The roles of flp1 and tadD in Actinobacillus pleuropneumoniae pilus biosynthesis and pathogenicity.
Actinobacillus Infections
/ blood
Actinobacillus pleuropneumoniae
/ growth & development
Animals
Bacterial Adhesion
/ genetics
Bacterial Proteins
/ genetics
Biofilms
/ growth & development
Cell Line
Disease Models, Animal
Female
Fimbriae Proteins
/ genetics
Fimbriae, Bacterial
/ genetics
Gene Expression Regulation, Bacterial
Genes, Bacterial
Homologous Recombination
Mice, Inbred BALB C
Microbial Viability
Phagocytosis
Phenotype
Sequence Deletion
Virulence
Actinobacillus pleuropneumoniae
Flp pilus
Pathogenicity
flp1
tadD
Journal
Microbial pathogenesis
ISSN: 1096-1208
Titre abrégé: Microb Pathog
Pays: England
ID NLM: 8606191
Informations de publication
Date de publication:
Jan 2019
Jan 2019
Historique:
received:
04
07
2018
revised:
02
11
2018
accepted:
05
11
2018
pubmed:
13
11
2018
medline:
5
3
2019
entrez:
13
11
2018
Statut:
ppublish
Résumé
Pili have been demonstrated to contribute to the pathogenicity of many bacterial pathogens. Flp pilus encoded by the tad locus belongs to the type IVb pilus. Our previous study has revealed that the intact tad locus is essential for Flp pilus formation in Actinobacillus pleuropneumoniae, a very important porcine respiratory pathogen. To further investigate the functions of Flp pilus in A. pleuropneumoniae pathogenesis, the flp1 and tadD single deletion mutants were constructed by homologous recombination. Both of the mutant strains lost pilus on their cell surfaces. The abilities of biofilm formation, cell adhesion, resistance to phagocytosis, survival in swine whole blood, and in vivo colonization of the two mutants were significantly reduced compared with those of the parental strain. The corresponding complemented strains recovered the phenotypes. These results demonstrated that flp1 and tadD were essential for the biosynthesis of Flp pilus and that the pilus played important roles during infection of A. pleuropneumoniae.
Identifiants
pubmed: 30419341
pii: S0882-4010(18)31209-9
doi: 10.1016/j.micpath.2018.11.010
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Fimbriae Proteins
147680-16-8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
310-317Informations de copyright
Copyright © 2018 Elsevier Ltd. All rights reserved.