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Riemerella anatipestifer gene AS87_08785 encodes a functional component, GldK, of the type IX secretion system
- Source :
- Veterinary Microbiology. 231:93-99
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- Riemerella anatipestifer is an important pathogen of waterfowl, causing septicemic and exudative diseases. In our previous study, we demonstrated that the deletion of the AS87_08785 gene significantly reduced the virulence of R. anatipestifer strain Yb2, but the mechanism remained unclear. In this study, R. anatipestifer strains with mutated or complemented AS87_08785 genes were constructed and characterized. A sequence analysis indicated that the AS87_08785 gene encoded a putative GldK protein, which localized to the membrane fraction in a western blotting analysis. The mutant strain Yb2ΔgldK displayed defective gliding motility on agar plates, reduced protease activity, and a reduced capacity for protein secretion. RNA sequencing and quantitative PCR analyses indicated that the transcription of 13 genes was downregulated in mutant Yb2ΔgldK. Animal experiments showed that the bacterial loads in the blood of Yb2ΔgldK-infected ducks were significantly reduced relative to those in wild-type strain Yb2 infected ducks. Most of the defective biological properties of the mutant were restored in complementation strain cYb2ΔgldK. Our results demonstrated that R. anatipestifer gene AS87_08785 encoded a component of the type IX secretion system, GldK, which functioned in bacterial gliding motility, protein secretion, and bacterial virulence.
- Subjects :
- Virulence Factors
Gliding motility
Sequence analysis
Mutant
Gene Expression
Virulence
Biology
Polymerase Chain Reaction
Microbiology
Bacterial Adhesion
Type IV Secretion Systems
Riemerella
03 medical and health sciences
Flavobacteriaceae Infections
Animals
Secretion
Gene
Poultry Diseases
030304 developmental biology
0303 health sciences
General Veterinary
Sequence Analysis, RNA
030306 microbiology
Riemerella anatipestifer
General Medicine
Molecular biology
Bacterial Load
Complementation
Ducks
Mutation
Peptide Hydrolases
Subjects
Details
- ISSN :
- 03781135
- Volume :
- 231
- Database :
- OpenAIRE
- Journal :
- Veterinary Microbiology
- Accession number :
- edsair.doi.dedup.....94f152d684dbeba46115e83bf1bcfaa1