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Identification and expression analysis on bactericidal permeability-increasing protein/lipopolysaccharide-binding protein of blunt snout bream, Megalobrama amblycephala.
- Source :
-
Fish & shellfish immunology [Fish Shellfish Immunol] 2015 Aug; Vol. 45 (2), pp. 630-40. Date of Electronic Publication: 2015 May 14. - Publication Year :
- 2015
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Abstract
- Bactericidal permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP) belong to the lipid transfer protein/lipopolysaccharide-binding protein family and play a critical role in the innate immune response to Gram-negative bacteria. In the present study, a novel BPI/LBP from blunt snout bream, Megalobrama amblycephala (maBPI/LBP) was isolated by RACE techniques. The open reading frame (ORF) of maBPI/LBP gene encoded a polypeptide of 474 amino acids with a putative 18-aa hydrophobic signal peptide. Structurally, the maBPI/LBP showed highly similar to those of BPI/LBPs from invertebrate and teleost, LBPs and BPIs from mammal, which contained an N-terminal BPI/LBP/CETP domain BPI1 with a LPS-binding domain, a C-terminal BPI/LBP/CETP domain BPI2, and proline-rich domain. The homologous identities of deduced amino acid sequences displayed that the maBPI/LBP possessed significant similarity (96.61% and 90.07%) with those of grass carp and common carp, respectively. The recombinant protein of maBPI/LBP showed effectively kill Gram-negative bacteria. The maBPI/LBP gene was expressed in a wide range of normal tested tissues, with the highest expression levels in the kidney. The experiments revealed that the mRNA expression of maBPI/LBP in spleen considerably up-regulated from 2 h to 8 h post LPS stimulation, and peaked rapidly at 2 h (7.40-fold, P < 0.05), which confirmed that maBPI/LBP was the absolute sensitive to LPS stimulation. Furthermore, the level of maBPI/LBP mRNA expression reached the maximum for a second time at 24 h after LPS stimulation. These results suggested that maBPI/LBP was a constitutive and inducible acute-phase protein contributing to the host immune defense against pathogenic bacterial infection in M. amblycephala. This study will further our understanding of the function of BPI/LBP and the molecular mechanism of innate immunity in teleost.<br /> (Copyright © 2015 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
DNA, Complementary genetics
Gills metabolism
Head Kidney metabolism
Kidney metabolism
Lipopolysaccharides pharmacology
Liver metabolism
Molecular Sequence Data
Muscles metabolism
RNA genetics
Recombinant Proteins genetics
Recombinant Proteins immunology
Recombinant Proteins metabolism
Spleen immunology
Spleen metabolism
Acute-Phase Proteins genetics
Acute-Phase Proteins immunology
Acute-Phase Proteins metabolism
Antimicrobial Cationic Peptides genetics
Antimicrobial Cationic Peptides immunology
Antimicrobial Cationic Peptides metabolism
Blood Proteins genetics
Blood Proteins immunology
Blood Proteins metabolism
Carrier Proteins genetics
Carrier Proteins immunology
Carrier Proteins metabolism
Fish Proteins genetics
Fish Proteins immunology
Fish Proteins metabolism
Fishes genetics
Fishes immunology
Membrane Glycoproteins genetics
Membrane Glycoproteins immunology
Membrane Glycoproteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9947
- Volume :
- 45
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Fish & shellfish immunology
- Publication Type :
- Academic Journal
- Accession number :
- 25982396
- Full Text :
- https://doi.org/10.1016/j.fsi.2015.05.013