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Enteropathogenic
- Source :
- International Journal of Molecular Sciences
- Publication Year :
- 2019
-
Abstract
- Enteropathogenic Escherichia coli (EPEC) uses a type three secretion system to inject effector proteins into host intestinal epithelial cells, causing diarrhea. EPEC induces the formation of pedestals underlying attached bacteria, disrupts tight junction (TJ) structure and function, and alters apico-basal polarity by redistributing the polarity proteins Crb3 and Pals1, although the mechanisms are unknown. Here we investigate the temporal relationship of PAR polarity complex and TJ disruption following EPEC infection. EPEC recruits active aPKCζ, a PAR polarity protein, to actin within pedestals and at the plasma membrane prior to disrupting TJ. The EPEC effector EspF binds the endocytic protein sorting nexin 9 (SNX9). This interaction impacts actin pedestal organization, recruitment of active aPKCζ to actin at cell–cell borders, endocytosis of JAM-A S285 and occludin, and TJ barrier function. Collectively, data presented herein support the hypothesis that EPEC-induced perturbation of TJ is a downstream effect of disruption of the PAR complex and that EspF binding to SNX9 contributes to this phenotype. aPKCζ phosphorylates polarity and TJ proteins and participates in actin dynamics. Therefore, the early recruitment of aPKCζ to EPEC pedestals and increased interaction with actin at the membrane may destabilize polarity complexes ultimately resulting in perturbation of TJ.
- Subjects :
- enteropathogenic E. coli (EPEC)
atypical aPKCζ
Fluorescent Antibody Technique
Cell Communication
sorting nexin 9 (SNX9)
Article
Tight Junctions
Enteropathogenic Escherichia coli
Mice
Animals
Humans
Protein Interaction Domains and Motifs
polarity
Intestinal Mucosa
Phosphorylation
Sorting Nexins
Escherichia coli Infections
Protein Kinase C
EspF
Cell Polarity
transepithelial electrical resistance (TER)
tight junctions (TJ)
Disease Models, Animal
bacteria
Biomarkers
Protein Binding
Subjects
Details
- ISSN :
- 14220067
- Volume :
- 21
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- International journal of molecular sciences
- Accession number :
- edsair.pmid..........a46974e4bbee1dfee88f4932c0691d09