作者: Anxing Li , Ruijun Li , Yuxi Huang , Xiao Han , Huan Peng
DOI: 10.1016/J.DCI.2021.104040
关键词:
摘要: l-amino acid oxidase (LAAO) is a recently discovered novel fish immune enzyme. To explore the role of LAAO in system bony fishes, we cloned full-length coding sequence (CDS) zebrafish Danio rerio (ZF-LAAO), conducted bioinformatics analysis ZF-LAAO, and analyzed its expression profile infected with pathogen Streptococcus agalactiae. The CDS ZF-LAAO was 1,515 base pairs long, encoded protein contained an 18 amino signal peptide. conserved domains family (dinucleotide binding motif GG-motif), 2 N-glycosylation sites, 2 O-glycosylation it stable hydrophilic exocrine protein. Similarity LAAOs 14 other species >50% all cases. greatest similarity (79.45%) Anabarilius grahami, these two were grouped together phylogenetic tree. In wild-type S. agalactiae, changes gene (zflaao) occurred mainly early stage infection, zflaao more pronounced than those enzyme lysozyme (LYZ). levels both LYZ (zflyz) significantly elevated at 6 h after infection (p < 0.001), but zflyz spleen decreased 12 h whereas liver peaked 12 h. These results provided reference for functional studies fish.