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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...

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Autores principales: Stolf, Beatriz S., Smyrnias, Ioannis, Lopes, Lucia R., Vendramin, Alcione, Goto, Hiro, Laurindo, Francisco R. M., Shah, Ajay M., Santos, Celio X. C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2011
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.
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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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