8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus.
Respiratory syncytial virus (RSV), along with other prominent respiratory RNA viruses such as influenza and SARS-CoV-2, significantly contributes to the global incidence of respiratory tract infections. These pathogens induce the production of reactive oxygen species (ROS), which play a crucial role...
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| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2024-10-01
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| Series: | PLoS Pathogens |
| Online Access: | https://doi.org/10.1371/journal.ppat.1012616 |
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| author | Lang Pan Ke Wang Wenjing Hao Yaoyao Xue Xu Zheng Ritwika S Basu Tapas K Hazra Azharul Islam Yashoda Hosakote Bing Tian Matthieu G Gagnon Xueqing Ba Istvan Boldogh |
| author_facet | Lang Pan Ke Wang Wenjing Hao Yaoyao Xue Xu Zheng Ritwika S Basu Tapas K Hazra Azharul Islam Yashoda Hosakote Bing Tian Matthieu G Gagnon Xueqing Ba Istvan Boldogh |
| author_sort | Lang Pan |
| collection | DOAJ |
| description | Respiratory syncytial virus (RSV), along with other prominent respiratory RNA viruses such as influenza and SARS-CoV-2, significantly contributes to the global incidence of respiratory tract infections. These pathogens induce the production of reactive oxygen species (ROS), which play a crucial role in the onset and progression of respiratory diseases. However, the mechanisms by which viral RNA manages ROS-induced base oxidation remain poorly understood. Here, we reveal that 8-oxo-7,8-dihydroguanine (8-oxoGua) is not merely an incidental byproduct of ROS activity but serves as a strategic adaptation of RSV RNA to maintain genetic fidelity by hijacking the 8-oxoguanine DNA glycosylase 1 (OGG1). Through RNA immunoprecipitation and next-generation sequencing, we discovered that OGG1 binding sites are predominantly found in the RSV antigenome, especially within guanine-rich sequences. Further investigation revealed that viral ribonucleoprotein complexes specifically exploit OGG1. Importantly, inhibiting OGG1's ability to recognize 8-oxoGua significantly decreases RSV progeny production. Our results underscore the viral replication machinery's adaptation to oxidative challenges, suggesting that inhibiting OGG1's reading function could be a novel strategy for antiviral intervention. |
| format | Article |
| id | doaj-art-4fb7b110766a4feca2c22f32b1f19250 |
| institution | Kabale University |
| issn | 1553-7366 1553-7374 |
| language | English |
| publishDate | 2024-10-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj-art-4fb7b110766a4feca2c22f32b1f192502024-11-28T05:31:03ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742024-10-012010e101261610.1371/journal.ppat.10126168-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus.Lang PanKe WangWenjing HaoYaoyao XueXu ZhengRitwika S BasuTapas K HazraAzharul IslamYashoda HosakoteBing TianMatthieu G GagnonXueqing BaIstvan BoldoghRespiratory syncytial virus (RSV), along with other prominent respiratory RNA viruses such as influenza and SARS-CoV-2, significantly contributes to the global incidence of respiratory tract infections. These pathogens induce the production of reactive oxygen species (ROS), which play a crucial role in the onset and progression of respiratory diseases. However, the mechanisms by which viral RNA manages ROS-induced base oxidation remain poorly understood. Here, we reveal that 8-oxo-7,8-dihydroguanine (8-oxoGua) is not merely an incidental byproduct of ROS activity but serves as a strategic adaptation of RSV RNA to maintain genetic fidelity by hijacking the 8-oxoguanine DNA glycosylase 1 (OGG1). Through RNA immunoprecipitation and next-generation sequencing, we discovered that OGG1 binding sites are predominantly found in the RSV antigenome, especially within guanine-rich sequences. Further investigation revealed that viral ribonucleoprotein complexes specifically exploit OGG1. Importantly, inhibiting OGG1's ability to recognize 8-oxoGua significantly decreases RSV progeny production. Our results underscore the viral replication machinery's adaptation to oxidative challenges, suggesting that inhibiting OGG1's reading function could be a novel strategy for antiviral intervention.https://doi.org/10.1371/journal.ppat.1012616 |
| spellingShingle | Lang Pan Ke Wang Wenjing Hao Yaoyao Xue Xu Zheng Ritwika S Basu Tapas K Hazra Azharul Islam Yashoda Hosakote Bing Tian Matthieu G Gagnon Xueqing Ba Istvan Boldogh 8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus. PLoS Pathogens |
| title | 8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus. |
| title_full | 8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus. |
| title_fullStr | 8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus. |
| title_full_unstemmed | 8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus. |
| title_short | 8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus. |
| title_sort | 8 oxoguanine dna glycosylase1 conceals oxidized guanine in nucleoprotein associated rna of respiratory syncytial virus |
| url | https://doi.org/10.1371/journal.ppat.1012616 |
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