Characterization of a CD209-Like Lectin in Black Rockfish(Sebastes schlegelii):Structure Features and Binding Activities as a Pathogen Recognition Receptor  

作　　者：HUO Huijun YANG Tianzhen ZHU Qing LI Chao 

机构地区：[1]School of Marine Science and Engineering,Qingdao Agricultural University,Qingdao 266109,China

出　　处：《Journal of Ocean University of China》2023年第4期1098-1108,共11页中国海洋大学学报（英文版）

基　　金：financially supported by the National Natural Science Foundation of China (No.32002422);the Natural Science Foundation of Shandong Province (No.ZR 2020QC212);the Young Experts of Taishan Scholars (No.tsqn201909130);the Shandong Technical System of Fish Industry (No. SDAIT-12-03);the Science and Technology Support Plan for Youth Innovation of Colleges and Universities in Shandong Province (No. 2019KJF003);the Breeding Plan of Shandong Provincial Qingchuang Research Team (2019);the Advanced Talents Foundation of QAU Grant (No. 663-1120023)

摘　　要：CD209,a transmembrane lectin belonging to the C-type lectin family,can recognize carbohydrates on the surface of host cells and invading pathogens,and play an important role in cell adhesion and migration,pathogen recognition and immune activation.Although well characterized in mammals,CD209 is still under-researched in fish.Here,we report a CD209-like gene,which was named SsCD209like,in black rockfish Sebastes schlegelii,and analyzed its structure features,expression patterns and ligand-binding activities.SsCD209like displays structural similarities to mammalian CD209s,with a cytosolic tail at N-terminus,a transmembrane region and an extracellular part containing a neck region and a CRD at C-terminus.The extracellular region and the neck region of SsCD-209like can both form dimers,which is different with the tetramer in human homologue.This result demonstrates the multimerization of CD209 homologue in fish for the first time.The EPN motif,a functional motif participating in sugar binding and affinity determination,is conserved in the CRD of SsCD209like,which is consistent with the higher binding strength of this lectin to L-fucose,D-GlcNAc and D-mannose.The binding of SsCD209like to different bacteria strains and bacteria-derived pathogen associated molecular patterns(PAMPs)are also observed in a dose-dependent manner.Results in this study show the sequence and structure features of SsCD209like and demonstrate its binding properties as a pathogen recognition receptor,which promotes our understanding of CD209 homologues in fish and provides basis for more in-depth studies of this molecule in the future.

关 键 词：CD209 DC-SIGN pathogen recognition C-type lectin Sebastes schlegelii 

分 类 号：S943[农业科学—水产养殖]