Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response.
All poxviruses contain a set of proteinaceous structures termed lateral bodies (LB) that deliver viral effector proteins into the host cytosol during virus entry. To date, the spatial proteotype of LBs remains unknown. Using the prototypic poxvirus, vaccinia virus (VACV), we employed a quantitative...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2022-07-01
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| Series: | PLoS Pathogens |
| Online Access: | https://doi.org/10.1371/journal.ppat.1010614 |
| _version_ | 1818192701847240704 |
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| author | Susanna R Bidgood Jerzy Samolej Karel Novy Abigail Collopy David Albrecht Melanie Krause Jemima J Burden Bernd Wollscheid Jason Mercer |
| author_facet | Susanna R Bidgood Jerzy Samolej Karel Novy Abigail Collopy David Albrecht Melanie Krause Jemima J Burden Bernd Wollscheid Jason Mercer |
| author_sort | Susanna R Bidgood |
| collection | DOAJ |
| description | All poxviruses contain a set of proteinaceous structures termed lateral bodies (LB) that deliver viral effector proteins into the host cytosol during virus entry. To date, the spatial proteotype of LBs remains unknown. Using the prototypic poxvirus, vaccinia virus (VACV), we employed a quantitative comparative mass spectrometry strategy to determine the poxvirus LB proteome. We identified a large population of candidate cellular proteins, the majority being mitochondrial, and 15 candidate viral LB proteins. Strikingly, one-third of these are VACV redox proteins whose LB residency could be confirmed using super-resolution microscopy. We show that VACV infection exerts an anti-oxidative effect on host cells and that artificial induction of oxidative stress impacts early and late gene expression as well as virion production. Using targeted repression and/or deletion viruses we found that deletion of individual LB-redox proteins was insufficient for host redox modulation suggesting there may be functional redundancy. In addition to defining the spatial proteotype of VACV LBs, these findings implicate poxvirus redox proteins as potential modulators of host oxidative anti-viral responses and provide a solid starting point for future investigations into the role of LB resident proteins in host immunomodulation. |
| first_indexed | 2024-12-12T00:34:42Z |
| format | Article |
| id | doaj.art-d3a0110eda7146bcbc882c71dcde7494 |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-12T00:34:42Z |
| publishDate | 2022-07-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-d3a0110eda7146bcbc882c71dcde74942022-12-22T00:44:24ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742022-07-01187e101061410.1371/journal.ppat.1010614Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response.Susanna R BidgoodJerzy SamolejKarel NovyAbigail CollopyDavid AlbrechtMelanie KrauseJemima J BurdenBernd WollscheidJason MercerAll poxviruses contain a set of proteinaceous structures termed lateral bodies (LB) that deliver viral effector proteins into the host cytosol during virus entry. To date, the spatial proteotype of LBs remains unknown. Using the prototypic poxvirus, vaccinia virus (VACV), we employed a quantitative comparative mass spectrometry strategy to determine the poxvirus LB proteome. We identified a large population of candidate cellular proteins, the majority being mitochondrial, and 15 candidate viral LB proteins. Strikingly, one-third of these are VACV redox proteins whose LB residency could be confirmed using super-resolution microscopy. We show that VACV infection exerts an anti-oxidative effect on host cells and that artificial induction of oxidative stress impacts early and late gene expression as well as virion production. Using targeted repression and/or deletion viruses we found that deletion of individual LB-redox proteins was insufficient for host redox modulation suggesting there may be functional redundancy. In addition to defining the spatial proteotype of VACV LBs, these findings implicate poxvirus redox proteins as potential modulators of host oxidative anti-viral responses and provide a solid starting point for future investigations into the role of LB resident proteins in host immunomodulation.https://doi.org/10.1371/journal.ppat.1010614 |
| spellingShingle | Susanna R Bidgood Jerzy Samolej Karel Novy Abigail Collopy David Albrecht Melanie Krause Jemima J Burden Bernd Wollscheid Jason Mercer Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response. PLoS Pathogens |
| title | Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response. |
| title_full | Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response. |
| title_fullStr | Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response. |
| title_full_unstemmed | Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response. |
| title_short | Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response. |
| title_sort | poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative response |
| url | https://doi.org/10.1371/journal.ppat.1010614 |
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