VirologyPub Date : 2025-02-21DOI: 10.1016/j.virol.2025.110460
Rio Harada , Takahiro Hiono , Manabu Igarashi , Daiki Kobayashi , Hinako Ban , Norikazu Isoda , Yoshihiro Sakoda
{"title":"Altered receptor-binding specificity of gull-adapted H13 avian influenza viruses corresponds to their unique host preferences","authors":"Rio Harada , Takahiro Hiono , Manabu Igarashi , Daiki Kobayashi , Hinako Ban , Norikazu Isoda , Yoshihiro Sakoda","doi":"10.1016/j.virol.2025.110460","DOIUrl":"10.1016/j.virol.2025.110460","url":null,"abstract":"<div><div>Avian influenza viruses (AIVs) recognize α2-3 sialosides as receptors. Previous studies showed that the structural diversity within α2-3 sialosides is related to the host specificity of AIVs. H13 AIVs are primarily isolated from gulls, although almost all AIV subtypes have been isolated from ducks, the natural hosts of AIVs. To elucidate the molecular basis of the host specificity of H13 viruses to gulls, the receptor-binding specificity of H13 hemagglutinins (HAs) and the distribution of viral receptors in gulls were investigated. The results revealed that recombinant HA (rHA) of H13 viruses had a binding preference for fucosylated α2-3 sialosides, which were distributed widely in the respiratory tract and intestines of gulls but not in the colon of ducks. Moreover, the receptor-binding specificity of mutant rHAs revealed that amino acids in the 130-loop and at position 227 of H13 HA were critical for the preference for fucosylated α2-3 sialosides. The results of the present study suggest that the binding specificity of H13 HA to fucosylated α2-3 sialosides is a key factor for the host susceptibility of H13 viruses to gulls.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"605 ","pages":"Article 110460"},"PeriodicalIF":2.8,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143474925","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-21DOI: 10.1016/j.virol.2025.110458
James Lok , James M. Harris , Ivana Carey , Kosh Agarwal , Jane A. McKeating
{"title":"Assessing the virological response to direct-acting antiviral therapies in the HBV cure programme","authors":"James Lok , James M. Harris , Ivana Carey , Kosh Agarwal , Jane A. McKeating","doi":"10.1016/j.virol.2025.110458","DOIUrl":"10.1016/j.virol.2025.110458","url":null,"abstract":"<div><div>Hepatitis B virus (HBV) is a global health problem with over 250 million people affected worldwide. Nucleos(t)ide analogues remain the standard of care and suppress production of progeny virions; however, they have limited effect on the viral transcriptome and long-term treatment is associated with off-target toxicities. Promising results are emerging from clinical trials and several drug classes have been evaluated, including capsid assembly modulators and RNA interfering agents. Whilst peripheral biomarkers are used to monitor responses and define treatment endpoints, they fail to reflect the full reservoir of infected hepatocytes. Given these limitations, consideration should be given to the merits of sampling liver tissue, especially in the context of clinical trials. In this review article, we will discuss methods for profiling HBV in liver tissue and their value to the HBV cure programme.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"605 ","pages":"Article 110458"},"PeriodicalIF":2.8,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143519819","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-20DOI: 10.1016/j.virol.2025.110457
Yuejia Qiu , Ming Qiu , Shubin Li , Shubo Li , Jianzhong Zhu , Kegong Tian , Nanhua Chen
{"title":"Emergence, prevalence and evolution of porcine reproductive and respiratory syndrome virus 1 in China from 1994 to 2024","authors":"Yuejia Qiu , Ming Qiu , Shubin Li , Shubo Li , Jianzhong Zhu , Kegong Tian , Nanhua Chen","doi":"10.1016/j.virol.2025.110457","DOIUrl":"10.1016/j.virol.2025.110457","url":null,"abstract":"<div><div>Porcine reproductive and respiratory syndrome virus 1 (PRRSV-1) was first detected in Chinese swine herds during an epidemiological investigation since 1994. Even though PRRSV-1 has been existed in China for 30 years, much less attention was paid on PRRSV-1 than PRRSV-2. This review systematically evaluated the emergence, prevalence and evolution of Chinese PRRSV-1 from 1994 to 2024. Here we showed that PRRSV-1 has been detected in at least 28 regions of China, which can be divided into eight subgroups within subtype 1. During the evolution in Chinese swine herds, a large number of substitutions, insertions and deletions were identified. Recombination events were also commonly detected accompanying with nsp1-nsp3, nsp9-nsp10 and ORF2-ORF6 regions as the cross-over hotspots. Remarkably, Chinese PRRSV-1 isolates showed a trend of increasing in pathogenicity in recent years. At last, we discussed the differential detection methods and cross-protection strategies against PRRSV-1 isolates. Overall, PRRSV-1 has become one of the widely-spread viruses in China posing a significant threat to China's swine industry.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"605 ","pages":"Article 110457"},"PeriodicalIF":2.8,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143474924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-20DOI: 10.1016/j.virol.2025.110454
Sangita Venkataraman , Handanahal S. Savithri , M.R.N. Murthy
{"title":"Recent advances in the structure and assembly of non-enveloped spherical viruses","authors":"Sangita Venkataraman , Handanahal S. Savithri , M.R.N. Murthy","doi":"10.1016/j.virol.2025.110454","DOIUrl":"10.1016/j.virol.2025.110454","url":null,"abstract":"<div><div>Non-enveloped spherical viruses (NSVs) are characterized by their highly symmetrical capsids that serve to protect and encapsulate the genomes. The stability and functionality of the capsids determine their ability for survival and proliferation in harsh environments. Over four decades of structural studies using X-ray crystallography and NMR have provided static, high-resolution snapshots of several viruses. Recently, advances in cryo-electron microscopy, together with AI-based structure predictions and traditional methods, have aided in elucidating not only the structural details of complex NSVs but also the mechanistic processes underlying their assembly. The knowledge thus generated has been instrumental in critical understanding of the conformational changes and interactions associated with the coat proteins, the genome, and the auxiliary factors that regulate the capsid dynamics. This review seeks to summarize current literature regarding the structure and assembly of the NSVs and discusses how the data has facilitated a deeper understanding of their biology and phylogeny.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"606 ","pages":"Article 110454"},"PeriodicalIF":2.8,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143610904","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-20DOI: 10.1016/j.virol.2025.110456
Marta Acchioni , Chiara Acchioni , John Hiscott , Marco Sgarbanti
{"title":"Origin and function of anti-interferon type I viral proteins","authors":"Marta Acchioni , Chiara Acchioni , John Hiscott , Marco Sgarbanti","doi":"10.1016/j.virol.2025.110456","DOIUrl":"10.1016/j.virol.2025.110456","url":null,"abstract":"<div><div>Type I interferons (IFN-I) are the most important innate immune cytokines produced by vertebrate host cells following, virus infection. Broadly speaking, detection of infecting viral nucleic acids by pattern recognition receptors (PRR) and subsequent downstream signaling triggers synthesis of a large number of IFN-I-stimulated genes (ISGs), endowed with diverse antiviral effector function. The co-evolution of virus-host interactions over million years has resulted in the emergence of viral strategies that target and inhibit host PRR-mediated detection, signal transduction pathways and IFN-I-mediated stimulation of ISGs. In this review, we illustrate the multiple mechanisms of viral immune evasion and discuss the co-evolution of anti-IFN-I viral proteins by summarizing key examples from recent literature. Due to the large number of anti-IFN-I proteins described, we provide here an evaluation of the prominent examples from different virus families. Understanding the unrelenting evolution of viral evasion strategies will provide mechanistic detail concerning these evolving interactions but will further enhance the development of tailored antiviral approaches.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"605 ","pages":"Article 110456"},"PeriodicalIF":2.8,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143479784","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-15DOI: 10.1016/j.virol.2025.110450
Abdelaal H.A. Shehata , Michael A. Mayfield , Edward J. Sikora , Kathleen M. Martin
{"title":"Characterization of soybean vein necrosis virus (SVNV) proteins: Sequence analysis of field strains and comparison of localization patterns in differing cell types","authors":"Abdelaal H.A. Shehata , Michael A. Mayfield , Edward J. Sikora , Kathleen M. Martin","doi":"10.1016/j.virol.2025.110450","DOIUrl":"10.1016/j.virol.2025.110450","url":null,"abstract":"<div><div>Soybean vein necrosis virus (SVNV) is a persistent, propagative, ambisense single-stranded RNA virus in the genus Orthotospovirus, transmitted by <em>Nehydatothrips variabilis</em>. To understand SVNV in the field, 33 samples exhibiting symptoms of SVNV were collected. The N, NSs, and NSm open reading frames (ORFs) were sequenced, revealing amino acid mutations in each gene. The five open reading frames of the SVNV Tennessee strain (N, NSs, NSm, GN, and GC) were fused in frame to GFP for experimentation in both plant and insect cells. N and NSs localize in plants at the cell periphery and nucleus. NSm induces cell death in plant cells, but not in insect cells, where cytoplasmic localization is observed. G<sub>N</sub> and G<sub>C</sub> glycoproteins localize to the membranes and display increased cytoplasmic localization in insect cells. The findings of this study contribute to understanding the genes of SVNV and capture sequence changes that have occurred over the past fifteen years.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"604 ","pages":"Article 110450"},"PeriodicalIF":2.8,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143445573","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-15DOI: 10.1016/j.virol.2025.110455
Syed M. Jamal , Salman Khan , Hanif Ur Rahman , Syed Asad Ali Shah , Noemi Polo , Ginette Wilsden , Krupali Parekh , Clare Browning , Jemma Wadsworth , Nick J. Knowles , Anna Ludi , Donald P. King , Michael Eschbaumer , Graham J. Belsham
{"title":"Emergence of new sublineages of serotype O foot-and-mouth disease viruses circulating in Pakistan during 2012–2021","authors":"Syed M. Jamal , Salman Khan , Hanif Ur Rahman , Syed Asad Ali Shah , Noemi Polo , Ginette Wilsden , Krupali Parekh , Clare Browning , Jemma Wadsworth , Nick J. Knowles , Anna Ludi , Donald P. King , Michael Eschbaumer , Graham J. Belsham","doi":"10.1016/j.virol.2025.110455","DOIUrl":"10.1016/j.virol.2025.110455","url":null,"abstract":"<div><div>Foot-and-mouth disease (FMD) is endemic in Pakistan and serotypes O, A and Asia-1 of FMD virus (FMDV) are responsible for the outbreaks in the country. The dominant serotype is type O represented by the O/ME-SA/PanAsia-2 lineage, which has diverged into different sublineages. Characterizing circulating viruses helps to trace the origin of outbreaks and provides evidence to select appropriate vaccines. The present study characterized viruses belonging to the O/ME-SA/PanAsia-2 lineage collected from bovines during 2012–2021. Phylogenetic analyses using the VP1 coding sequences revealed that these viruses grouped into five sublineages, of which two have been described previously, i.e. O/ME-SA/PanAsia-2<sup>BAL−09</sup> and O/ME-SA/PanAsia-2<sup>ANT−10</sup>, while the three new sublineages are designated here as O/ME-SA/PanAsia-2<sup>KHO−10</sup>, O/ME-SA/PanAsia-2<sup>ICT−12</sup> and O/ME-SA/PanAsia-2<sup>PUN−16</sup>. Antigenic profiling of selected viruses belonging to the PanAsia-2<sup>ICT−12</sup> and PanAsia-2<sup>PUN−16</sup> sublineages was carried out using antisera raised against three reference vaccine strains: O Manisa, O/TUR 5/2009 and O 3039. The data highlighted that some of the viruses, belonging to these sublineages, were not efficiently neutralized by the reference antisera. This may be due to the individual or combined effects of multiple amino acid changes in these field isolates at known antigenic sites. This study reveals that serotype O FMDVs are continuously evolving in Pakistan and that continuous surveillance to characterize viruses causing field outbreaks is important to identify the emergence of new FMDV sublineages that may be poorly controlled using existing FMD vaccines.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"605 ","pages":"Article 110455"},"PeriodicalIF":2.8,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143464305","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-15DOI: 10.1016/j.virol.2025.110452
Peijun Lin , Suling Liu , Zhi Cao , Yi Zeng , Yuechu Zhao , Ting Li , Chuangqiang Lin , Bing Gu , Bei Hu
{"title":"An experimental study on the lytic bacteriophage MSP15 with wide-spectrum targeting methicillin-resistant Staphylococcus aureus","authors":"Peijun Lin , Suling Liu , Zhi Cao , Yi Zeng , Yuechu Zhao , Ting Li , Chuangqiang Lin , Bing Gu , Bei Hu","doi":"10.1016/j.virol.2025.110452","DOIUrl":"10.1016/j.virol.2025.110452","url":null,"abstract":"<div><h3>Background</h3><div>Methicillin-resistant <em>Staphylococcus aureus</em> (MRSA) is identified as one of the main drug-resistant pathogens, increasing the risk of no antibiotic availability in clinical settings and necessitating the urgent search for alternative antibacterial treatments. Phage therapy has been proposed as a therapeutic approach for bacterial infections, offering numerous advantages and broad application prospects. However, the efficacy of phage therapy in treating drug-resistant infections in humans remains uncertain. Given the current advances in phage therapy and the grim situation posed by MRSA infections, the application of lytic bacteriophages with wide-spectrum activity to treat difficult MRSA infections is proposed.</div></div><div><h3>Objective</h3><div>The objective is to isolate, purify, and screen lytic bacteriophages targeting MRSA from the environment and to assess their efficacy and safety through in vitro and in vivo experiments, with the aim of providing another therapy for MRSA infection.</div></div><div><h3>Methods</h3><div>Firstly, representative MRSA strains were selected, and their corresponding phages were isolated and purified from hospital sewage. Secondly, the isolated phages were screened to identify lytic bacteriophages with broad-spectrum activity, and their biological characteristics were analyzed. Thirdly, a systemic infection mouse model was established to evaluate the efficacy and safety of phage MSP15 against MRSA infection.</div></div><div><h3>Results</h3><div>In this study, <em>Staphylococcus aureus</em> Phage MSP15, a lytic bacteriophage with broad-spectrum activity targeting MRSA, was successfully isolated, purified and screened. Furthermore, in the systemic infection mouse model, administration of phage MSP15 led to prolonged survival time of MRSA-infected mice. A 100% survival rate was observed in infected mice with both immediate and delayed administration of high doses of phage MSP15 (MOI = 1), although efficacy may potentially be reduced with delayed treatment compared to immediate treatment. Additionally, an immune response was induced by phage MSP15, resulting in the production of IgG against phage MSP15, while no adverse events such as changes in core body temperature, allergic reactions, or other adverse effects were observed in mice.</div></div><div><h3>Conclusion</h3><div>Lytic bacteriophages with a wide spectrum can become an auxiliary approach for treating MRSA infection.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"605 ","pages":"Article 110452"},"PeriodicalIF":2.8,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143464307","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-14DOI: 10.1016/j.virol.2025.110453
Wenwen Xiao , Zhuang Li , Chaoqun Chen , Yuting Shi , Puxian Fang , Shaobo Xiao , Liurong Fang
{"title":"Revisiting the roles of trypsin in the productive infection of porcine deltacoronavirus in porcine-derived cells","authors":"Wenwen Xiao , Zhuang Li , Chaoqun Chen , Yuting Shi , Puxian Fang , Shaobo Xiao , Liurong Fang","doi":"10.1016/j.virol.2025.110453","DOIUrl":"10.1016/j.virol.2025.110453","url":null,"abstract":"<div><div>Porcine deltacoronavirus (PDCoV) is an emerging enteric coronavirus with the potential for interspecies transmission. Trypsin has been shown to play a positive role in the isolation and multiplication of PDCoV in vitro, however, the functions of trypsin during PDCoV replication cycle remain controversial. In this study, we revisited the roles of trypsin for PDCoV infection by utilizing two kinds of PDCoV, PDCoV<sup>T+</sup> and PDCoV<sup>T−</sup>, which were prepared in the presence or absence of trypsin, respectively. We found that PDCoV<sup>T+</sup> was able to continuously proliferate in the medium containing trypsin, achieving a higher titer as the infection progress in LLC-PK1 and other tested porcine-derived cells. However, its replication was only transiently improved at 12 hours post-infection, and lower viral titers were observed under trypsin-free culture conditions. Furthermore, the trypsin-mediated enhancement of viral replication could be inhibited by trypsin inhibitor SBTI, suggesting that the second-round viral reproduction of PDCoV<sup>T</sup><sup>+</sup> might be impeded without trypsin. We further investigated the replication dynamics of PDCoV<sup>T−</sup> in LLC-PK1 cells in the presence or absence of trypsin. The results indicated that PDCoV<sup>T−</sup> generated lower viral titers under trypsin-free culture conditions, while the addition of trypsin reverted the infectivity of PDCoV<sup>T−</sup>. Additionally, we demonstrated that trypsin cleaved the PDCoV spike protein, activating viral attachment and internalization. Moreover, trypsin promoted viral replication and release, accelerating PDCoV maturation and facilitating second-round infection. Taken together, this study systematically revaluated and emphasized an essential role of trypsin in PDCoV infection, providing mechanistic insights into the productive infection of PDCoV in porcine-derived cells.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"604 ","pages":"Article 110453"},"PeriodicalIF":2.8,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143420298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
VirologyPub Date : 2025-02-12DOI: 10.1016/j.virol.2025.110451
Shasha Li , Linhao Wang , Yanqiao Wen , Jinyuan Han , Jixia Hou , Zhengyang Hou , Jingying Xie , Huixia Li , Xiangrong Li , Yanmei Yang , Ruofei Feng
{"title":"Porcine epidemic diarrhea virus nsp14 inhibited IFN-Ⅰ production by targeting RIG-I for degradation","authors":"Shasha Li , Linhao Wang , Yanqiao Wen , Jinyuan Han , Jixia Hou , Zhengyang Hou , Jingying Xie , Huixia Li , Xiangrong Li , Yanmei Yang , Ruofei Feng","doi":"10.1016/j.virol.2025.110451","DOIUrl":"10.1016/j.virol.2025.110451","url":null,"abstract":"<div><div>Porcine epidemic diarrhea virus (PEDV) is enteropathogenic coronavirus, and mainly damages intestines, causing diarrhea, vomiting, anorexia, and depression. PEDV highly pathogenic strains spread rapidly and pose significant economic and public health concerns in our country. After virus invasion, RIG-I detects viral double-stranded RNA to activate antiviral innate immunity, inducing IFN responses. PEDV genome encodes 16 non-structure proteins (nsp1-nsp16). These nsps have been effectively involved in the interaction of PEDV and host. PEDV nsp14 is a bi-functional enzyme that is responsible for proofreading and RNA cap G-N-7 methylation during viral infection. In this study, we confirmed that PEDV nsp14 was an interferon antagonist and inhibited IFN production induced by SeV and Poly(I:C). Further, we declared that PEDV infection decreased protein level of RIG-I, and the PEDV nsp14 played a part in this inhibitory effect. PEDV nsp14 induced cell apoptosis and then degraded RIG-I through caspase 8 and caspase 9 pathway during PEDV infection. The N7 MTase domain was critical for nsp14-mediated degradation of RIG-I. Our results revealed the novel function of PEDV nsp14 in virus-host interaction and provided a potential antiviral drug target.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"605 ","pages":"Article 110451"},"PeriodicalIF":2.8,"publicationDate":"2025-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143464306","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}