Veterinary microbiology最新文献_第4页

Flagellin deficiency drives multi-drug resistance in Salmonella through biofilm adaptation and efflux pump activation 鞭毛蛋白缺乏通过生物膜适应和外排泵激活驱动沙门氏菌的多重耐药

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-14 DOI: 10.1016/j.vetmic.2025.110607

Yanzhe Tang , Huijuan Chen , Jiali Deng , Xiumei Yang , Huoying Shi , Quan Li

{"title":"Flagellin deficiency drives multi-drug resistance in Salmonella through biofilm adaptation and efflux pump activation","authors":"Yanzhe Tang , Huijuan Chen , Jiali Deng , Xiumei Yang , Huoying Shi , 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}

引用次数: 0

Neutrophils undergo migration and produce an antiviral response following porcine epidemic diarrhea virus infection 中性粒细胞在猪流行性腹泻病毒感染后进行迁移并产生抗病毒反应

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-13 DOI: 10.1016/j.vetmic.2025.110605

Yichao Ma, Xinming Qin, Jian Zheng, Xuebin Peng, Shiqi Liu, Ruoyang Lin, Baoyan Meng, Xiaojing Cui, Qian Yang

{"title":"Neutrophils undergo migration and produce an antiviral response following porcine epidemic diarrhea virus infection","authors":"Yichao Ma, Xinming Qin, Jian Zheng, Xuebin Peng, Shiqi Liu, Ruoyang Lin, Baoyan Meng, Xiaojing Cui, 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}

引用次数: 0

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 鸭瘟病毒DNA聚合酶亚基的协同核输入：pUL42 NLS增强pUL30核输入和病毒复制，VP22作为补偿因子

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-13 DOI: 10.1016/j.vetmic.2025.110603

Yuxi Cui , Mingshu Wang , Anchun Cheng , Qiao Yang , Xumin Ou , Di Sun , Yu He , Xinxin Zhao , Ying Wu , Shaqiu Zhang , Bin Tian , Juan Huang , Zhen Wu , Yanling Yu , Ling Zhang , Dekang Zhu , Shun Chen , Mafeng Liu , Renyong Jia

{"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 , Mingshu Wang , Anchun Cheng , Qiao Yang , Xumin Ou , Di Sun , Yu He , Xinxin Zhao , Ying Wu , Shaqiu Zhang , Bin Tian , Juan Huang , Zhen Wu , Yanling Yu , Ling Zhang , Dekang Zhu , Shun Chen , Mafeng Liu , 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}

引用次数: 0

Pseudorabies virus DNA binding to porcine NLRC3 unleashes the activation of the porcine NLRP3 inflammasome 伪狂犬病毒DNA结合猪NLRC3释放猪NLRP3炎性体的激活

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-13 DOI: 10.1016/j.vetmic.2025.110604

Minjie Li , Xiangyu Huang , Hongyan Yin , Lvye Chai , Haiwei Wang , Xin Li

{"title":"Pseudorabies virus DNA binding to porcine NLRC3 unleashes the activation of the porcine NLRP3 inflammasome","authors":"Minjie Li , Xiangyu Huang , Hongyan Yin , Lvye Chai , Haiwei Wang , 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}

引用次数: 0

TGEV-M up-regulates ATP5D to promote mPTP opening via inhibiting BIRC6-236aa encoded by circBIRC6-2 TGEV-M通过抑制circBIRC6-2编码的BIRC6-236aa，上调ATP5D，促进mPTP打开

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-13 DOI: 10.1016/j.vetmic.2025.110606

Jianxiong Guo , Lingling Chang , Fengxi Zhang, Xingyi Dang, Xiangyin Zhang, Fenli Zhang, Xiaomin Zhao, Dewen Tong

{"title":"TGEV-M up-regulates ATP5D to promote mPTP opening via inhibiting BIRC6-236aa encoded by circBIRC6-2","authors":"Jianxiong Guo , Lingling Chang , Fengxi Zhang, Xingyi Dang, Xiangyin Zhang, Fenli Zhang, Xiaomin Zhao, 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<sup>+</sup> 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}

引用次数: 0

The ubiquitin-proteasome system is essential for efficient propagation of Pseudorabies virus 泛素-蛋白酶体系统对伪狂犬病毒的高效繁殖至关重要

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-13 DOI: 10.1016/j.vetmic.2025.110602

Wei Wen , Yi Lu , Zhendong Zhang , Wenqiang Wang , Zhenbang Zhu , Xiangdong Li

{"title":"The ubiquitin-proteasome system is essential for efficient propagation of Pseudorabies virus","authors":"Wei Wen , Yi Lu , Zhendong Zhang , Wenqiang Wang , Zhenbang Zhu , 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}

引用次数: 0

UGPase: A novel molecule that regulates LPS synthesis, virulence, and immunogenicity of Brucella melitensis UGPase：一种调节布鲁氏菌脂多糖合成、毒力和免疫原性的新分子

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-11 DOI: 10.1016/j.vetmic.2025.110600

Si Chen , Yuxin Liu , Yang Gao , Dong Zhang , Ru Zhang , Fei Tu , Nan Li , Qingkui Jiang , Linna Liu , Yanling Yang

{"title":"UGPase: A novel molecule that regulates LPS synthesis, virulence, and immunogenicity of Brucella melitensis","authors":"Si Chen , Yuxin Liu , Yang Gao , Dong Zhang , Ru Zhang , Fei Tu , Nan Li , Qingkui Jiang , Linna Liu , Yanling Yang","doi":"10.1016/j.vetmic.2025.110600","DOIUrl":"10.1016/j.vetmic.2025.110600","url":null,"abstract":"<div><div>UTP-glucose-1-phosphoryl transferase (UGPase) catalyzes the synthesis of UDP-glucose, a key precursor for glycogen production and an essential component in bacterial lipopolysaccharide (LPS) synthesis. In this study, we demonstrate that UGPase deletion significantly disrupted LPS synthesis in <em>Brucella</em>, leading to a phenotypic shift from a smooth to a rough type and a marked reduction in bacterial virulence. <em>In vitro</em> and <em>in vivo</em> experiments revealed that UGPase deletion impaired <em>Brucella</em>’s ability to infect host cells and diminished its pathogenicity in mice. The deletion also significantly altered the LPS structure of the 16M-ΔUGPase strain, reducing its specific binding to <em>Brucella</em>-positive serum. Additionally, macrophages infected with the UGPase deletion mutant exhibited a decreased inflammatory response. In mice, infection with the mutant strain led to altered cytokine profiles, characterized by upregulation of pro-inflammatory markers (TNF-ɑ, IFN-γ, and IL-2) and downregulation of anti-inflammatory markers (IL-10 and IL-4) compared to infections with the wild-type strain. This study identifies UGPase as a critical determinant of <em>Brucella</em> virulence and immunogenicity for the first time. The findings provide novel insights into the molecular mechanisms underlying <em>Brucella</em> pathogenesis and highlight UGPase as a promising target for the development of <em>Brucella</em> vaccines.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110600"},"PeriodicalIF":2.4,"publicationDate":"2025-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144549590","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}

引用次数: 0

The unforeseen presence of Bordetella pertussis in animal hosts beyond humans: Assessing reliability amidst metagenomic species-resolution challenges 百日咳博德泰拉在人类以外的动物宿主中不可预见的存在：在宏基因组物种分辨率挑战中评估可靠性

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-10 DOI: 10.1016/j.vetmic.2025.110599

Wenjuan Zhao, Zengguo Wang

引用次数: 0

Genotyping of Ehrlichia canis TRP36 isolated from ticks and dogs in Iran 伊朗蜱和犬分离的犬埃利希体TRP36基因分型研究

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-10 DOI: 10.1016/j.vetmic.2025.110592

Iradj Ashrafi Tamai , Hamid Staji , Babak Pakbin

{"title":"Genotyping of Ehrlichia canis TRP36 isolated from ticks and dogs in Iran","authors":"Iradj Ashrafi Tamai , Hamid Staji , Babak Pakbin","doi":"10.1016/j.vetmic.2025.110592","DOIUrl":"10.1016/j.vetmic.2025.110592","url":null,"abstract":"<div><div><em>Ehrlichia canis</em> is the primary causative agent of Canine Monocytic Ehrlichiosis, a tick-borne zoonosis transmitted by <em>Rhipicephalus sanguineus</em> tick that significantly impacts canine health worldwide. This study investigated the prevalence rate, genetic diversity, and molecular characterization of <em>E. canis</em> isolated from dogs collected from northern areas of Iran and Tehran city, focusing on the tandem repeat protein 36 (<em>TRP36</em>) gene. A total of 355 blood samples and 199 ticks were collected from stray, sheltered, and household dogs. We identified <em>E. canis</em> in 21.4 % of blood and 39.19 % of tick samples, with TRP36 detected in 31 samples. Phylogenetic analysis of the <em>TRP36</em> gene revealed 15 sequence types (STs), with molecular signatures and two highly conserved regions across all isolates. Notably, 60 % of isolates clustered within the Taiwan genotypic group, exhibiting specific amino acid signatures. Our findings highlight the genetic diversity and epidemiological characteristics of <em>E. canis</em> in Iran, providing valuable insights into the pathogen’s molecular evolution and regional distribution. These results contribute to a better understanding of <em>E. canis</em> genotypes and their implications for ehrlichiosis diagnostics, treatment, and epidemiological control strategies.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110592"},"PeriodicalIF":2.4,"publicationDate":"2025-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144271313","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}

引用次数: 0

IRF8 facilitates bovine ephemeral fever virus replication by downregulating IRF9 IRF8通过下调IRF9促进牛短暂热病毒复制

IF 2.4 2区农林科学

Veterinary microbiology Pub Date : 2025-06-09 DOI: 10.1016/j.vetmic.2025.110597

Peili Hou , Jie Chen , Hongchao Zhu , Xiaoyang Yao, Zixuan Gao, Yingying Li, Hongbin He, Hongmei Wang

{"title":"IRF8 facilitates bovine ephemeral fever virus replication by downregulating IRF9","authors":"Peili Hou , Jie Chen , Hongchao Zhu , Xiaoyang Yao, Zixuan Gao, Yingying Li, Hongbin He, Hongmei Wang","doi":"10.1016/j.vetmic.2025.110597","DOIUrl":"10.1016/j.vetmic.2025.110597","url":null,"abstract":"<div><div>Interferon regulatory factor 8 (IRF8), an essential member of the IRFs protein family, serves as a critical transcriptional regulator in cytokine signaling, gene transcription, and the differentiation and proliferation of immune cells. However, its function on the bovine ephemeral fever virus (BEFV) infection has not been described. In this study, we demonstrate that BEFV infection upregulates the expression of IRF8, and IRF8 promotes the replication of BEFV. Subsequent investigations reveal that IRF8 suppresses the type I IFN signaling pathway via the degradation of IRF9 in the context of BEFV infection. Mechanistically, IRF8 up-regulates NEDD4 Like E3 ubiquitin ligase (NEDD4L) expression, thereby promoting the IRF9 degradation through the ubiquitin-proteasome pathway. Notably, the inhibitory effect of IRF8 on the BEFV-mediated type I IFN signaling pathway was markedly reduced, and the promoting effect of IRF8 on BEFV replication was attenuated in NEDD4L-knockdown cells, unveiling a novel mechanism by which IRF8-NEDD4L-IRF9 axis hijacks type I interferon signaling pathway to facilitate BEFV infection. These findings board valuable insights into the function of IRF8, which may serve as a basis for the design of novel antiviral agents.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"307 ","pages":"Article 110597"},"PeriodicalIF":2.4,"publicationDate":"2025-06-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144270862","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}

引用次数: 0