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Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer

Aeromonas sobria is a Gram-negative pathogen that causes food-borne illness. In immunocompromised patients and the elderly, A. sobria opportunistically leads to severe extraintestinal diseases including sepsis, peritonitis, and meningitis. If A. sobria that infects the intestinal tract causes such a...

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Autores principales: Ueda, Mitsunobu, Kobayashi, Hidetomo, Seike, Soshi, Takahashi, Eizo, Okamoto, Keinosuke, Yamanaka, Hiroyasu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8902146/
https://www.ncbi.nlm.nih.gov/pubmed/35273923
http://dx.doi.org/10.3389/fcimb.2022.824547
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author Ueda, Mitsunobu
Kobayashi, Hidetomo
Seike, Soshi
Takahashi, Eizo
Okamoto, Keinosuke
Yamanaka, Hiroyasu
author_facet Ueda, Mitsunobu
Kobayashi, Hidetomo
Seike, Soshi
Takahashi, Eizo
Okamoto, Keinosuke
Yamanaka, Hiroyasu
author_sort Ueda, Mitsunobu
collection PubMed
description Aeromonas sobria is a Gram-negative pathogen that causes food-borne illness. In immunocompromised patients and the elderly, A. sobria opportunistically leads to severe extraintestinal diseases including sepsis, peritonitis, and meningitis. If A. sobria that infects the intestinal tract causes such an extraintestinal infection, the pathogen must pass through the intestinal epithelial barrier. In our earlier study using intestinal cultured cells (T84 cells), we observed that an A. sobria strain with higher A. sobria serine protease (ASP) production caused a marked level of bacterial translocation across the T84 intestinal epithelial monolayer. Herein, we investigated the effect of ASP on tight junctions (TJs) in T84 cells. We observed that ASP acts on TJs and causes the destruction of ZO-1, ZO-2, ZO-3, and claudin-7 (i.e., some of the protein components constituting TJs), especially in the strains with high ASP productivity. Based on the present results together with those of our earlier study, we propose that ASP may cause a disruption of the barrier function of the intestinal epithelium as a whole due to the destruction of TJs (in addition to the destruction of adherens junctions) and that ASP may assist invasion of the pathogens from the intestinal epithelium into deep sites in the human body.
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spelling pubmed-89021462022-03-09 Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer Ueda, Mitsunobu Kobayashi, Hidetomo Seike, Soshi Takahashi, Eizo Okamoto, Keinosuke Yamanaka, Hiroyasu Front Cell Infect Microbiol Cellular and Infection Microbiology Aeromonas sobria is a Gram-negative pathogen that causes food-borne illness. In immunocompromised patients and the elderly, A. sobria opportunistically leads to severe extraintestinal diseases including sepsis, peritonitis, and meningitis. If A. sobria that infects the intestinal tract causes such an extraintestinal infection, the pathogen must pass through the intestinal epithelial barrier. In our earlier study using intestinal cultured cells (T84 cells), we observed that an A. sobria strain with higher A. sobria serine protease (ASP) production caused a marked level of bacterial translocation across the T84 intestinal epithelial monolayer. Herein, we investigated the effect of ASP on tight junctions (TJs) in T84 cells. We observed that ASP acts on TJs and causes the destruction of ZO-1, ZO-2, ZO-3, and claudin-7 (i.e., some of the protein components constituting TJs), especially in the strains with high ASP productivity. Based on the present results together with those of our earlier study, we propose that ASP may cause a disruption of the barrier function of the intestinal epithelium as a whole due to the destruction of TJs (in addition to the destruction of adherens junctions) and that ASP may assist invasion of the pathogens from the intestinal epithelium into deep sites in the human body. Frontiers Media S.A. 2022-02-22 /pmc/articles/PMC8902146/ /pubmed/35273923 http://dx.doi.org/10.3389/fcimb.2022.824547 Text en Copyright © 2022 Ueda, Kobayashi, Seike, Takahashi, Okamoto and Yamanaka https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cellular and Infection Microbiology
Ueda, Mitsunobu
Kobayashi, Hidetomo
Seike, Soshi
Takahashi, Eizo
Okamoto, Keinosuke
Yamanaka, Hiroyasu
Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer
title Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer
title_full Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer
title_fullStr Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer
title_full_unstemmed Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer
title_short Aeromonas sobria Serine Protease Degrades Several Protein Components of Tight Junctions and Assists Bacterial Translocation Across the T84 Monolayer
title_sort aeromonas sobria serine protease degrades several protein components of tight junctions and assists bacterial translocation across the t84 monolayer
topic Cellular and Infection Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8902146/
https://www.ncbi.nlm.nih.gov/pubmed/35273923
http://dx.doi.org/10.3389/fcimb.2022.824547
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