A novel lipopolysaccharide-binding protein (LBP) gene from sweetfish Plecoglossus altivelis: Molecular characterization and its role in the immune response of monocytes/macrophages

• Published in: Fish & shellfish immunology 2014-05, Vol.38 (1), p.111-118
• Main Authors: Lu, Xin-Jiang, Chu, Chang-Qing, Chen, Qiang, Chen, Jiong
• Format: Article
• Language: English
• Subjects: Acute-Phase Proteins - genetics; Acute-Phase Proteins - metabolism; Amino Acid Sequence; Animals; Carrier Proteins - genetics; Carrier Proteins - metabolism; Gene Expression Regulation - immunology; Gram-Negative Bacterial Infections - immunology; Gram-Negative Bacterial Infections - microbiology; Gram-Negative Bacterial Infections - veterinary; Immunity, Cellular - physiology; Lipopolysaccharide-binding protein; Listonella; Macrophages - physiology; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Molecular Sequence Data; Monocytes - physiology; Monocytes/macrophages; Osmeriformes - metabolism; Phylogeny; Pro-inflammatory cytokine expression; Respiratory burst; RNA, Messenger - genetics; RNA, Messenger - metabolism; Tissue expression pattern
• ISSN: 1050-4648; 1095-9947
• DOI: 10.1016/j.fsi.2014.02.021

Lipopolysaccharide-binding protein (LBP) belongs to the lipid transfer/LBP (LT–LBP) family, and plays a crucial role in the recognition of bacterial components that modulate cellular signals in phagocytic cells. Although several LBPs have been identified in teleosts, the effects of LBP homologs on teleost phagocytic cells are still obscure. Here, we report the cloning a novel full-length cDNA sequence of LBP-like protein (paLBP) gene from sweetfish, Plecoglossus altivelis. The paLBP cDNA encoded a 464 aa polypeptide, which was closest to that of rainbow smelt (Osmerus mordax). paLBP mRNA was detected mainly in the spleen, liver, and head kidney and levels dramatically increased in various tissues after Listonella anguillarum infection. In contrast to mammalian studies, paLBP mRNA could also be detected in sweetfish monocytes/macrophages. Recombinant paLBP showed LPS-binding activity and Western blot results revealed a significant increase of paLBP in the supernatant of sweetfish monocytes/macrophages challenged with L. anguillarum. Moreover, paLBP neutralization led to up-regulation of IL-1β and TNF-α mRNA as well as respiratory burst activity in sweetfish monocytes/macrophages in response to L. anguillarum or LPS challenge. Therefore, these results suggest that paLBP is an inducible acute-phase protein mediating the immune response of sweetfish monocytes/macrophages upon bacterial challenge. •We characterized a novel LBP gene from sweefish.•Tissue paLBP mRNA was increased in sweetfish upon Listonella anguillarum infection.•paLBP mRNA and protein were expressed in sweetfish monocytes/macrophages.•Anti-paLBP IgG increased cytokine transcripts in LPS treated monocytes/macrophages.