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Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli
Enteropathogenic Escherichia coli (EPEC) infection causes a histopathological lesion including recruitment of F‐actin beneath the attached bacteria and formation of actin‐rich pedestal‐like structures. Another important target of EPEC is the tight junction (TJ), and EspF induces displacement of TJ p...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6925160/ https://www.ncbi.nlm.nih.gov/pubmed/31568664 http://dx.doi.org/10.1002/mbo3.931 |
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author | Ugalde‐Silva, Paul Navarro‐Garcia, Fernando |
author_facet | Ugalde‐Silva, Paul Navarro‐Garcia, Fernando |
author_sort | Ugalde‐Silva, Paul |
collection | PubMed |
description | Enteropathogenic Escherichia coli (EPEC) infection causes a histopathological lesion including recruitment of F‐actin beneath the attached bacteria and formation of actin‐rich pedestal‐like structures. Another important target of EPEC is the tight junction (TJ), and EspF induces displacement of TJ proteins and increased intestinal permeability. Previously, we determined that an EPEC strain lacking EspF did not cause TJ disruption; meanwhile, pedestals were located on the TJ and smaller than those induced by the wild‐type strain. Therefore, EspF could be playing an important role in both phenotypes. Here, using different cell models, we found that EspF was essential for pedestal maturation through ZO‐1 disassembly from TJ, leading to (a) ZO‐1 recruitment to the pedestal structure; no other main TJ proteins were required. Recruited ZO‐1 allowed the afadin recruitment. (b) Afadin recruitment caused an afadin–ZO‐1 transient interaction, like during TJ formation. (c) Afadin and ZO‐1 were segregated to the tip and the stem of pedestal, respectively, causing pedestal maturation. Initiation of these three discrete phases for pedestal maturation functionally and physically required EspF expression. Pedestal maturation process could help coordinate the epithelial actomyosin function by maintaining the actin‐rich column composing the pedestal structure and could be important in the dynamics of the pedestal movement on epithelial cells. |
format | Online Article Text |
id | pubmed-6925160 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-69251602019-12-24 Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli Ugalde‐Silva, Paul Navarro‐Garcia, Fernando Microbiologyopen Original Articles Enteropathogenic Escherichia coli (EPEC) infection causes a histopathological lesion including recruitment of F‐actin beneath the attached bacteria and formation of actin‐rich pedestal‐like structures. Another important target of EPEC is the tight junction (TJ), and EspF induces displacement of TJ proteins and increased intestinal permeability. Previously, we determined that an EPEC strain lacking EspF did not cause TJ disruption; meanwhile, pedestals were located on the TJ and smaller than those induced by the wild‐type strain. Therefore, EspF could be playing an important role in both phenotypes. Here, using different cell models, we found that EspF was essential for pedestal maturation through ZO‐1 disassembly from TJ, leading to (a) ZO‐1 recruitment to the pedestal structure; no other main TJ proteins were required. Recruited ZO‐1 allowed the afadin recruitment. (b) Afadin recruitment caused an afadin–ZO‐1 transient interaction, like during TJ formation. (c) Afadin and ZO‐1 were segregated to the tip and the stem of pedestal, respectively, causing pedestal maturation. Initiation of these three discrete phases for pedestal maturation functionally and physically required EspF expression. Pedestal maturation process could help coordinate the epithelial actomyosin function by maintaining the actin‐rich column composing the pedestal structure and could be important in the dynamics of the pedestal movement on epithelial cells. John Wiley and Sons Inc. 2019-09-30 /pmc/articles/PMC6925160/ /pubmed/31568664 http://dx.doi.org/10.1002/mbo3.931 Text en © 2019 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Ugalde‐Silva, Paul Navarro‐Garcia, Fernando Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli |
title | Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli
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title_full | Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli
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title_fullStr | Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli
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title_full_unstemmed | Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli
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title_short | Coordinated transient interaction of ZO‐1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli
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title_sort | coordinated transient interaction of zo‐1 and afadin is required for pedestal maturation induced by espf from enteropathogenic escherichia coli |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6925160/ https://www.ncbi.nlm.nih.gov/pubmed/31568664 http://dx.doi.org/10.1002/mbo3.931 |
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