{"title":"病毒蛋白与游离氯的反应性:结构见解和病毒失活的意义。","authors":"Chonglin Zhu, and , Yinyin Ye*, ","doi":"10.1021/acs.est.5c01689","DOIUrl":null,"url":null,"abstract":"<p >Viruses exhibit diverse susceptibility to free chlorine inactivation, but the underlying mechanisms that drive these differences are poorly understood. To investigate this, we applied a multiplex and cost-effective tandem mass tag-based quantitative proteomics to characterize peptide decay kinetics and reactions in three model viruses, namely, MS2, PhiX174, and T4, when they were treated with free chlorine. Strong correlations were observed between peptide decay rate constants and both solvent-accessible surface areas (SASAs) of methionine residues (Pearson's <i>r</i> = 0.78, <i>p</i> < 0.0001) and SASAs per residue in methionine-lacking peptides (Pearson's <i>r</i> = 0.81, <i>p</i> < 0.0001). A multiple linear regression model fitted using these two independent structural variables accurately predicted peptide decay rate constants in the three viruses (<i>R</i><sup>2</sup> = 0.91 for MS2 peptides, <i>R</i><sup>2</sup> = 0.72 for PhiX174 peptides, and <i>R</i><sup>2</sup> = 0.86 for T4 peptides). Notably, the peptide decay kinetics in viral proteins responsible for host attachment and genome injection better predicted virus resistance than that in other viral proteins. Furthermore, peptides containing methionine sulfoxide, 3-chlorotyrosine, and nonspecific peptide bond cleavages were detected in chlorine-treated viruses. This study combines proteomics and structural analysis, providing new insights into protein reactivity and virus inactivation by free chlorine.</p>","PeriodicalId":36,"journal":{"name":"环境科学与技术","volume":"59 32","pages":"17188–17197"},"PeriodicalIF":11.3000,"publicationDate":"2025-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Reactivity of Viral Proteins with Free Chlorine: Structural Insights and Implications for Virus Inactivation\",\"authors\":\"Chonglin Zhu, and , Yinyin Ye*, \",\"doi\":\"10.1021/acs.est.5c01689\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >Viruses exhibit diverse susceptibility to free chlorine inactivation, but the underlying mechanisms that drive these differences are poorly understood. To investigate this, we applied a multiplex and cost-effective tandem mass tag-based quantitative proteomics to characterize peptide decay kinetics and reactions in three model viruses, namely, MS2, PhiX174, and T4, when they were treated with free chlorine. Strong correlations were observed between peptide decay rate constants and both solvent-accessible surface areas (SASAs) of methionine residues (Pearson's <i>r</i> = 0.78, <i>p</i> < 0.0001) and SASAs per residue in methionine-lacking peptides (Pearson's <i>r</i> = 0.81, <i>p</i> < 0.0001). A multiple linear regression model fitted using these two independent structural variables accurately predicted peptide decay rate constants in the three viruses (<i>R</i><sup>2</sup> = 0.91 for MS2 peptides, <i>R</i><sup>2</sup> = 0.72 for PhiX174 peptides, and <i>R</i><sup>2</sup> = 0.86 for T4 peptides). Notably, the peptide decay kinetics in viral proteins responsible for host attachment and genome injection better predicted virus resistance than that in other viral proteins. Furthermore, peptides containing methionine sulfoxide, 3-chlorotyrosine, and nonspecific peptide bond cleavages were detected in chlorine-treated viruses. This study combines proteomics and structural analysis, providing new insights into protein reactivity and virus inactivation by free chlorine.</p>\",\"PeriodicalId\":36,\"journal\":{\"name\":\"环境科学与技术\",\"volume\":\"59 32\",\"pages\":\"17188–17197\"},\"PeriodicalIF\":11.3000,\"publicationDate\":\"2025-07-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"环境科学与技术\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://pubs.acs.org/doi/10.1021/acs.est.5c01689\",\"RegionNum\":1,\"RegionCategory\":\"环境科学与生态学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"ENGINEERING, ENVIRONMENTAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"环境科学与技术","FirstCategoryId":"1","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acs.est.5c01689","RegionNum":1,"RegionCategory":"环境科学与生态学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"ENGINEERING, ENVIRONMENTAL","Score":null,"Total":0}
引用次数: 0
摘要
病毒对游离氯失活表现出不同的敏感性,但驱动这些差异的潜在机制尚不清楚。为了研究这一点,我们采用了一种多重且成本效益高的串联质量标签定量蛋白质组学方法来表征三种模型病毒(MS2、PhiX174和T4)在游离氯处理下的肽衰变动力学和反应。肽衰变速率常数与蛋氨酸残基的溶剂可及表面积(SASAs) (Pearson’s r = 0.78, p < 0.0001)和缺乏蛋氨酸肽残基的SASAs (Pearson’s r = 0.81, p < 0.0001)之间存在很强的相关性。利用这两个独立结构变量拟合的多元线性回归模型准确预测了三种病毒的肽衰减率常数(MS2肽R2 = 0.91, PhiX174肽R2 = 0.72, T4肽R2 = 0.86)。值得注意的是,与其他病毒蛋白相比,负责宿主附着和基因组注射的病毒蛋白中的肽衰变动力学更能预测病毒的抗性。此外,在氯处理的病毒中检测到含有蛋氨酸亚砜、3-氯酪氨酸和非特异性肽键裂解的肽。该研究结合了蛋白质组学和结构分析,为蛋白质反应性和游离氯灭活病毒提供了新的见解。
Reactivity of Viral Proteins with Free Chlorine: Structural Insights and Implications for Virus Inactivation
Viruses exhibit diverse susceptibility to free chlorine inactivation, but the underlying mechanisms that drive these differences are poorly understood. To investigate this, we applied a multiplex and cost-effective tandem mass tag-based quantitative proteomics to characterize peptide decay kinetics and reactions in three model viruses, namely, MS2, PhiX174, and T4, when they were treated with free chlorine. Strong correlations were observed between peptide decay rate constants and both solvent-accessible surface areas (SASAs) of methionine residues (Pearson's r = 0.78, p < 0.0001) and SASAs per residue in methionine-lacking peptides (Pearson's r = 0.81, p < 0.0001). A multiple linear regression model fitted using these two independent structural variables accurately predicted peptide decay rate constants in the three viruses (R2 = 0.91 for MS2 peptides, R2 = 0.72 for PhiX174 peptides, and R2 = 0.86 for T4 peptides). Notably, the peptide decay kinetics in viral proteins responsible for host attachment and genome injection better predicted virus resistance than that in other viral proteins. Furthermore, peptides containing methionine sulfoxide, 3-chlorotyrosine, and nonspecific peptide bond cleavages were detected in chlorine-treated viruses. This study combines proteomics and structural analysis, providing new insights into protein reactivity and virus inactivation by free chlorine.
期刊介绍:
Environmental Science & Technology (ES&T) is a co-sponsored academic and technical magazine by the Hubei Provincial Environmental Protection Bureau and the Hubei Provincial Academy of Environmental Sciences.
Environmental Science & Technology (ES&T) holds the status of Chinese core journals, scientific papers source journals of China, Chinese Science Citation Database source journals, and Chinese Academic Journal Comprehensive Evaluation Database source journals. This publication focuses on the academic field of environmental protection, featuring articles related to environmental protection and technical advancements.