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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...

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Detalles Bibliográficos
Autores principales: Li, Xia, Zhang, Yuhan, Zhao, Yanqing, Qiao, Ke, Feng, Meng, Zhou, Hang, Tachibana, Hiroshi, Cheng, Xunjia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
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.
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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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