Journal of General Virology最新文献

{"title":"<i>Wisteria floribunda</i> agglutinin enhances <i>Zaire ebolavirus</i> entry through interactions at specific <i>N</i>-linked glycosylation sites on the virus glycoprotein complex.","authors":"Joshua D Duncan, Monika Pathak, Barnabas J King, Holly Bamber, Paul Radford, Jayasree Dey, Charlotte Richardson, Stuart Astbury, Patrick McClure, Jonathan K Ball, Richard A Urbanowicz, Alexander W Tarr","doi":"10.1099/jgv.0.002120","DOIUrl":"10.1099/jgv.0.002120","url":null,"abstract":"<p><p>Entry of <i>Zaire</i> e<i>bolavirus</i> (EBOV) into a host cell is a complex process requiring interactions between the viral glycoproteins (GPs) and cellular factors. These entry factors are cell-specific and can include cell surface lectins and phosphatidylserine receptors. Niemann-Pick type C1 is critical to the late stage of the entry process. Entry has been demonstrated to be enhanced by interactions between the virion and surface-expressed lectins, which interact with carbohydrate moieties attached to the GP. In addition, soluble lectins, including mannose-binding lectin, can enhance entry <i>in vitro</i>. However, the mechanism of lectin-mediated enhancement remains to be defined. This study investigated the possibility that plant lectins, <i>Wisteria floribunda</i> agglutinin (WFA), soybean agglutinin (SBA) and <i>Galanthus nivalis</i> agglutinin (GNA), which possess different carbohydrate-binding specificities, influence EBOV entry. WFA was observed to potently enhance entry of lentiviral pseudotype viruses (PVs) expressing the GP of three <i>Ebolavirus</i> species [Zaire, Sudan (<i>Sudan ebolavirus</i>) and Reston (<i>Reston ebolavirus</i>)], with the greatest impact on EBOV. SBA had a modest enhancing effect on entry that was specific to EBOV, whilst GNA had no impact on the entry of any of the <i>Ebolavirus</i> species. None of the lectins enhanced the entry of control PVs expressing the surface proteins of other RNA viruses tested. WFA was demonstrated to bind directly with the EBOV-GP via the glycans, and mutational analysis implicated N²³⁸ as contributing to the interaction. Furthermore, enhancement was observed in both human and bat cell lines, indicating a highly conserved mechanism of action. We conclude that the binding of WFA to EBOV-GP through interactions including the glycan at N²³⁸ results in GP alterations that enhance entry, providing evidence of a mechanism for lectin-mediated virus entry enhancement. Targeting lectin-ligand interactions presents a potential strategy for restricting <i>Ebolavirus</i> entry.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 6","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12210185/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144234275","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":"Functional analysis of <i>BmTsp.C</i> in modulating infection of BmNPV through apoptosis pathways in domestic silkworm (<i>Bombyx mori</i>).","authors":"Yuanyuan Xu, Yimeng Wei, Jing Zhang, Dan Zhang, Qiaoling Zhao, Dongxu Shen","doi":"10.1099/jgv.0.002098","DOIUrl":"https://doi.org/10.1099/jgv.0.002098","url":null,"abstract":"<p><p>The silkworm, <i>Bombyx mori</i>, is a crucial model insect in agriculture and biological research. Tetraspanins, known for their effects in regulating cellular functions like cell signalling, adhesion, migration and diffusion, take on a crucial role in viral dynamics, influencing both viral spread and entry into host cells. In this study, a tetraspanin gene called <i>BmTsp.C</i> from the silkworm genome was identified and investigated. Tissue profiles showed that <i>BmTsp.C</i> has the highest transcription level in midgut, with a marked increase following viral infection. The immunofluorescence localization suggested that BmTsp.C is primarily distributed on the cell membrane. Additionally, overexpression of <i>BmTsp.C</i> in BmN cells facilitated the proliferation of BmNPV. Meanwhile, siRNA-mediated knockdown of <i>BmTsp.C</i> could inhibit viral proliferation. In addition, knockdown of <i>BmTsp</i>.C at the individual level further validated the remarkable effect of <i>BmTsp.C</i> during viral infestation. Furthermore, overexpression of <i>BmTsp.C</i> could regulate the expression of apoptosis-related genes. Results from flow cytometry indicated a decrease in the number of apoptotic cells after overexpression of <i>BmTsp.C</i>. Taken together, our results demonstrated that <i>BmTsp.C</i>, as an important factor in the Tetraspanin-enriched microdomains, exerts a significant influence on the proliferation of BmNPV, most likely through the cellular apoptosis pathway.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 5","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12064854/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143999782","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":"Development of a loop-mediated isothermal amplification assay for the rapid detection of Alongshan virus.","authors":"Wenlong Huang, Meiyi Chen, Yiwen Wang, Li Li, Tianmin Niu, Xin Guo, Jiaxuan Wang, Kaifeng He, Zhengkai Wei, Quan Liu","doi":"10.1099/jgv.0.002094","DOIUrl":"https://doi.org/10.1099/jgv.0.002094","url":null,"abstract":"<p><p>Alongshan virus (ALSV) is a recently discovered tick-borne zoonotic virus. Currently, there is no rapid and accurate clinical method for ALSV detection. This study aimed to develop a loop-mediated isothermal amplification (LAMP) assay for precise ALSV infection detection. Specific primers were designed based on the S1 segment of the ALSV NE-TH4 strain's genome (GenBank accession no. ON408067.1). The reaction time, temperature and concentration of the neutral red staining solution in the LAMP assay were optimized. Thorough evaluations of specificity, sensitivity and repeatability led to the development of a visually interpretable LAMP assay. The optimal amplification time was 50 min. The minimum detection limit for cDNA was as low as 0.005 pg μl^-1, and sensitivity for standards was 1.68×10³ copies per μl, surpassing that of PCR and real-time PCR. No cross-reactivity was observed with Jingmen tick virus, Bole tick virus 4 and Beiji nairovirus. These results indicate that the LAMP assay is more sensitive and accurate than PCR and real-time PCR. The developed LAMP assay allows for on-site detection, reduces testing costs and provides rapid and accurate results. Thus, it lays a solid foundation for the prevention and control of emerging tick-borne ALSV.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 5","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12062536/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144023211","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":"Novel endornaviruses infecting <i>Phytophthora cactorum</i> that attenuate vegetative growth, promote sporangia formation and confer hypervirulence to the host oomycete.","authors":"Kohei Sakuta, Aori Ito, Yukiko Sassa-O'Brien, Tomohiro Yoshida, Toshiyuki Fukuhara, Seiji Uematsu, Ken Komatsu, Hiromitsu Moriyama","doi":"10.1099/jgv.0.002099","DOIUrl":"https://doi.org/10.1099/jgv.0.002099","url":null,"abstract":"<p><p>Two novel endornaviruses were found in <i>Phytophthora cactorum</i> isolated from black lesions on <i>Boehmeria nivea</i> var. <i>nipononivea</i> plants in a Japanese forest. These two endornaviruses were named Phytophthora cactorum alphaendornavirus 4 (PcAEV4) and Phytophthora cactorum alphaendornavirus 5 (PcAEV5) and have site-specific nick structures in their positive RNA strands, which are hallmarks of alphaendornaviruses. Ribavirin and cycloheximide treatment of the protoplasts effectively cured the host oomycete (strain Kara1) of the viruses. The resultant virus-free strain (Kara1-C) displayed abundant mycelial growth with less zoosporangia formation as compared to the Kara1 strain. Remarkably, the Kara1-C strain exhibited a reduced ability to form black lesions on <i>B. nivea</i> leaves, suggesting that the presence of PcAEV4 and PcAEV5 in the Kara1 strain led to enhanced virulence in host plants. Under osmotic pressure and cell wall synthesis inhibition, the Kara1 strain exhibited less growth inhibition compared with the Kara1-C strain. In contrast, the Kara1 strain showed more growth inhibition in the presence of membrane-permeable surfactant compared with the Kara1-C strain, indicating that the two endornaviruses can alter the susceptibility of the host oomycete to abiotic stresses. Co-localization and cell fractionation analyses showed that PcAEV4 and PcAEV5 localized to intracellular membranes, particularly the endoplasmic reticulum membrane fraction. Furthermore, infection with these two endornaviruses was found to affect the host's response to exogenous sterols, which enhanced vegetative growth and zoosporangia formation, as well as virulence of the host oomycete. These results provide insights into the effects of endornavirus infection in <i>Phytophthora</i> spp. and also highlight the usefulness of protoplast-based methods in advancing <i>Phytophthora</i> virus studies.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 5","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12046096/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143988324","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 identification of a novel interaction site for the human immunodeficiency virus capsid on nucleoporin 153.","authors":"Shunji Li, Peik Lund-Andersen, Szu-Huan Wang, F Marty Ytreberg, Mandar T Naik, Jagdish Suresh Patel, Paul Andrew Rowley","doi":"10.1099/jgv.0.002104","DOIUrl":"10.1099/jgv.0.002104","url":null,"abstract":"<p><p>Human immunodeficiency virus type-1 (HIV-1) can infect non-dividing cells by passing through the selective permeability barrier of the nuclear pore complex. The viral capsid is essential for successfully delivering the HIV-1 genome into the nucleus. Nucleoporin 153 (NUP153) interacts with the HIV-1 capsid via a C-terminal capsid-binding motif (hereafter named CbM.1) to licence HIV-1 nuclear ingress. Deletion or mutation of CbM.1 in NUP153 causes a reduction in capsid interaction but does not prevent HIV-1 nuclear ingress or completely block capsid interaction. This paper combines molecular modelling with biochemical and HIV infection assays to identify capsid-binding motif 2 (CbM.2) in the C-terminus of NUP153 that is similar in sequence to CbM.1. CbM.2 has an FG dipeptide motif predicted to interact with a hydrophobic pocket in capsid protein (CA) hexamers similar to CbM.1. CA hexamers can interact with CbM.2, and the deletion of both CbM.1 and CbM.2 results in a lower capsid interaction than a single CbM.1 deletion. The loss of CbM.1 is complemented by CbM.2, an interaction dependent on the FG motif. In the context of the nuclear pore complex, a loss-of-function mutation in CbM.1 reduces HIV nuclear ingress as measured by transduction and 2-LTR circles, whereas the mutation of CbM.2 causes a large increase in 2-LTR circles. Our results highlighted a previously unidentified FG dipeptide-containing motif (CbM.2) in NUP153 that binds the HIV-1 capsid at the common hydrophobic pocket on CA hexamers.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 5","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12078792/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143999422","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":"An aegerolysin-like protein from Heliothis virescens ascovirus 3h (HvAV-3h) shows immune suppression and antibacterial activity.","authors":"Heba A H Zaghloul, Zhengkun Xiao, Jun Tang, Ting Xiao, Jiajun Gao, Jianjun Hu, Guo-Hua Huang","doi":"10.1099/jgv.0.002107","DOIUrl":"10.1099/jgv.0.002107","url":null,"abstract":"<p><p>Aegerolysins are lipid-binding proteins associated with multiple functions, including membrane pore-formation, insecticidal toxicity and defence against predators. Whilst distributed over the kingdoms of the Tree of Life, ascoviruses are the only representative viruses that encode an aegerolysin-like protein. Ascoviruses are entomopathogenic and possess a large dsDNA genome. The present study aimed to functionally characterize the aegerolysin-like protein of Heliothis virescens ascovirus 3h (HvAV-3h), encoded by ORF85, and to explore its potential roles in the interaction between the ascovirus and its host. Our results demonstrate the importance of this species-specific protein to HvAV-3h replication in host cells. <i>In vivo</i>, silencing of this gene for 12-72 h significantly increased the expression of some innate immunity-associated genes, including Toll (114-fold), IMD (44.7-fold) and Hopscotch (22.9-fold). In parallel, we detected significant gradual increases in MyD88 and Relish and decreases in PIAS. Moreover, histopathological analyses of infected larval tissues indicated reduced tissue damage after 72 h of ORF85 gene silencing. The prokaryotic expression of the HvAV-3h aegerolysin, followed by feeding to third-instar <i>Spodoptera exigua</i> larvae for 24 or 48 h led to significant reductions in larval weight. Moreover, the <i>in vitro</i> treatment demonstrated a bactericidal action against <i>Lysinibacillus xylanilyticus</i>, a bacterial resident of some insect guts. Overall, our findings suggest that the protein encoded by ORF85 is associated with the pathogenicity of HvAV-3h and its ability to replicate in host cells. Additionally, aegerolysin may inhibit or kill specific bacterial species in the host microbiome during infection, potentially modulating the host immune response.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 5","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12163727/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144173898","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 impact of pre-existing immunity on the emergence of within-host immune-escape mutations in Omicron lineages.","authors":"Muna N Ahmed, Ummay Salma Abu Habib, Abdallah M Abdallah, Mohamed M Emara, Arnab Pain, Asmaa A Althani, Gheyath K Nasrallah, Hadi M Yassine, Hebah A Al-Khatib","doi":"10.1099/jgv.0.002108","DOIUrl":"10.1099/jgv.0.002108","url":null,"abstract":"<p><p>The Omicron variant of SARS-CoV-2 circulating amongst highly immunized populations is anticipated to induce immunological pressures, potentially compromising existing immunity. This study investigates vaccine-induced immunity's impact on within-host diversity of Omicron variants and evaluates sub-consensus mutations at spike protein antigenic sites. Next-generation sequencing assessed the within-host diversity of 728 Omicron-positive samples (421 vaccinated; 307 unvaccinated). Quantitative analysis revealed limited vaccine impact, regardless of lineage, vaccine type or doses. Non-lineage mutations (39, 33 and 25 in BA.2*, BA.4* and BA.5* lineages, respectively) were detected, some showing higher incidence in vaccinated individuals. Six mutations detected at sub-consensus levels at antigenic sites suggest increased immune pressure on the spike protein in vaccinated individuals. Four high-prevalence antigenic mutations, absent from global GISAID sequences, were identified. Although within-host diversity did not significantly differ between vaccination statuses, detected mutations suggest that vaccine-induced immunity may influence within-host mutation patterns.</p>","PeriodicalId":15880,"journal":{"name":"Journal of General Virology","volume":"106 5","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12075854/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143995922","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":"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":"A high frequency of detection of koala retrovirus fragments in Victorian koalas suggests historic integration of KoRV.","authors":"Louize Zheng, Alistair R Legione","doi":"10.1099/jgv.0.002097","DOIUrl":"https://doi.org/10.1099/jgv.0.002097","url":null,"abstract":"<p><p>Recombinant koala retrovirus (recKoRV) is a recently discovered variant of koala retrovirus (KoRV), which likely emerged due to recombination with another retrovirus (such as Phascolarctos endogenous retrovirus). KoRV spread and endogenization in Australia were thought to be ongoing in a north to south direction given the low prevalence of the virus in southern koala populations, based on molecular detection of the <i>pol</i> gene. However, recKoRV has highlighted that fragments of KoRV with the <i>pol</i> region missing are present within southern koalas. In this study, a new 5'-region-based KoRV PCR assay was developed, capable of detecting both intact KoRV and all known variants of recKoRV. Using this assay, 319 archived DNA samples from 287 Victorian koalas were retested to investigate KoRV endogenization. We found 98.3% (282/287) of these samples were positive for the KoRV-5' fragment, the majority of which were KoRV-<i>pol</i> negative (222/287) on prior testing. Our findings demonstrate extensive KoRV integration into the Victorian koala populations, suggestive of a historic presence of KoRV in Victorian koalas. This finding makes biological sense relative to the translocation history of Victorian koalas, compared to the prior paradigm of low virus prevalence, and provides new epidemiological and practical management implications.</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/PMC12032406/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144022142","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}