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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. 45:630-640
- Publication Year :
- 2015
- Publisher :
- Elsevier BV, 2015.
-
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.
- Subjects :
- Fish Proteins
Gills
Lipopolysaccharides
Signal peptide
DNA, Complementary
Lipopolysaccharide
Molecular Sequence Data
Aquatic Science
Kidney
chemistry.chemical_compound
Animals
Environmental Chemistry
Amino Acid Sequence
Membrane Glycoproteins
Base Sequence
biology
Muscles
Binding protein
Fishes
Blood Proteins
pathological conditions, signs and symptoms
General Medicine
Head Kidney
biology.organism_classification
Bactericidal/permeability-increasing protein
Molecular biology
Recombinant Proteins
nervous system diseases
Grass carp
body regions
Open reading frame
Liver
chemistry
Immunology
biology.protein
RNA
population characteristics
Carrier Proteins
Plant lipid transfer proteins
Lipopolysaccharide binding protein
Spleen
Acute-Phase Proteins
Antimicrobial Cationic Peptides
Subjects
Details
- ISSN :
- 10504648
- Volume :
- 45
- Database :
- OpenAIRE
- Journal :
- Fish & Shellfish Immunology
- Accession number :
- edsair.doi.dedup.....1a6affc3708f6183fc2f585c2f1406a9