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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| Format: | Article |
| Language: | English |
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Wiley
2011-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1100/2011/289182 |
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| author | Beatriz S. Stolf Ioannis Smyrnias Lucia R. Lopes Alcione Vendramin Hiro Goto Francisco R. M. Laurindo Ajay M. Shah Celio X. C. Santos |
| author_facet | Beatriz S. Stolf Ioannis Smyrnias Lucia R. Lopes Alcione Vendramin Hiro Goto Francisco R. M. Laurindo Ajay M. Shah Celio X. C. Santos |
| author_sort | Beatriz S. Stolf |
| collection | DOAJ |
| 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 | Article |
| id | doaj-art-8aeb7bc3d65c4b82b06aefbed6948c70 |
| institution | Kabale University |
| issn | 1537-744X |
| language | English |
| publishDate | 2011-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-8aeb7bc3d65c4b82b06aefbed6948c702025-02-03T05:50:56ZengWileyThe Scientific World Journal1537-744X2011-01-01111749176110.1100/2011/289182289182Protein Disulfide Isomerase and Host-Pathogen InteractionBeatriz S. Stolf0Ioannis Smyrnias1Lucia R. Lopes2Alcione Vendramin3Hiro Goto4Francisco R. M. Laurindo5Ajay M. Shah6Celio X. C. Santos7Department of Parasitology, University of São Paulo, São Paulo, SP, BrazilCardiovascular Division, British Heart Foundation Centre, King's College London, 125 Coldharbour Lane, London SE5 9NU, UKDepartment of Pharmacology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, BrazilDepartment of Parasitology, School of Medicine of Jundiaí, São Paulo, SP, BrazilSchool of Medicine and Tropical Medicine Institute, University of São Paulo, São Paulo, SP, BrazilVascular Biology Laboratory, Heart Institute (InCor), São Paulo, BrazilCardiovascular Division, British Heart Foundation Centre, King's College London, 125 Coldharbour Lane, London SE5 9NU, UKCardiovascular Division, British Heart Foundation Centre, King's College London, 125 Coldharbour Lane, London SE5 9NU, UKReactive 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.http://dx.doi.org/10.1100/2011/289182 |
| spellingShingle | Beatriz S. Stolf Ioannis Smyrnias Lucia R. Lopes Alcione Vendramin Hiro Goto Francisco R. M. Laurindo Ajay M. Shah Celio X. C. Santos Protein Disulfide Isomerase and Host-Pathogen Interaction The Scientific World Journal |
| 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 |
| url | http://dx.doi.org/10.1100/2011/289182 |
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