Veterinary microbiology最新文献

{"title":"Exploring the epidemiology and genetic complexity of Escherichia coli in vertically integrated pig production systems using whole genome sequencing","authors":"Anna Vilaró ,&nbsp;Laia Serra ,&nbsp;Emma Solé ,&nbsp;Ingrid Seró ,&nbsp;Elena Novell ,&nbsp;Vicens Enrique-Tarancón ,&nbsp;Lorenzo Fraile ,&nbsp;Lourdes Migura-Garcia","doi":"10.1016/j.vetmic.2025.110610","DOIUrl":"10.1016/j.vetmic.2025.110610","url":null,"abstract":"<div><div><em>Escherichia coli</em> is a major pathogen responsible for enteric diseases in swine. This study aims to assess the genetic diversity, virulence factors, and antimicrobial resistance genes of <em>E. coli</em> isolated from diarrheic pigs within Spanish integrated production systems. Metadata, including epidemiological data and minimum inhibitory concentration (MIC), was collected for 350 clinical isolates reported to the laboratory between 2018 and 2022. MIC analysis using Ward’s hierarchical clustering identified 17 phenotypic resistance clusters. A subset of 206 isolates, representing different production pyramids and phenotypic clusters, was selected for whole genome sequencing (WGS). <em>In silico</em> serotyping and multilocus sequence typing revealed high genetic diversity, with predominant serotypes O138:H14, O147:H14, O141:H4, and O108:H39, and sequence types ST10 and ST42. Only three ST131 isolates were found in a single production pyramid suggesting that swine associated ST131 is not contributing significantly to the epidemiology of human infections associated to this ST. Isolates were classified into six phylogroups, with phylogroup A being the most represented. AMR profiling identified a high percentage of resistance (&gt; 50 %) to tetracyclines, aminoglycosides, quinolones, trimethoprim and sulphonamides, while resistance to third-generation cephalosporins and colistin remained low (&lt; 25 %). Comparative genomic analysis demonstrated high genetic diversity within production pyramids, although, some clones persisted over time, suggesting transmission within batches. Statistical analyses found no association between genetic traits and farm origins, although outbreaks often involved clones with minimal SNP differences. This study underscores the complexity of <em>E. coli</em> transmission in swine and highlights the need for genomic surveillance to monitor AMR.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110610"},"PeriodicalIF":2.4,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144364436","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"BVDV antagonizes the antiviral activity of MDA5 by promoting its degradation via CCDC50-dependent selective autophagy","authors":"Zhen Wang,&nbsp;Shizhe Liu,&nbsp;Liang Xu,&nbsp;Jingyu Wang,&nbsp;Shaotang Ye,&nbsp;Siqi Cai,&nbsp;Kun Jia,&nbsp;Shoujun Li","doi":"10.1016/j.vetmic.2025.110601","DOIUrl":"10.1016/j.vetmic.2025.110601","url":null,"abstract":"<div><div>Bovine viral diarrhea-mucosal disease (BVD-MD), caused by bovine viral diarrhea virus (BVDV), is a major infectious disease affecting the cattle industry. The nonstructural protein NS4B of BVDV has been shown to induce autophagy and antagonize the expression of the host innate immune sensor MDA5. However, the precise mechanism underlying NS4B-mediated suppression of MDA5 remains unclear. In this study, we demonstrate that NS4B interacts with the host protein CCDC50, as confirmed by co-immunoprecipitation and indirect immunofluorescence assays. Stable overexpression of CCDC50 significantly promoted MDA5 degradation and enhanced BVDV replication, whereas CCDC50 knockdown markedly impaired NS4B-mediated degradation of MDA5 in HEK293T cells. Interestingly, CCDC50 also suppressed the production of type I interferons (IFN-I) and interferon-stimulated genes (ISGs) during BVDV infection. Furthermore, the translocation of CCDC50 reduced MDA5 protein levels through the autophagy pathway. Mechanistically, we found that CCDC50 interacts with MDA5 and facilitates NS4B-mediated autophagic degradation of MDA5. These findings uncover a novel mechanism by which BVDV NS4B hijacks the host protein CCDC50 to subvert antiviral innate immunity by promoting MDA5 autophagic degradation and suppressing IFN-I signaling.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110601"},"PeriodicalIF":2.4,"publicationDate":"2025-06-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144313144","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Gross pathology and epidemiological features of mule deerpox virus infections in farmed white-tailed deer (Odocoileus virginianus) in Florida","authors":"An-Chi Cheng ,&nbsp;Pedro H.O. Viadanna ,&nbsp;Tracey L. Moquin ,&nbsp;Laura Roldan ,&nbsp;John A. Lednicky ,&nbsp;Samantha M. Wisely ,&nbsp;Kuttichantran Subramaniam ,&nbsp;Juan M. Campos Krauer","doi":"10.1016/j.vetmic.2025.110608","DOIUrl":"10.1016/j.vetmic.2025.110608","url":null,"abstract":"<div><div>Mule deerpox virus (DPV) is a member of the <em>Poxviridae</em> family that affects various deer species, causing crustaceous skin lesions and potentially lethal infections. In this study, we aimed to investigate the spatial and temporal distribution of DPV in farmed white-tailed deer (WTD; <em>Odocoileus virginianus</em>) in Florida, USA, from 2017 to 2023. Necropsies were performed, and specimens were collected from 776 deer. Focusing on 145 animals with DPV-like lesions, polymerase chain reaction (PCR) testing and whole genome sequencing confirmed the presence of DPV in multiple specimen types. The results indicated that 49 out of 145 deer (33.8 %, 95 % CI: 25.7 %-40.9 %) tested positive for DPV. Mule deerpox virus was identified in 20 of the 37 counties and 8 of the 10 deer management units (DMUs) where we collected specimens. All DPV infection cases occurred in summer and fall. Lesion swabs (4/4, 100 %) and lesion tissues (16/18, 89 %) exhibited the highest PCR-positivity rates among the specimens collected from DPV-infected animals, while no whole blood samples (0/13, 0 %) tested positive. Additionally, DPV nucleic acid was also detected in fecal swabs (4/9, 44 %), suggesting that DPV may be transmitted through the oral-fecal route. Fawns aged 1–3 months (37/70, 52.9 %, 95 % CI: 41.3 %-64.1 %) exhibited statistically higher positivity rates than other age groups. This is the first study investigating the spatial and temporal patterns of DPV in farmed WTD in Florida. The findings emphasize the need for enhanced disease surveillance, non-invasive testing methods, and preventive measures to mitigate the impact of DPV on the deer farming industry and wildlife conservation.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110608"},"PeriodicalIF":2.4,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144365988","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evidence of autophagic and Wnt/β-catenin signaling occurrence during Schmallenberg virus (SBV) infection on BHK-21 cells","authors":"Consiglia Longobardi ,&nbsp;Davide Lelli ,&nbsp;Manuel Corsa ,&nbsp;Ugo Pagnini ,&nbsp;Francesco Origgi ,&nbsp;Hyun-Jin Shin ,&nbsp;Gianmarco Ferrara","doi":"10.1016/j.vetmic.2025.110609","DOIUrl":"10.1016/j.vetmic.2025.110609","url":null,"abstract":"<div><div>Schmallenberg virus (SBV) is a ruminant pathogen that is widely distributed around the world, but little is known about its interactions with permissive cells or about its pathogenetic mechanisms. This study highlighted, through a phenotypic approach, the changes in the expression of some autophagy and Wnt/β-catenin pathway markers that SBV causes on baby hamster kidney (BHK-21) cells. Western blot analysis revealed that SBV caused autophagy induction at 48 h post infection. Several markers, such as PI3K, Akt, and Wnt/β-catenin, were downregulated at the same time point. Furthermore, downregulation in the expression of PI3K, p-mTOR and Beclin-1 showed differences between multiplicity of infection (MOI) 0.05 and 0.5, but not between MOI 0.5 and 1.5. Exceptions for this trend were Akt and LC3-II, which progressively decreased depending on time, and β-catenin, whose expression almost disappeared regardless of MOI. The use of several chemical inducers and inhibitors has demonstrated the efficacy of late autophagy inhibitors (bafilomycin and chloroquine) in significantly lowering SBV infection and also preventing the changes caused by viral replication. Early autophagy inhibitors and inducers showed no effect on cellular viability or viral titers. Silencing the expression of Akt and β-catenin revealed a slight increase in the expression of viral glycoprotein Gc. These findings revealed the relationship that SBV has in important cellular regulatory pathways, expanding the knowledge about the cellular interactions of this virus and suggesting a central role for late stages of autophagy in the replication of this bunyavirus.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110609"},"PeriodicalIF":2.4,"publicationDate":"2025-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144307290","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Flagellin deficiency drives multi-drug resistance in Salmonella through biofilm adaptation and efflux pump activation","authors":"Yanzhe Tang ,&nbsp;Huijuan Chen ,&nbsp;Jiali Deng ,&nbsp;Xiumei Yang ,&nbsp;Huoying Shi ,&nbsp;Quan Li","doi":"10.1016/j.vetmic.2025.110607","DOIUrl":"10.1016/j.vetmic.2025.110607","url":null,"abstract":"<div><div><em>Salmonella</em> remains a leading foodborne pathogen of global public health concern. Of particular clinical relevance is the monophasic variant of <em>S.</em> Typhimurium, serotyped as <em>S.</em> 4,[5],12:i:-, which has emerged as an increasingly prevalent multi-drug resistance (MDR) strain worldwide. Characterized by the absence of phase 2 flagellar antigen expression, this variant has drawn significant attention due to its association with antimicrobial resistance. In this study, we systematically investigated the impact of flagellin deficiency on antibiotic tolerance in <em>S.</em> Typhimurium and <em>S.</em> Choleraesuis through the construction of isogenic mutants rSC0196 (<em>S.</em> Typhimurium UK-1(Δ<em>fljB</em>Δ<em>fliC</em>)) and rSC0199 (<em>S.</em> Choleraesuis C78-3(Δ<em>fljB</em>Δ<em>fliC</em>)). Our findings reveal that flagellin gene deletion confers enhanced antibiotic resistance in both serovars, despite significantly impairing their biofilm-forming capacity. Intriguingly, while biofilm biomass was reduced in the mutants, the residual biofilms displayed markedly increased antibiotic tolerance. Further studies demonstrated that flagellin deficiency significantly upregulated efflux pump activity in both mutant strains. These findings provide compelling evidence that flagellin deletion may serve as a key driver of MDR in <em>S.</em> 4,[5],12:i:- clinical isolates, potentially through dual mechanisms involving biofilm phenotypic alterations and efflux pump potentiation. This work not only advances our fundamental understanding of flagellin function in <em>Salmonella</em> pathogenesis but also provides valuable insights for the development of novel antimicrobial strategies targeting flagellin-mediated pathways.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110607"},"PeriodicalIF":2.4,"publicationDate":"2025-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144307291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neutrophils undergo migration and produce an antiviral response following porcine epidemic diarrhea virus infection","authors":"Yichao Ma,&nbsp;Xinming Qin,&nbsp;Jian Zheng,&nbsp;Xuebin Peng,&nbsp;Shiqi Liu,&nbsp;Ruoyang Lin,&nbsp;Baoyan Meng,&nbsp;Xiaojing Cui,&nbsp;Qian Yang","doi":"10.1016/j.vetmic.2025.110605","DOIUrl":"10.1016/j.vetmic.2025.110605","url":null,"abstract":"<div><div>The importance of the host's initial innate immune and acute inflammatory responses in combating viral infections has increasingly garnered interest. Neutrophils are the initial responders to infection and inflammation; however, their specific function in the host's antiviral immune defence remains ambiguous. Here, we observed that the porcine epidemic diarrhea virus (PEDV), which is the primary pathogen responsible for diarrhea in newborn piglets, triggered the release of intestinal neutrophil-attracting chemokines, recruiting neutrophils to the intestinal epithelium and inducing an antiviral response. In the co-culture model of Vero cells (a cell line used to study the replication and dynamics of PEDV <em>in vitro</em>) and neutrophils, infection of Vero cells with PEDV facilitated the transepithelial migration of neutrophils. Additionally, direct contact between neutrophils and PEDV-infected Vero cells enhanced viral clearance. Transcriptome analysis revealed significant upregulation of C3 expression in Vero cells after neutrophils were introduced 6 h after PEDV infection, and the antiviral effect of neutrophils was diminished after siRNA-mediated knockdown of C3. Consistently, C3 expression was markedly upregulated in the small intestine of PEDV-infected piglets, supporting complement system activation. Furthermore, the supernatant from cells infected with PEDV has the capacity to increase the expression of antiviral agents such as β-defensin-2 and myeloperoxidase in neutrophils. Taken together, our results reveal the role of neutrophil recruitment in the antiviral response during enterovirus infection, highlighting the importance of neutrophilic activity in the host antiviral innate immune response.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110605"},"PeriodicalIF":2.4,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144297520","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cooperative nuclear import of duck plague virus DNA polymerase subunits: pUL42 NLS Enhances pUL30 nuclear import and viral replication, with VP22 as a compensatory factor","authors":"Yuxi Cui ,&nbsp;Mingshu Wang ,&nbsp;Anchun Cheng ,&nbsp;Qiao Yang ,&nbsp;Xumin Ou ,&nbsp;Di Sun ,&nbsp;Yu He ,&nbsp;Xinxin Zhao ,&nbsp;Ying Wu ,&nbsp;Shaqiu Zhang ,&nbsp;Bin Tian ,&nbsp;Juan Huang ,&nbsp;Zhen Wu ,&nbsp;Yanling Yu ,&nbsp;Ling Zhang ,&nbsp;Dekang Zhu ,&nbsp;Shun Chen ,&nbsp;Mafeng Liu ,&nbsp;Renyong Jia","doi":"10.1016/j.vetmic.2025.110603","DOIUrl":"10.1016/j.vetmic.2025.110603","url":null,"abstract":"<div><div>Duck plague (DP), caused by duck plague virus (DPV), is an acute, febrile, and septic disease fatal to geese, ducks, and other wild waterfowl. The DPV <em>UL42</em> gene product, pUL42, an accessory subunit of the viral DNA polymerase, whose nuclear import is critical for viral replication; however, the underlying mechanism remains unclear. In this study, we identified a 33-amino acids region at the C-terminus of pUL42, containing its nuclear localization signal (NLS). This NLS not only mediated the nuclear entry of pUL42, but also promoted the nuclear import of the DNA polymerase catalytic subunit pUL30. The deletion of this region impaired viral replication. Furthermore, we discovered that the viral protein VP22 alleviates the nuclear import defect of NLS-deficient pUL42 through compensatory nuclear trafficking facilitation. Our findings revealed the first mechanistic model for DPV pUL42 nuclear translocation, offering insights into conserved herpesvirus replication mechanisms and highlighting potential antiviral strategies targeting the pUL42-VP22 transport axis.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110603"},"PeriodicalIF":2.4,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144291678","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pseudorabies virus DNA binding to porcine NLRC3 unleashes the activation of the porcine NLRP3 inflammasome","authors":"Minjie Li ,&nbsp;Xiangyu Huang ,&nbsp;Hongyan Yin ,&nbsp;Lvye Chai ,&nbsp;Haiwei Wang ,&nbsp;Xin Li","doi":"10.1016/j.vetmic.2025.110604","DOIUrl":"10.1016/j.vetmic.2025.110604","url":null,"abstract":"<div><div>Viral infection activates multiple inflammatory pathways, with the NLRP3 inflammasome playing a pivotal role in host defense. However, negative regulation of the NLRP3 inflammasome is essential for maintaining host homeostasis. Here, we report that double-stranded DNA (dsDNA) from pseudorabies virus (PRV) induces NLRP3 inflammasome activation and pyroptosis through gasdermin D (GSDMD) cleavage and IL-1β secretion. Importantly, the inhibitory NLR porcine NLRC3 (pNLRC3) interacts with porcine NLRP3 (pNLRP3) and attenuates GSDMD cleavage and IL-1β release. Upon PRV infection, overexpression of pNLRC3 enhances GSDMD cleavage and lactate dehydrogenase release, whereas knockdown of pNLRC3 reduces pyroptosis. Mechanistically, pNLRC3 binds PRV dsDNA and unleashes its inhibitory effect on pNLRP3, functioning as a checkpoint to regulate inflammasome activation. Furthermore, pNLRC3 contributes to PRV restriction by controlling viral replication and limiting infection. In summary, our findings reveal a dual role of pNLRC3, acting both as a negative regulator of the pNLRP3 inflammasome and as a viral sensor that regulates pyroptosis-mediated viral clearance. These insights provide a deeper understanding of virus-host interactions and innate immune regulation.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110604"},"PeriodicalIF":2.4,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144291249","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"TGEV-M up-regulates ATP5D to promote mPTP opening via inhibiting BIRC6-236aa encoded by circBIRC6-2","authors":"Jianxiong Guo ,&nbsp;Lingling Chang ,&nbsp;Fengxi Zhang,&nbsp;Xingyi Dang,&nbsp;Xiangyin Zhang,&nbsp;Fenli Zhang,&nbsp;Xiaomin Zhao,&nbsp;Dewen Tong","doi":"10.1016/j.vetmic.2025.110606","DOIUrl":"10.1016/j.vetmic.2025.110606","url":null,"abstract":"<div><div>Transmissible gastroenteritis virus (TGEV) infection can down-regulate circBIRC6–2 expression and induce mitochondrial permeability transition pore (mPTP) opening abnormally. BIRC6–236aa, encoded by circBIRC6–2, can suppress mPTP opening by interacting with VDAC1. However, the molecular mechanism of circBIRC6–2 downregulation by TGEV infection is unsuspected, and it is unclear that whether BIRC6–236aa can inhibit mPTP opening by post translational modifications (PTM) and downstream regulatory proteins. In this study, we found that TGEV membrane protein (TGEV-M) can suppress circBIRC6–2 expression by interacting with heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) and inhibiting the translocation of hnRNPA1, which can bind to baculoviral IAP repeat containing 6 (<em>birc6</em>) pre-mRNA to promote the formation of circBIRC6–2. In addition, glycogen synthase kinase-3 beta (GSK-3β) can phosphorylate Ser180 of BIRC6–236aa, and phosphorylated-BIRC6–236aa (p-BIRC6–236aa) can inhibit mPTP opening. 271 differential expression proteins (DEPs) were identified after overexpression of BIRC6–236aa. ATP synthase, H⁺ transporting, mitochondrial F1 complex, delta subunit (ATP5D, also named ATP5F1D), one of the DEPs was down-regulated in response to BIRC6–236aa, and ATP5D can promote mPTP opening induced by TGEV. In conclusion, TGEV-M can suppress the expression of circBIRC6–2 through targeting hnRNPA1. The Ser180 of BIRC6–236aa encoded by circBIRC6–2 can be phosphorylated by GSK-3β, and p-BIRC6–236aa can inhibit mPTP opening by down-regulating ATP5D expression.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110606"},"PeriodicalIF":2.4,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144330124","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The ubiquitin-proteasome system is essential for efficient propagation of Pseudorabies virus","authors":"Wei Wen ,&nbsp;Yi Lu ,&nbsp;Zhendong Zhang ,&nbsp;Wenqiang Wang ,&nbsp;Zhenbang Zhu ,&nbsp;Xiangdong Li","doi":"10.1016/j.vetmic.2025.110602","DOIUrl":"10.1016/j.vetmic.2025.110602","url":null,"abstract":"<div><div>Pseudorabies virus (PRV) is a pathogen that affects multiple animal species and can infect nearly all mammals, with pigs being its natural host. PRV infection in pigs causes significant economic losses in global pig industry. The ubiquitin-proteasome system (UPS) plays a crucial role in cellular protein homeostasis by regulating protein quality. Nevertheless, the interplay between PRV and UPS is not well understood. In this study, We investigated the role of UPS in PRV replication. We found that the proteasome inhibitors (MG132, Lactacystin, and Bortezomib) significantly decreased PRV replication in a dose dependent manner. The suppression of the UPS primarily occurs at the early stage of virus replication. MG132 impaired the PRV uncoating process. In addition, PRV infection dramatically reduced the expression of poly-ubiquitin and free ubiquitin. Ectopic expression of ubiquitin in MG132-treated cells partially mitigated the inhibitory effect of MG132 on PRV proliferation. These findings suggest that PRV exploits the UPS to enhance its own replication.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110602"},"PeriodicalIF":2.4,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144288964","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}