Streptococcus suis suilysin compromises the function of a porcine tracheal epithelial barrier model.
Epithelial barrier
Respiratory epithelial cells
Streptococcus suis
Suilysin
Journal
Microbial pathogenesis
ISSN: 1096-1208
Titre abrégé: Microb Pathog
Pays: England
ID NLM: 8606191
Informations de publication
Date de publication:
Feb 2020
Feb 2020
Historique:
received:
06
06
2019
revised:
29
11
2019
accepted:
03
12
2019
pubmed:
10
12
2019
medline:
27
10
2020
entrez:
10
12
2019
Statut:
ppublish
Résumé
Streptococcus suis is a bacterial pathogen that mainly colonizes the upper respiratory tract of pigs. It is known to cause severe infections such as septicemia, meningitis, arthritis, and endocarditis in pigs and to be responsible for major economic losses in the swine industry worldwide. To better understand the interactions between S. suis and the porcine respiratory epithelium, we investigated the ability of this pathogen to cause damage to the tracheal epithelial barrier. We showed that S. suis compromises the integrity of a tracheal epithelial barrier model as determined by measuring transepithelial electrical resistance and paracellular flux of FITC-dextran. As a consequence of this breakdown, S. suis translocates across the epithelial cell monolayer. On the other hand, a S. suis mutant deficient in the production of suilysin, a cholesterol-dependent cytolysin, was significantly impaired in its ability to cause damage to the epithelial barrier. In addition, a recombinant suilysin disrupted the integrity of the tracheal epithelial barrier. Immunofluorescence staining suggested that suilysin affects two major tight junction proteins (occludin and zonula occludens-1). In summary, S. suis is able to compromise the function of the porcine respiratory epithelial barrier through the action of suilysin. This better knowledge of the interactions between S. suis and tracheal epithelial cells may help in the development of novel strategies to prevent the invasion of the epithelium by this and other swine respiratory pathogens.
Identifiants
pubmed: 31816403
pii: S0882-4010(19)31024-1
doi: 10.1016/j.micpath.2019.103913
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Hemolysin Proteins
0
suilysin
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
103913Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no conflicts of interest.