PUBLICATION
Identification of Ly2 members as antimicrobial peptides from zebrafish Danio rerio
- Authors
- Liu, X., Cao, X., Wang, S., Ji, G., Zhang, S., Li, H.
- ID
- ZDB-PUB-161217-7
- Date
- 2017
- Source
- Bioscience Reports 37(1): (Journal)
- Registered Authors
- Li, Hongyan
- Keywords
- Antimicrobial peptides, Ly6 gene cluster, zebrafish Danio rerio
- MeSH Terms
-
- Aeromonas hydrophila/drug effects*
- Analysis of Variance
- Animals
- Antigens, Ly/chemistry
- Antigens, Ly/genetics
- Antigens, Ly/isolation & purification
- Antigens, Ly/pharmacology*
- Antimicrobial Cationic Peptides/chemistry
- Antimicrobial Cationic Peptides/genetics
- Antimicrobial Cationic Peptides/isolation & purification
- Antimicrobial Cationic Peptides/pharmacology*
- Bacillus subtilis/drug effects
- Erythrocytes/drug effects
- Escherichia coli/drug effects*
- Humans
- Lipopolysaccharides/metabolism
- Mice
- Protein Refolding
- RAW 264.7 Cells/drug effects
- Recombinant Proteins/genetics
- Recombinant Proteins/isolation & purification
- Recombinant Proteins/metabolism
- Recombinant Proteins/pharmacology
- Staphylococcus aureus/drug effects
- Zebrafish/genetics
- Zebrafish/immunology*
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics
- Zebrafish Proteins/isolation & purification
- Zebrafish Proteins/pharmacology*
- PubMed
- 27980020 Full text @ Biosci. Rep.
Citation
Liu, X., Cao, X., Wang, S., Ji, G., Zhang, S., Li, H. (2017) Identification of Ly2 members as antimicrobial peptides from zebrafish Danio rerio. Bioscience Reports. 37(1).
Abstract
The emergence of multi-drug resistant (MDR) microbes caused by overuse of antibiotics leads to urgent demands for novel antibiotics exploration. Our recent data showed that Ly2.1-3 (a novel Ly6 gene cluster) were proteins with cationic nature and rich in cysteines content, that are characteristics of antimicrobial peptides (AMPs), and their expression were all significantly up-regulated after challenge with LPS. These strongly suggested that Ly2.1-3 are potential AMPs, but firm evidences are lacking. Here we clearly showed that the recombinant proteins of Ly2.1-3 were capable of killing Gram-negative bacteria A. hydrophila and E. coli , while they had little bactericidal activity against the Gram-positive bacteria S. aureus and B. subtilis We also showed that rLy2.1-3 were able to bind to the Gram-negative bacteria A. hydrophila , E. coli and the microbial signature molecule LPS, but not to the Gram-positive bacteria S. aureus and B. subtilis as well as the microbial signature molecule LTA. Moreover, the Scatchard analysis revealed that rLy2.1-3 could specifically bind to LPS. Finally, we found that Ly2.1-3 were not cytotoxic to mammalian cells. All these together indicate that Ly2.1-3 can function as AMPs.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping