<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Pan L</submitter><funding>National Institute of Allergy and Infectious Diseases</funding><funding>NIAID NIH HHS</funding><funding>Crohn's &amp; Colitis Foundation</funding><funding>National Natural Science Foundation of China</funding><funding>National Postdoctoral Program for Innovative Talents</funding><funding>Welch Foundation</funding><pagination>e1012616</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11515973</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>20(10)</volume><pubmed_abstract>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 s</pubmed_abstract><journal>PLoS pathogens</journal><pubmed_title>8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus.</pubmed_title><pmcid>PMC11515973</pmcid><funding_grant_id>32170591 and 31970686</funding_grant_id><funding_grant_id>688953</funding_grant_id><funding_grant_id>H-2032-20230405</funding_grant_id><funding_grant_id>31900424</funding_grant_id><funding_grant_id>R21 AI176297</funding_grant_id><funding_grant_id>BX20200362</funding_grant_id><funding_grant_id>923759</funding_grant_id><funding_grant_id>AI062885</funding_grant_id><funding_grant_id>P01 AI062885</funding_grant_id><pubmed_authors>Zheng X</pubmed_authors><pubmed_authors>Hosakote Y</pubmed_authors><pubmed_authors>Tian B</pubmed_authors><pubmed_authors>Gagnon MG</pubmed_authors><pubmed_authors>Ba X</pubmed_authors><pubmed_authors>Hao W</pubmed_authors><pubmed_authors>Basu RS</pubmed_authors><pubmed_authors>Islam A</pubmed_authors><pubmed_authors>Boldogh I</pubmed_authors><pubmed_authors>Wang K</pubmed_authors><pubmed_authors>Xue Y</pubmed_authors><pubmed_authors>Hazra TK</pubmed_authors><pubmed_authors>Pan L</pubmed_authors></additional><is_claimable>false</is_claimable><name>8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus.</name><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 s</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Oct</publication><modification>2026-07-06T03:09:57.103Z</modification><creation>2025-04-06T14:23:03.264Z</creation></dates><accession>S-EPMC11515973</accession><cross_references><pubmed>39413143</pubmed><doi>10.1371/journal.ppat.1012616</doi></cross_references></HashMap>