Journal of General Virology最新文献

{"title":"Distribution of aminopeptidase N coronavirus receptors in the respiratory and digestive tracts of domestic and wild artiodactyls and carnivores.","authors":"Fabian Z X Lean, Giulia Gallo, Joseph Newman, Stuart Ackroyd, Simon Spiro, Ruth Cox, Ingebjørg Helena Nymo, Caroline Bröjer, Aleksija Neimanis, Alejandro Suárez-Bonnet, Simon L Priestnall, Holly Everest, Sarah Keep, Dalan Bailey, Richard J Delahay, Amanda H Seekings, Lorraine M McElhinney, Sharon M Brookes, Alejandro Núñez","doi":"10.1099/jgv.0.002092","DOIUrl":"10.1099/jgv.0.002092","url":null,"abstract":"<p><p>Aminopeptidase N (APN) is a transmembrane protein that mediates the attachment of the spike protein of several clinically important coronaviruses (CoVs) responsible for respiratory and intestinal diseases in animals and humans. To assess the potential for APN-mediated viral tropism, we characterized APN receptor distribution in the respiratory and intestinal tissues of various artiodactyls (cervids, bovids, camelids and suids) and carnivores (canids, felids, mustelids and phocids) using immunohistochemistry. In the lungs, APN expression was limited to artiodactyls, with strong expression in the bronchiolar epithelium and weaker expression in pneumocytes. Nasal turbinate and tracheal samples, where available, showed stronger APN expression in artiodactyls over carnivores. APN was consistently detected on the microvilli of enterocytes in the small intestine across multiple taxa, while the presence in the colon was more variable. Of the animals examined, pig and alpaca consistently expressed the most abundant APN in the upper and lower respiratory tract. <i>In silico</i> evaluation of APN orthologue sequences from humans, artiodactyls and carnivores identified distinct evolutionary relationships. Further <i>in silico</i> binding predictions for alpaca alphacoronavirus and human coronavirus 229E with cognate and heterologous alpaca and human APN revealed substantial overlapping binding footprints with high conservation of amino acid residues, suggesting an evolutionary divergence and subsequent adaptation of a 229E-like or ancestral virus within a non-human animal host. This combined anatomical and <i>in silico</i> approach enhances understanding of host susceptibility, tissue tropism and viral transmission mechanisms in APN-dependent CoVs and has the potential to inform future strategies for disease modelling, surveillance and control.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 4","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11971486/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143779923","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":"Myosin IXB protects immune cells from virus infection.","authors":"Leticia Kogachi, Taís Matozo, Yuli Thamires Magalhães, Marina Janoni Bayerlein, Tania Carolina Braga, Felippe E C Camargo, Kamilla B da S Souza, Fábio Luis Forti, Bruna Cunha de Alencar","doi":"10.1099/jgv.0.002090","DOIUrl":"10.1099/jgv.0.002090","url":null,"abstract":"<p><p>Actin-associated proteins have been implicated in several stages of virus infection. However, the role of myosins, which are actin-dependent molecular motors, during virus infection and pathogenesis is poorly understood. Myosin IXB (Myo9b) is a member of the myosin family abundantly expressed in immune cells. Myo9b displays a RhoGTPase-activating protein domain capable of modulating actin dynamics by inhibiting RhoGTPase activity. To enquire upon Myo9b participation in virus infections, we have silenced Myo9b in U937 and Jurkat cells and infected them with vesicular stomatitis virus glycoprotein (VSV-G)-pseudotyped HIV-1. Myo9b-silenced U937 showed a remarkable increase of above ten times more HIV-VSV-G infection than control cells. We observed a similar pattern in Jurkat cell infection with both WT Env and VSV-G-pseudotyped HIV, albeit to a lesser extent. Myo9b-silenced U937 cells presented elevated levels of phosphorylated cofilin, but lower levels of polymerized actin. The use of a RhoA, B and C inhibitor, as well as a Rac1 inhibitor, reduced virus infection. Finally, we have also observed an increment in virus internalization and fusion in cells knockdown for Myo9b, which may explain the increase in virus infection. Taken together, our data suggests that Myo9b might hinder viral entry and infection by controlling the activity of RhoGTPases in immune cells.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 4","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11962068/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143752329","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 loss of both pUL16 and pUL21 in HSV-1-infected cells alters capsid-tegument composition, nuclear membrane architecture, cytoplasmic maturation and cell-to-cell spread.","authors":"Kellen Roddy, Peter Grzesik, Barbara J Smith, Nathan Ko, Sanjay Vashee, Prashant J Desai","doi":"10.1099/jgv.0.002083","DOIUrl":"10.1099/jgv.0.002083","url":null,"abstract":"<p><p>Previously, we had developed synthetic genomics methods to assemble an infectious clone of herpes simplex virus type-1 (HSV-1) strain KOS. To do this, the genome was assembled from 11 separate cloned fragments in yeast using transformation-associated recombination. Using this method, we generated null mutations in five tegument protein-coding genes as well as different combinations of these mutants. The single-locus mutants were all able to plaque on Vero cells. However, one multi-locus combination, ∆UL16/UL21, proved lethal for virus replication in non-permissive cells. The proteins encoded by the genes UL16 and UL21 are of interest because they are known to physically interact and are constituents of the tegument structure. Furthermore, their roles in HSV-1-infected cells are unclear. Both are dispensable for HSV-1 replication; however, in HSV-2, their mutation results in nuclear retention of assembled capsids and has activities that impact nuclear membrane integrity as well as activities of proteins that function in nuclear egress. We thus characterized these HSV-1 viruses that carry the single and double mutants. What we found was that the single mutants could replicate within cells and spread from infected to uninfected cells, albeit at significantly reduced levels. However, the double mutant (∆16/21) could not produce infectious progeny in a 24 h growth cycle and could not spread from cell to cell. Confocal microscopy of VP16-Venus expressed by these viruses as well as immunofluorescence assays for glycoprotein B showed perturbation of the nuclear membrane, which was pronounced in ∆21 and ∆16/21 infected cells. All the mutants assembled DNA-filled capsids as judged by ultrastructural analyses and sedimentation studies. Electron microscopy revealed the presence of numerous mature viruses in WT-infected cells but fewer such particles in the ∆16- and ∆21-infected cells. What we discovered is that in cells where both pUL16 and pUL21 are absent, cytoplasmic capsids were evident, but mature enveloped particles were not detected. The capsid particles isolated from all the single- and multi-locus mutant-infected cells showed significantly lower levels of incorporation of both VP16 and pUL37 when compared to the WT capsids. This reduced incorporation may be related to the loss of the integrity of the architecture of the nuclear membrane. Interestingly, the incorporation of pUL16 was not affected by the absence of pUL21 and vice versa, as judged by immunoblots. These data now show that of the tegument proteins, like the essential pUL36, pUL37 and VP16, the complex of pUL16 and pUL21 should be considered as important mediators of maturation and cell-to-cell spread of the particle.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11912938/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143624895","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":"NEDD4-binding protein 1 suppresses hepatitis B virus replication by regulating viral RNAs.","authors":"Nobuhiro Kobayashi, Saori Suzuki, Yuki Sakamoto, Rigel Suzuki, Kento Mori, Yume Kosugi, Tomoya Saito, Yuan Ma, Lihan Liang, Takuma Izumi, Kisho Noda, Daisuke Okuzaki, Yumi Kanegae, Sanae Hayashi, Yasuhito Tanaka, Atsuya Yamashita, Kohji Moriishi, Yoshiharu Matsuura, Osamu Takeuchi, Tomokazu Tamura, Akinobu Taketomi, Takasuke Fukuhara","doi":"10.1099/jgv.0.002082","DOIUrl":"https://doi.org/10.1099/jgv.0.002082","url":null,"abstract":"<p><p>Chronic infection with hepatitis B virus (HBV) (chronic HBV infection) places patients at increased risk for liver cirrhosis and hepatocellular carcinoma. Although nucleos(t)ide analogues are mainly used for the treatment of HBV, they require long-term administration and may lead to the emergence of drug-resistant mutants. Therefore, to identify targets for the development of novel anti-HBV drugs, we screened for HBV-suppressive host factors using a plasmid expression library of RNA-binding proteins (RBPs). We tested the effect of 132 RBPs on HBV replication by ectopically expressing these proteins along with HBV in hepatocellular carcinoma and evaluated the intracellular capsid-associated HBV DNA level. Our screen identified NEDD4-binding protein 1 (N4BP1) as having an anti-HBV effect. In hepatocellular carcinoma cell lines transfected or infected with HBV, the overexpression of N4BP1 decreased core-associated HBV DNA levels, while knockdown or knockout of the gene encoding N4BP1 rescued core-associated HBV DNA levels. N4BP1 possesses the KH-like and RNase domains, and both were required for the anti-HBV effect of N4BP1. Additionally, we measured levels of HBV pregenomic RNA (pgRNA) and covalently closed circular DNA in the RBP-transfected cells and confirmed that N4BP1 binds pgRNA directly and regulates both the 3.5 and 2.4/2.1 kb HBV RNA. In summary, N4BP1 is a newly identified host factor able to counteract HBV production by regulating 3.5 and 2.1/2.4 kb HBV RNA.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143663559","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":"Cytoplasmic retention of dengue virus capsid protein by metformin impairing nuclear transport.","authors":"Ian Carlos Puello-Nakayama, Jonathan Hernandez-Castillo, Juan Manuel Castillo, Daniel Talamás-Lara, Selvin Noé Palacios-Rápalo, Rosa María Del Ángel","doi":"10.1099/jgv.0.002089","DOIUrl":"10.1099/jgv.0.002089","url":null,"abstract":"<p><p>Nuclear transport of proteins larger than 60 kDa occurs via energy-dependent active transport, whereas smaller proteins diffuse into the nucleus through nuclear pore complexes via passive nuclear transport. Although the dengue virus (DENV) replication cycle primarily takes place in the cytoplasm, the capsid protein and non-structural protein 5 (NS5) are imported into the nucleus through a nuclear localization sequence-dependent mechanism. However, given its small molecular weight (14 kDa), the DENV capsid protein may also enter the nucleus via passive diffusion. While some drugs primarily inhibit active nuclear transport, few are known to block passive diffusion. Notably, biguanides have been associated with inhibitory effects on passive nuclear transport. Since biguanides such as metformin (MET) exhibit anti-DENV properties, we investigated the effects of MET on the nuclear transport of DENV proteins. Our results suggest that MET induces changes in the nuclear membrane of Huh-7 cells and reduces capsid nuclear localization without affecting NS5 nuclear import. Furthermore, MET treatment did not alter capsid nuclear import in BHK-21 cells. Additionally, mimicking MET's effects using a non-hydrolyzable ATP analogue increased capsid cytoplasmic retention and decreased DENV-2 replication. Finally, the inhibition of the classical active nuclear transport pathway did not block capsid nuclear transport, suggesting that DENV-2 capsid enters the nucleus in Huh-7 and Vero cells independently of this pathway.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11926096/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143663558","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":"No evidence of subclinical infection in sheep surviving oral challenge with prions.","authors":"M Khalid F Salamat, Nora Hunter, E Fiona Houston","doi":"10.1099/jgv.0.002087","DOIUrl":"10.1099/jgv.0.002087","url":null,"abstract":"<p><p>Variant Creutzfeldt-Jakob disease (vCJD) is a fatal zoonotic disease caused by the ingestion of bovine spongiform encephalopathy (BSE)-infected meat products. Although the number of vCJD cases due to dietary exposure has significantly declined, the true burden of subclinical infections remains uncertain. Several large-scale surveys using appendix tissue samples have indicated the presence of abnormal prion protein (PrP^Sc; Sc for scrapie) in lymphoid tissue of a small proportion of the UK population. These may represent silent carriers of infection, with the potential to contribute to transmission, persistence and re-emergence of vCJD. Previously, we showed that subclinical infection is a frequent outcome of low-dose prion exposure by blood transfusion in sheep. To determine whether subclinical infection was also found following low-dose exposure by another clinically relevant route for humans, we screened archived tissues from sheep orally challenged with a range of doses of BSE, which did not show clinical or pathological signs of disease after several years of follow-up post-infection. Using a highly sensitive protein misfolding cyclic amplification assay, we were unable to detect PrP^Sc in the lymph node/tonsil of 15 sheep, or in a wider range of lymphoid tissues and brain (medulla oblongata) from a subset of 5 sheep. Our findings suggest that the route of infection/exposure may significantly influence the probability of establishing subclinical infection, with the oral route apparently much less efficient than intravenous infection by blood transfusion in sheep.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11928478/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143674064","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":"Dynamic regulation of autophagy during Semliki Forest virus infection of neuroblastoma cells.","authors":"Robert J Stott-Marshall, Craig McBeth, Thomas Wileman","doi":"10.1099/jgv.0.002086","DOIUrl":"10.1099/jgv.0.002086","url":null,"abstract":"<p><p>Autophagy can defend against infection by delivering viruses to lysosomes for degradation. Semliki Forest virus (SFV) is a positive-sense, single-stranded RNA virus of the alphavirus genus which has been used extensively as a model for arbovirus infection and neuronal encephalitis. Here, we show that autophagy is suppressed during the early hours of SFV infection of neurons. We also show that a switch between autophagy suppression and upregulation between the early and later stages was mediated through modulation of the mammalian target of rapamycin (mTOR) activity during infection. At later stages of infection, autophagosomes colocalize with SFV nonstructural proteins suggesting the formation of a platform for virus replication. Inhibition of mTOR by torin reduced infectious virus production and intracellular virus gene expression while improving cell survival during infection. The results suggest that autophagy is suppressed early during infection of neurons to increase cell survival and then upregulated at later times to facilitate replication. This biphasic regulation of autophagy seen for SFV may be important for other arboviruses, and knowledge about the regulation of autophagy by alphaviruses may be useful for the development of antiviral therapies.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11882037/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143557043","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":"Genetic characterization of rotavirus A strains circulating in children under 5 years of age with acute gastroenteritis in Tehran, Iran, in 2023-2024: dissemination of the emerging equine-like G3P[8]-I2-E2 DS-1-like strains.","authors":"Somayeh-Sadat Hosseini-Fakhr, Somayeh Jalilvand, Ali Maleki, Atefeh Kachooei, Farzane Behnezhad, Mahtab Mir-Hosseinian, Seiedehparnian Taghvaei, Sayed Mahdi Marashi, Zabihollah Shoja","doi":"10.1099/jgv.0.002088","DOIUrl":"10.1099/jgv.0.002088","url":null,"abstract":"<p><p>The present study was conducted to monitor the genotype diversity of circulating species A rotavirus (RVA) in Iran. A total of 300 faecal specimens were collected from children under 5 years of age hospitalized for acute gastroenteritis between October 2023 and October 2024. G3P[8] represented 72.91% (70/96) of all RVA-positive samples, further subdivided into equine-like G3P[8]-I2-E2 DS-1-like and human G3P[8]-I1-E1 Wa-like. A retrospective genetic analysis of G3P[8] strains isolated from 2015 to 2017 was also performed and showed that G3P[8] strains belong to the G3P[8]-E1-I1 Wa-like genetic pattern, which is typically similar to human G3P[8] Wa-like strains in this study. The emergence of equine-like G3P[8] DS-1-like strains in Iran may not be related to selection pressure from rotavirus vaccination, but rather to cross-border migration of rotavirus strains due to population movements.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11936345/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143657523","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 Cap-proximal secondary structures of the 5'UTRs of parainfluenza virus 5 mRNAs specify differential sensitivity to type I interferon and IFIT1.","authors":"Jacqueline Hankinson, Dan Young, Elizabeth B Wignall-Fleming, Radoslaw Lukoszek, Victoria H Cowling, Richard Randall, Steve Goodbourn","doi":"10.1099/jgv.0.002093","DOIUrl":"10.1099/jgv.0.002093","url":null,"abstract":"<p><p>Parainfluenza virus 5 (PIV5) is a paramyxovirus that has been isolated from numerous mammalian hosts and is notable for its ability to cause persistent infections. Although PIV5-infected cells are resistant to IFN due to the ability of the V protein to target STAT1 for degradation, PIV5 shows residual IFN sensitivity when infecting cells that have already been exposed to IFN. We have previously reported that the human IFN-stimulated gene with the greatest inhibitory effect on PIV5 is IFIT1. IFIT1 inhibits the translation of incompletely methylated mRNAs (Cap0) but not those 2'-O-methylated at the first transcribed nucleotide (Cap1). All <i>Mononegavirales</i> are thought to generate Cap1 mRNA, so the sensitivity of PIV5 to IFIT1 is surprising. Here, we show that PIV5 generates Cap0 mRNA but not Cap1 mRNA, thus explaining its sensitivity to IFIT1. Furthermore, the sensitivity of different PIV5 genes to IFIT1-mediated translation inhibition varies. In the absence of complete Cap methylation, we show that the presence or absence of 5'-terminal RNA hairpin structures in the 5'UTRs of PIV5 genes determines the extent to which they are sensitive to IFIT1. Notably, the genes involved in RNA synthesis are relatively resistant to IFIT1 inhibition. This presents a potential mechanism by which IFIT1 can regulate the outcome of PIV5 infection in response to IFN and may be important in allowing the virus to establish prolonged/persistent infections.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11950200/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143730325","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>Adnaviria</i> 2025.","authors":"Mart Krupovic, Fengbin Wang, Virginija Cvirkaite-Krupovic, Jens H Kuhn, Valerian V Dolja, David Prangishvili, Edward H Egelman, Eugene V Koonin","doi":"10.1099/jgv.0.002091","DOIUrl":"https://doi.org/10.1099/jgv.0.002091","url":null,"abstract":"<p><p>Viruses assigned to the realm <i>Adnaviria</i> have linear, dsDNA genomes in which the DNA is structured in the A-form rather than the usual B-form. Virions are flexible or rigid filaments, with or without envelopes. Adnavirians share homologous major capsid proteins (MCPs) with a distinct <i>α</i>-helical structural fold not observed in other known viruses. The MCPs form homodimeric or heterodimeric capsomers that wrap around and condense the genomic dsDNA into helically symmetrical virions. Adnavirians infect hyperthermophilic, thermoacidophilic and methanotrophic archaea. This is a summary of the International Committee on Taxonomy of Viruses Report on the realm <i>Adnaviria</i>, which is available at ictv.global/report/adnaviria.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 3","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143730323","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}