PUBLICATION
Broad-Spectrum Robust Direct Bactericidal Activity of Fish IFNφ1 Reveals an Antimicrobial Peptide-like Function for Type I IFNs in Vertebrates
- Authors
- Xiao, X., Zhu, W., Zhang, Y., Liao, Z., Wu, C., Yang, C., Zhang, Y., Xiao, S., Su, J.
- ID
- ZDB-PUB-210212-1
- Date
- 2021
- Source
- Journal of immunology (Baltimore, Md. : 1950) 206(6): 1337-1347 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Aeromonas hydrophila/immunology
- Aeromonas hydrophila/isolation & purification
- Amino Acid Sequence
- Animals
- Antimicrobial Cationic Peptides/metabolism*
- Bacterial Load
- Carps/genetics
- Carps/immunology
- Carps/metabolism
- Disease Models, Animal
- Fish Diseases/immunology*
- Fish Diseases/microbiology
- Immunity, Innate
- Interferon Type I/genetics
- Interferon Type I/isolation & purification
- Interferon Type I/metabolism*
- Interferons/genetics
- Interferons/isolation & purification
- Interferons/metabolism*
- Microbial Sensitivity Tests
- Models, Animal
- Recombinant Proteins/genetics
- Recombinant Proteins/isolation & purification
- Recombinant Proteins/metabolism
- Zebrafish/genetics
- Zebrafish/immunology
- Zebrafish/metabolism
- Zebrafish Proteins/genetics
- Zebrafish Proteins/isolation & purification
- Zebrafish Proteins/metabolism*
- PubMed
- 33568398 Full text @ J. Immunol.
Citation
Xiao, X., Zhu, W., Zhang, Y., Liao, Z., Wu, C., Yang, C., Zhang, Y., Xiao, S., Su, J. (2021) Broad-Spectrum Robust Direct Bactericidal Activity of Fish IFNφ1 Reveals an Antimicrobial Peptide-like Function for Type I IFNs in Vertebrates. Journal of immunology (Baltimore, Md. : 1950). 206(6):1337-1347.
Abstract
Type I IFNs (IFN-Is) play pivotal roles in host defense against viral infections but remain enigmatic against bacterial pathogens. In this study, we recombinantly expressed and purified intact grass carp (Ctenopharyngodon idella) IFNφ1 (gcIFNφ1), a teleost IFN-I. gcIFNφ1 widely powerfully directly kills both Gram-negative and Gram-positive bacteria in a dose-dependent manner. gcIFNφ1 binds to LPS or peptidoglycan and provokes bacterial membrane depolarization and disruption, resulting in bacterial death. Furthermore, gcIFNφ1 can efficiently protect zebrafish against Aeromonas hydrophila infection and significantly reduce the bacterial loads in tissues by an infection model. In addition, we wonder whether antibacterial IFN-I members exist in other vertebrates. The amino acid compositions of representative IFN-Is with strong positive charges from Pisces, Amphibia, reptiles, Aves, and Mammalia demonstrate high similarities with those of 2237 reported cationic antimicrobial peptides in antimicrobial peptide database. Recombinant intact representative IFN-I members from the nonmammalian sect exhibit potent broad-spectrum robust bactericidal activity through bacterial membrane depolarization; in contrast, the bactericidal activity is very weak from mammalian IFN-Is. The findings display a broad-spectrum potent direct antimicrobial function for IFN-Is, to our knowledge previously unknown. The results highlight that IFN-Is are important and robust in host defense against bacterial pathogens, and unify direct antibacterial and indirect antiviral bifunction in nonmammalian jawed vertebrates.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping