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Autophagy Activated by Peroxiredoxin of Entamoeba histolytica
Autophagy, an evolutionarily conserved mechanism to remove redundant or dangerous cellular components, plays an important role in innate immunity and defense against pathogens, which, in turn, can regulate autophagy to establish infection within a host. However, for Entamoeba histolytica, an intesti...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7696310/ https://www.ncbi.nlm.nih.gov/pubmed/33198056 http://dx.doi.org/10.3390/cells9112462 |
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author | Li, Xia Zhang, Yuhan Zhao, Yanqing Qiao, Ke Feng, Meng Zhou, Hang Tachibana, Hiroshi Cheng, Xunjia |
author_facet | Li, Xia Zhang, Yuhan Zhao, Yanqing Qiao, Ke Feng, Meng Zhou, Hang Tachibana, Hiroshi Cheng, Xunjia |
author_sort | Li, Xia |
collection | PubMed |
description | Autophagy, an evolutionarily conserved mechanism to remove redundant or dangerous cellular components, plays an important role in innate immunity and defense against pathogens, which, in turn, can regulate autophagy to establish infection within a host. However, for Entamoeba histolytica, an intestinal protozoan parasite causing human amoebic colitis, the interaction with the host cell autophagy mechanism has not been investigated. In this study, we found that E. histolytica peroxiredoxin (Prx), an antioxidant enzyme critical for parasite survival during the invasion of host tissues, could activate autophagy in macrophages. The formation of autophagosomes in macrophages treated with recombinant Prx of E. histolytica for 24 h was revealed by immunofluorescence and immunoblotting in RAW264.7 cells and in mice. Prx was cytotoxic for RAW264.7 macrophages after 48-h treatment, which was partly attributed to autophagy-dependent cell death. RNA interference experiments revealed that Prx induced autophagy mostly through the toll-like receptor 4 (TLR4)–TIR domain-containing adaptor-inducing interferon (TRIF) pathway. The C-terminal part of Prx comprising 100 amino acids was the key functional domain to activate autophagy. These results indicated that Prx of E. histolytica could induce autophagy and cytotoxic effects in macrophages, revealing a new pathogenic mechanism activated by E. histolytica in host cells. |
format | Online Article Text |
id | pubmed-7696310 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76963102020-11-29 Autophagy Activated by Peroxiredoxin of Entamoeba histolytica Li, Xia Zhang, Yuhan Zhao, Yanqing Qiao, Ke Feng, Meng Zhou, Hang Tachibana, Hiroshi Cheng, Xunjia Cells Article Autophagy, an evolutionarily conserved mechanism to remove redundant or dangerous cellular components, plays an important role in innate immunity and defense against pathogens, which, in turn, can regulate autophagy to establish infection within a host. However, for Entamoeba histolytica, an intestinal protozoan parasite causing human amoebic colitis, the interaction with the host cell autophagy mechanism has not been investigated. In this study, we found that E. histolytica peroxiredoxin (Prx), an antioxidant enzyme critical for parasite survival during the invasion of host tissues, could activate autophagy in macrophages. The formation of autophagosomes in macrophages treated with recombinant Prx of E. histolytica for 24 h was revealed by immunofluorescence and immunoblotting in RAW264.7 cells and in mice. Prx was cytotoxic for RAW264.7 macrophages after 48-h treatment, which was partly attributed to autophagy-dependent cell death. RNA interference experiments revealed that Prx induced autophagy mostly through the toll-like receptor 4 (TLR4)–TIR domain-containing adaptor-inducing interferon (TRIF) pathway. The C-terminal part of Prx comprising 100 amino acids was the key functional domain to activate autophagy. These results indicated that Prx of E. histolytica could induce autophagy and cytotoxic effects in macrophages, revealing a new pathogenic mechanism activated by E. histolytica in host cells. MDPI 2020-11-12 /pmc/articles/PMC7696310/ /pubmed/33198056 http://dx.doi.org/10.3390/cells9112462 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Li, Xia Zhang, Yuhan Zhao, Yanqing Qiao, Ke Feng, Meng Zhou, Hang Tachibana, Hiroshi Cheng, Xunjia Autophagy Activated by Peroxiredoxin of Entamoeba histolytica |
title | Autophagy Activated by Peroxiredoxin of Entamoeba histolytica |
title_full | Autophagy Activated by Peroxiredoxin of Entamoeba histolytica |
title_fullStr | Autophagy Activated by Peroxiredoxin of Entamoeba histolytica |
title_full_unstemmed | Autophagy Activated by Peroxiredoxin of Entamoeba histolytica |
title_short | Autophagy Activated by Peroxiredoxin of Entamoeba histolytica |
title_sort | autophagy activated by peroxiredoxin of entamoeba histolytica |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7696310/ https://www.ncbi.nlm.nih.gov/pubmed/33198056 http://dx.doi.org/10.3390/cells9112462 |
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