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Protein Disulfide Isomerase and Host-Pathogen Interaction
Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways in the host-pathogen interaction. These especia...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3201685/ https://www.ncbi.nlm.nih.gov/pubmed/22125433 http://dx.doi.org/10.1100/2011/289182 |
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author | Stolf, Beatriz S. Smyrnias, Ioannis Lopes, Lucia R. Vendramin, Alcione Goto, Hiro Laurindo, Francisco R. M. Shah, Ajay M. Santos, Celio X. C. |
author_facet | Stolf, Beatriz S. Smyrnias, Ioannis Lopes, Lucia R. Vendramin, Alcione Goto, Hiro Laurindo, Francisco R. M. Shah, Ajay M. Santos, Celio X. C. |
author_sort | Stolf, Beatriz S. |
collection | PubMed |
description | Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways in the host-pathogen interaction. These especially affect (i) pathogen entry through protein redox switches and redox modification (i.e., intra- and interdisulfide and cysteine oxidation) and (ii) phagocytic ROS production via Nox family NADPH oxidase enzyme and the control of phagolysosome function with key implications for antigen processing. The protein disulfide isomerase (PDI) family of redox chaperones is closely involved in both processes and is also implicated in protein unfolding and trafficking across the endoplasmic reticulum (ER) and towards the cytosol, a thiol-based redox locus for antigen processing. Here, we summarise examples of the cellular association of host PDI with different pathogens and explore the possible roles of pathogen PDIs in infection. A better understanding of these complex regulatory steps will provide insightful information on the redox role and coevolutional biological process, and assist the development of more specific therapeutic strategies in pathogen-mediated infections. |
format | Online Article Text |
id | pubmed-3201685 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-32016852011-11-28 Protein Disulfide Isomerase and Host-Pathogen Interaction Stolf, Beatriz S. Smyrnias, Ioannis Lopes, Lucia R. Vendramin, Alcione Goto, Hiro Laurindo, Francisco R. M. Shah, Ajay M. Santos, Celio X. C. ScientificWorldJournal Review Article Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways in the host-pathogen interaction. These especially affect (i) pathogen entry through protein redox switches and redox modification (i.e., intra- and interdisulfide and cysteine oxidation) and (ii) phagocytic ROS production via Nox family NADPH oxidase enzyme and the control of phagolysosome function with key implications for antigen processing. The protein disulfide isomerase (PDI) family of redox chaperones is closely involved in both processes and is also implicated in protein unfolding and trafficking across the endoplasmic reticulum (ER) and towards the cytosol, a thiol-based redox locus for antigen processing. Here, we summarise examples of the cellular association of host PDI with different pathogens and explore the possible roles of pathogen PDIs in infection. A better understanding of these complex regulatory steps will provide insightful information on the redox role and coevolutional biological process, and assist the development of more specific therapeutic strategies in pathogen-mediated infections. Hindawi Publishing Corporation 2011-10-11 /pmc/articles/PMC3201685/ /pubmed/22125433 http://dx.doi.org/10.1100/2011/289182 Text en Copyright © 2011 Beatriz S. Stolf et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Stolf, Beatriz S. Smyrnias, Ioannis Lopes, Lucia R. Vendramin, Alcione Goto, Hiro Laurindo, Francisco R. M. Shah, Ajay M. Santos, Celio X. C. Protein Disulfide Isomerase and Host-Pathogen Interaction |
title | Protein Disulfide Isomerase and Host-Pathogen Interaction |
title_full | Protein Disulfide Isomerase and Host-Pathogen Interaction |
title_fullStr | Protein Disulfide Isomerase and Host-Pathogen Interaction |
title_full_unstemmed | Protein Disulfide Isomerase and Host-Pathogen Interaction |
title_short | Protein Disulfide Isomerase and Host-Pathogen Interaction |
title_sort | protein disulfide isomerase and host-pathogen interaction |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3201685/ https://www.ncbi.nlm.nih.gov/pubmed/22125433 http://dx.doi.org/10.1100/2011/289182 |
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