PBEA2020YB02]
In this study, an L-rhamnose-binding lectin-like (OnRBL-1) was identified and characterized in Nile tilapia, showing its important role in recognition and agglutination of bacterial pathogens. The expression of OnRBL-1 was significantly upregulated in various tissues following challenges with pathogenic bacteria, indicating its involvement in the innate immune defense of O. niloticus.
Rhamnose-binding lectins (RBLs), a Ca2+-independent lectin family, are able to recognize varieties of pathogens and involve in the innate immune response. In this study, an L-rhamnose-binding lectin-like (OnRBL-1) was identified and functionally characterized from Nile tilapia (Oreochromis niloticus). The open reading frame of OnRBL-1 is 702 bp encoding 233 amino acids. The sequence of OnRBL-1 has relatively conservative characteristic peptide motifs, including YGR, DPC, and KYL-motif. Expression analysis showed that OnRBL-1 was abundantly distributed in liver tissue, and widely existed in all detected tissues. Meanwhile, the expressions of OnRBL-1 increased significantly in vivo (liver, spleen, head kidney, intestine, gills and peripheral blood) and in vitro (hepatocytes) following challenges with two important tilapia pathogenic bacteria Streptococcus agalactiae and Aeromonas hydrophila. Moreover, the recombinant OnRBL-1 was expressed and purified, which was found to bind and agglutinate S. agalactiae and A. hydrophila. Overall, This study indicated that OnRBL-1 may function as an important pattern recognition molecule, possessing recognition and agglutination activity to bacterial pathogens, thus involving in the innate immune defense of O. niloticus.
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