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Molecular identification and function analysis of bactericidal permeability-increasing protein/LPS-binding protein 1 (BPI/LBP1) from turbot (Scophthalmus maximus)

文献类型: 外文期刊

作者: Zhou, Shun 1 ; Jiang, Guangpeng 1 ; Zhu, Ying 3 ; Liu, Lanhao 1 ; Liu, Danyang 1 ; Diao, Jing 2 ; Liu, Hongjun 2 ; Xiu, Y 1 ;

作者机构: 1.Qingdao Agr Univ, Marine Sci & Engn Coll, Qingdao 266109, Shandong, Peoples R China

2.Marine Biol Inst Shandong Prov, Shandong Key Lab Dis Control Mariculture, Qingdao 266104, Shandong, Peoples R China

3.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Marine Fisheries, Minist Agr, Qingdao 266071, Shandong, Peoples R China

4.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Fisheries Sci & Food Prod Proc, Qingdao 266237, Shandong, Peoples R China

关键词: Bactericidal permeability-increasing protein (BPI); lipopolysaccharide-binding protein (LBP); Scophthabnus maximus; Antibacterial activity; Immune response

期刊名称:FISH & SHELLFISH IMMUNOLOGY ( 影响因子:4.581; 五年影响因子:4.851 )

ISSN: 1050-4648

年卷期: 2019 年 87 卷

页码:

收录情况: SCI

摘要: Bactericidal permeability increasing protein (BPI) and lipopolysaccharide-binding protein (LBP) play important roles in host antimicrobial defense. In the present study, we identified one isoform of BPI/LBP gene from turbot (Scophthabnus maximus), designated as SmBPI/LBP1. The full-length cDNA sequence of SmBPI/LBP1 was 1826 bp, which encoding one secreted protein with 480 amino acid residues. Structurally, the SmBPI/LBP1 showed high similarity to its homologs from other vertebrates or invertebrates, which all contained a signal peptide, a BPI/LBP/CETP N-terminal with a LPS-binding domain, and a BPI/LBP/CETP C-terminal domain. The deduced amino acid sequences of SmBPI/LBP1 shared significant similarity to BPI/LBP of Seriola lalandi dorsalis (71%) and Paralichthys olivaceus (69%). Phylogentic analysis further supported that SmBPI/LBP1 act as a new member of vertebrate BPI/LBP family. SmBPI/LBP1 was ubiquitously expressed in all tested tissues, with the highest expression level in spleen tissue. The mRNA expression of SmBPI/LBP1 in spleen and kidney were significantly up-regulated after Vibrio vulnificus challenge. Finally, the recombinant SmBPI/LBP1 showed high affinity to lipopolysaccharide, followed by peptidoglycan and lipoteichoic acid, which is the ubiquitous component of Gram-negative or Gram-positive bacteria. These results indicated that SmBPI/LBP1 probably played important roles in immune response against bacteria infection.

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