Journal of General Virology最新文献

{"title":"Corrigendum: A single amino acid in coat protein of Pepper mild mottle virus determines its subcellular localization and the chlorosis symptom on leaves of pepper.","authors":"Kelei Han, Hongying Zheng, Mengfei Ji, Weijun Cui, Shuzhen Hu, Jiejun Peng, Jinping Zhao, Yuwen Lu, Lin Lin, Yong Liu, Jianping Chen, Fei Yan","doi":"10.1099/jgv.0.002272","DOIUrl":"10.1099/jgv.0.002272","url":null,"abstract":"","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 5","pages":""},"PeriodicalIF":4.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13171146/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147930354","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evolutionary and taxonomic insights into the genomic divergence of cowpea mild mottle virus: rapid evolution in replication-associated protein gene, but strong negative selection on coat protein gene.","authors":"Bruno Arcanjo Silva, João Marcos Fagundes Silva, Caterynne Melo Kauffmann, Stephanny Barreto Dos Santos Cárdenas, Paloma de Souza Queiroz, Amanda Moraes do Vale Batista, Helena Beatriz da Silva Mota, Rosana Blawid, Débora Maria Sansini Freitas, Alice Kazuko Inoue-Nagata, Tatsuya Nagata","doi":"10.1099/jgv.0.002262","DOIUrl":"10.1099/jgv.0.002262","url":null,"abstract":"<p><p><i>Carlavirus vignae</i>, with the common name cowpea mild mottle virus (CPMMV), has become a widespread carlavirus infecting economically important crops worldwide. CPMMV is transmitted by whiteflies, whereas other members of the <i>Carlavirus</i> genus are generally transmitted by aphids. Recently, the virus has been isolated from various host plants, including cucurbit plants in Brazil, exhibiting a wide genomic variation. Here, we present a comprehensive analysis of CPMMV genome diversity, focusing on the replication-associated protein (Rep) and coat protein (CP) genes, two key genomic regions for <i>Betaflexiviridae</i> classification. Cucurbit isolates of CPMMV from Brazil showed high divergent Rep but low CP aa sequences among them. Based on pairwise aa sequence identity of the Rep, the CPMMV available in public databases can be divided into at least four distinct genogroups. In contrast, CP sequences exhibited a remarkable sequence conservation across all analysed isolates, likely due to strong negative selection maintaining its functional or structural integrity. Furthermore, we concluded that the recombination is not the reason for the higher conservation of the CP relative to the Rep. These findings support the hypothesis that, in the family <i>Betaflexiviridae</i>, the Rep evolves at a more constant rate, whereas the CP evolves by 'leaps' of fast evolution. Since the differences in Rep aa sequence identities are well below the threshold defined by the <i>Betaflexiviridae</i> species demarcation criteria, we propose classifying the CPMMV isolates into four distinct species.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 5","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13218543/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148042718","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Virus taxonomy and the ICTV - 21 FAQs for the perplexed virologist.","authors":"Donald B Smith, Peter Simmonds, Stuart G Siddell","doi":"10.1099/jgv.0.002243","DOIUrl":"10.1099/jgv.0.002243","url":null,"abstract":"<p><p>Just over 125 years has passed since the 'filterable' agents of tobacco mosaic disease and foot-and-mouth disease were first described as infectious, replicating entities smaller than bacteria. Today, viruses are formally classified into more than 16,000 species ranked into genera, families and higher taxa. The development of an official virus taxonomy has been overseen by an International Committee, first constituted in 1966 and renamed as the International Committee on Taxonomy of Viruses (ICTV) in 1975. Despite the engagement of the ICTV in virus taxonomy over the last 60 years, many aspects of virus classification and nomenclature may seem odd or sometimes incomprehensible to virologists more familiar with the taxonomy of cellular organisms. Who runs the ICTV? What are virus species demarcation criteria? Why have all virus species names become binomial? How can a sequence in a metagenomic dataset be assigned to a virus species? This article attempts to answer several such questions and outlines how a large, inclusive and global community of virologists has developed new and responsive policies for virus taxonomy in a decade when the pace of virus discovery has dramatically accelerated.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 5","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13170759/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147930326","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The SL-I structural element of the 3' UTR region of West Nile virus participates in the regulation of viral translation.","authors":"Cristina Romero-López, Pilar Bueno-Arribas, Alfredo Berzal-Herranz","doi":"10.1099/jgv.0.002268","DOIUrl":"10.1099/jgv.0.002268","url":null,"abstract":"<p><p>The genome of West Nile virus (WNV) is a positive, ssRNA molecule, which encodes a single ORF flanked by UTRs (5' and 3' UTRs). These UTRs are enriched with structural RNA elements that play critical roles in the viral cycle, including translation, replication and encapsidation. The 3' UTR is crucial for translation control by the combined enhancer and repressor activities of different structural elements. This manuscript provides new roles for the 3' UTR SL-I element as a translation inhibitor in WNV in cis. This inhibitory effect is primarily observed in a cap-dependent translation context, most likely affecting multi-round translation efficiency. The molecular mechanism underlying this phenomenon appears to involve the recruitment of the 40S ribosomal subunit by the 3' UTR. We have previously demonstrated that the 3' UTR recruits the 40S subunit at two independent sites and influences its proper positioning at the 5' UTR. The present work identifies the SL-I element as a critical regulator of WNV translation at late stages of protein synthesis. This can be due, at least partially, to the modulation of the 40S positioning at the 3' UTR, as detected by selective 2'-hydroxyl acylation analysed by primer extension (SHAPE) analyses. These findings provide new insights into the role of the 3' UTR SL-I element in translation regulation and suggest that WNV translation is a finely tuned process dependent on the coordinated and well-balanced interplay of multiple partners.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 5","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13224872/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148042636","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The MNV-1 protease-polymerase precursor cleaves a novel site in the NS1-2 protein.","authors":"Vernon K Ward, Geena M McKenzie-Goldsmith, Matt J Edwards, Vivienne L Young, Torsten Kleffmann, Louise A Stubbing, Andrew Siow, Margaret A Brimble","doi":"10.1099/jgv.0.002263","DOIUrl":"10.1099/jgv.0.002263","url":null,"abstract":"<p><p>Human noroviruses (HuNVs) are members of the <i>Caliciviridae</i> family and are a significant cause of gastroenteritis worldwide. Cell culture models are challenging for studying the intracellular replication of HuNV, with murine norovirus (MNV) routinely used to study norovirus replication. Norovirus genomes contain a non-structural (NS) polyprotein that is processed by the viral protease, generating precursor and mature proteins during replication. We identified a putative viral protease cleavage site at E⁶⁶/G⁶⁷ in the MNV-1 NS1-2 protein by sequence analysis that was cleaved by the protease-polymerase (ProPol) precursor but not Pro <i>in vitro</i> and during MNV-1 replication, with the cleavage site confirmed by MS. The P4-P4' LHAE⁶⁶/G⁶⁷PLA cleavage site of MNV-1 is conserved in some MNV strains, while other strains contain a predicted caspase cleavage site (LHAD⁶⁶/G⁶⁷PHA) at this position, indicating that cleavage of NS1 is widely conserved in MNV. Mutation of the ProPol cleavage site in MNV-1 NS1-2 to the caspase motif reduced viral protein expression and replication in Huh7CD300lf and BV2 cells, while removal of the site via an E⁶⁶A mutation caused a 100-fold reduction in viral yield in the naturally permissive BV-2 cell line. This study demonstrates that the protease function of the MNV-1 ProPol precursor has an important role during replication that is distinct to the mature protease and that cleavage of NS1-2 by ProPol at E⁶⁶/G⁶⁷ is important for MNV-1 replication.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 4","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13135481/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147773376","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synergistic antiviral effect of host Adipose Triglyceride Lipase-directed DABPU-DE with coronavirus RNA-dependent RNA polymerase-targeting remdesivir on feline infectious peritonitis virus.","authors":"Shaimaa Aboelmagd, Seok In Han, Ragab Farouk, Dae-Eun Cheong, Hae-Rang Seo, Dong Ju Lee, Sunwoo Lee, Kyoung-Oh Cho","doi":"10.1099/jgv.0.002261","DOIUrl":"10.1099/jgv.0.002261","url":null,"abstract":"<p><p>Feline infectious peritonitis virus (FIPV) poses a significant threat to cats worldwide. Besides the limited development of antiviral drugs that mainly target virus proteins, concerns about resistance to mutant strains - similar to those seen in human and other mammalian viruses - remain high. Therefore, addressing these challenges involves developing innovative antiviral therapies, such as host-directed treatments that target host cell processes essential for viral replication. FIPV infection induced distinctive dynamics of lipid droplet (LD) remodelling, characterized by an increase in LD abundance from early to mid-infection, followed by a subsequent decline. Phosphorylated hormone-sensitive lipase, a key mediator of LD hydrolysis and fatty-acid release, became activated after the mid-infection phase, potentially contributing to elevated intracellular fatty-acid availability during late infection. Notably, atglistatin (DABPU-DM) and its derivatives robustly suppressed FIPV replication in Crandell-Rees feline kidney (CRFK) and feline macrophage Fcwf-4 cells, coincident with preservation of LD integrity and inhibition of LD breakdown. Among these compounds, DABPU-DE had the best selectivity index (686.0±35.2) against FIPV, with a higher half-maximal cytotoxic concentration (274.4±3.6 µM) and a lower half-maximal inhibitory concentration (0.4±0.02 µM). Moreover, combining DABPU-DE (0.18 µM) with remdesivir (1.35 µM), a viral RNA-dependent RNA polymerase inhibitor, showed a very strong synergistic effect (CI=0.09 and Bliss synergy score=14.46±1.80) in inhibiting FIPV replication in CRFK cells, even at lower doses than either drug alone. In conclusion, DABPU-DE is a promising antiviral candidate for FIPV, and its synergistic effect with remdesivir warrants further research in cats infected with FIPV.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 4","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147773442","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Broadly neutralizing monoclonal antibodies derived from mRNA LNP immunization exhibit potent neutralizing ability against JN.1, KP.3.1.1 and XEC new Omicron variants.","authors":"Hsiao-Ling Chiang, Hsiu-Ting Lin, Wan-Yu Chen, Kang-Hao Liang, Ruei-Min Lu, Han-Chung Wu","doi":"10.1099/jgv.0.002251","DOIUrl":"10.1099/jgv.0.002251","url":null,"abstract":"<p><p>Since the emergence of severe acute respiratory syndrome coronavirus 2 Omicron, dramatic changes in the receptor-binding domain have allowed for virus escape from many therapeutic antibodies. Development of antibodies effective against current viral strains is, therefore, necessary to provide useful clinical treatments and can also yield fundamental information about viral neutralization. Here, we utilized single B-cell antibody technology to isolate and characterize neutralizing antibodies from splenocytes of mice immunized with mRNA-LNPs. With this approach, we identified five BA.5 and four XBB.1.5 neutralizing chimeric antibodies (ChAbs). The identified ChAbs, BA.5-ChAb-41, XBB.1.5-ChAb-17 and XBB.1.5-ChAb-26, each potently neutralized BA.5, XBB.1.5 and JN.1 pseudotype viruses with low IC₅₀ (1.9, 2.3 and 10.93 ng ml^-1). Furthermore, XBB.1.5-ChAb-26 showed neutralizing capability against the current JN.1-related variants, KP.3.1.1 and XEC. By performing single amino acid substitution of the receptor-binding motif (RBM), we observed that the epitopes of BA.5-ChAb-41 and XBB.1.5-ChAb-17 include Y453 and R498 in the RBM. Moreover, XBB.1.5-ChAb-26 epitope includes Y453 and T500, which may contribute to its ability to neutralize JN.1, KP.3.1.1 and XEC variants. In summary, our approach allowed us to efficiently screen for highly functional antibodies, and we further identified critical residues in the epitopes to aid in the design of therapeutic virus-neutralizing antibodies.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 4","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13131021/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147773361","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ICTV Virus Taxonomy Profile: <i>Krittikaviridae</i> 2026.","authors":"Apoorva Prabhu, Christian Rinke","doi":"10.1099/jgv.0.002239","DOIUrl":"10.1099/jgv.0.002239","url":null,"abstract":"<p><p>The family <i>Krittikaviridae</i> includes dsDNA viruses associated with the marine archaeal lineage <i>Poseidoniales</i>. These viruses have been identified through metagenomic analysis of brackish estuarine samples and are closely related to other 'magroviruses'. The family belongs to the order <i>Magrovirales</i> and includes the genus <i>Velanvirus</i> and the species <i>Velanvirus brisbanense</i>. Viruses in the family have a genome of about 80 kbp that includes modules for DNA replication and virion morphogenesis. Krittikavirids are predicted to form virions with an icosahedral capsid and helical tail, characteristic of viruses belonging to the class <i>Caudoviricetes</i>. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on the family <i>Krittikaviridae</i>, which is available at ictv.global/report/krittikaviridae.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 4","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147638907","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Co-release of tick-borne encephalitis virus RNA and structural proteins via virus-like particles and extracellular vesicles.","authors":"Ivana Křížová, Anna Klimešová, Alžběta Dostálková, Jana Racková, Jiřina Kaufmanová, Radim Novotný, Matěj Danda, Ivana Matošević, Zdeněk Franta, Hana Tykalová, Libor Grubhoffer, Michaela Rumlová","doi":"10.1099/jgv.0.002258","DOIUrl":"10.1099/jgv.0.002258","url":null,"abstract":"<p><p>Tick-borne encephalitis virus (TBEV) is a medically important flavivirus that causes severe neurological diseases in humans. The assembly of flaviviruses is initiated by the interaction between capsid (C) proteins and viral genomic RNA, yet the molecular determinants that govern RNA encapsidation remain unclear. In this study, we established a TBEV virus-like particle (VLP) system to analyse viral factors that influence viral RNA incorporation independently of productive infection. Using a reporter-containing TBEV minigenome, we investigated the contribution of UTRs to the incorporation of RNA into extracellular particles. Truncation of the 5' UTR, 3' UTR or both did not significantly affect the levels of minigenome RNA detected in pelleted extracellular fractions, indicating that RNA incorporation occurs largely in a non-specific manner. We further examined the role of C protein dimerization by introducing alanine substitutions into residues that form the α2-α2' and α4-α4' dimer interfaces. Paradoxically, these substitutions increased the levels of minigenome RNA detected in pelleted extracellular particles without altering intracellular RNA expression, indicating a complex relationship between the integrity of the C protein dimer interface and levels of extracellular viral RNA. Finally, we showed that TBEV proteins and minigenome RNA can be detected in extracellular vesicle (EV)-associated fractions under VLP-producing conditions. Using immunoaffinity purification, we demonstrate the presence of viral components in EVs, underscoring EV-associated release as a factor that complicates the analysis of flaviviral particle assembly.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 4","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13135480/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147773446","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural insights into the nuclear import of ovine gammaherpesvirus 2 ORF73 LANA homologue.","authors":"Babu Kanti Nath, Renate H M Schwab, Crystall M D Swarbrick, Silvia Pavan, Nazia Rahman, Brian P McSharry, Shane R Raidal, Daryl Ariawan, Ole Tietz, Shubhagata Das, Gualtiero Alvisi, Jade K Forwood","doi":"10.1099/jgv.0.002250","DOIUrl":"10.1099/jgv.0.002250","url":null,"abstract":"<p><p>Ovine gammaherpesviruses 2 (OvGHV2), a member of the <i>Macavirus</i> genus within the <i>Orthoherpesviridae</i> family, causes lymphoproliferative diseases in susceptible species, most notably sheep-associated malignant catarrhal fever. Research on OvGHV2 has been hindered by the absence of a permissive cell culture system, limiting investigations into viral replication, entry mechanisms and cell tropism. This challenge constrains progress towards understanding OvGHV2 pathogenesis and developing effective vaccines or therapeutics. We investigated the molecular mechanisms underlying OvGHV2 infection, focusing on the nuclear trafficking pathways of the latency-associated nuclear antigen (LANA), encoded by ORF73. In other gammaherpesviruses, LANA is known to mediate viral episome maintenance, chromatin tethering and latency through its nuclear localization. We identified and functionally characterized a novel bipartite nuclear localization signal (NLS) within the C-terminal region of OvGHV2 LANA and elucidated its interactions with host nuclear import receptors. Using high-resolution crystallography and quantitative binding assays, we mapped the key residues responsible for binding to importin alpha (IMP<i>α</i>) and demonstrated isoform-specific variations in binding affinity. Confocal microscopy revealed that the OvGHV2 LANA predominantly localizes to the nucleus through an IMP<i>α</i>/<i>β</i>1-dependent pathway, as mutation or inhibition of the NLS significantly reduced nuclear accumulation. Interestingly, partial nuclear localization under these conditions suggests an additional IMP<i>α</i>/<i>β</i>1-independent nuclear import mechanism. Collectively, our biochemical and structural analyses confirm that the identified NLS is essential for IMP<i>α</i>-mediated nuclear import of OvGHV2 LANA. These findings provide new insights into OvGHV2 host interactions and establish a molecular basis for developing targeted antiviral strategies against ovine gammaherpesvirus 2 infection.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"107 4","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13089313/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147716955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}