Emerging Microbes & Infections最新文献

{"title":"Limited added benefit of seasonal influenza vaccination before A(H5) vaccination in mice and ferrets challenged with A(H5N1).","authors":"Masato Hatta, Ying Huang, Jeremy A Duke, Joseph R Rouse, Chenchen Feng, Xudong Lin, Li Wang, Melvyn R Almanzar-Jordan, Zhu-Nan Li, James Stevens, Min Z Levine, David E Wentworth, Vivien G Dugan, C Todd Davis, Bin Zhou","doi":"10.1080/22221751.2026.2731495","DOIUrl":"10.1080/22221751.2026.2731495","url":null,"abstract":"<p><p>Limited A(H5)-specific vaccine supply is expected early in a potential A(H5N1) pandemic, raising the question of whether licensed seasonal influenza vaccines could enhance protection when administered before A(H5) vaccination. We evaluated this strategy in mouse and ferret models using clade 2.3.4.4b A(H5N1) viruses. Seasonal influenza vaccination induced antibodies to seasonal haemagglutinins but did not induce detectable antibodies against A(H5) and did not consistently enhance A(H5)-directed antibody responses after A(H5) vaccination. In lethal challenge studies, seasonal vaccine priming before A(H5) vaccination was associated with improved outcomes compared with A(H5) vaccination alone in one of three mouse experiments, but this effect was not observed in the other two mouse experiments or in ferrets. These findings suggest that seasonal influenza vaccine priming provides limited added benefit to A(H5) vaccine-mediated protection against A(H5N1) under the conditions tested.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":"15 1","pages":"2731495"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13600297/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149012018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ATG13 promotes K63-linked polyubiquitination of MAVS via ASB1 to restrict influenza A virus replication.","authors":"Yiyuan Lu, Jiale Chen, Huimin Xiao, Jinze Li, Haixu Wang, Tianhao Liang, Jiarui Wang, Xueyi Pang, Mingyang Cheng, Yu Sun, Tong Cui, Feiyang Pu, Jiaxing Zhan, Yibo Zhao, Hongyu Bao, Wentao Yang, Yanlong Jiang, Guilian Yang, Jianzhong Wang, Xin Cao, Chunfeng Wang, Xue Bai, Yan Zeng","doi":"10.1080/22221751.2026.2731501","DOIUrl":"10.1080/22221751.2026.2731501","url":null,"abstract":"<p><p>Autophagy-associated protein 13 (ATG13) plays a pivotal role in regulating the assembly of the autophagy initiation complex. However, the function and mechanism of action of ATG13 during influenza virus infection remain incompletely understood. This study elucidates that ATG13 restricts influenza A virus (IAV) replication while potentiating the activation of the type I interferon (IFN-I) pathway. Mechanistically, coimmunoprecipitation assays revealed that ATG13 interacts with MAVS and recruits the E3 ubiquitin ligase ASB1 to catalyze K63-linked polyubiquitination at the K348 residue, thereby amplifying the downstream antiviral signalling cascade. Furthermore, through dual-luciferase reporter assays and pharmacological inhibition of autophagy, we confirmed that this novel immunomodulatory function of ATG13 is independent of the canonical autophagy pathway. The present study identifies ATG13 as a novel host restriction factor against IAV and reveals a nonautophagic role for ATG13 in antiviral innate immunity.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":" ","pages":"2731501"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13587579/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148900117","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Repurposing loratadine to reverse colistin resistance in <i>Klebsiella pneumoniae</i> through targeting lipid A modification.","authors":"Xiaoying Wu, Zhanzhe Ge, Haojie Zhan, Mengxiang Zheng, Yiming Feng, Yajun Zhai, Li Yuan, Jianhua Liu, Yushan Pan, Gongzheng Hu, Xiaoyuan Ma, Dandan He","doi":"10.1080/22221751.2026.2623697","DOIUrl":"10.1080/22221751.2026.2623697","url":null,"abstract":"<p><p>The emergence of multidrug-resistant <i>Klebsiella pneumoniae</i> poses a significant challenge to clinical treatment and public health. Strategies combining antibiotics with FDA-approved non-antibiotic drugs have recently attracted attention as a promising approach to overcome antibiotic resistance. In this study, we systematically evaluated the synergistic effect of the antihistamine loratadine in combination with colistin against <i>K. pneumoniae</i>. Our results demonstrate that loratadine significantly restores the bactericidal activity of colistin against colistin-resistant <i>K. pneumoniae</i> both <i>in vitro</i> and <i>in vivo</i>, without increasing toxicity, while also delaying the development of colistin resistance. Mechanistic investigations using fluorescence-based assays and proteomic analysis revealed that loratadine acts as a potent adjuvant for colistin, effectively restoring its activity against colistin-resistant <i>K. pneumoniae</i> by interfering with lipid A modification. This phenomenon is further supported by the downregulation of lipid A-modifying enzyme-related protein EptB. In addition, the combination of loratadine and colistin disrupts the double-layer membrane barrier, leading to proton motive force (PMF) dysregulation, reduced intracellular ATP levels, and impaired efflux pump activity. Collectively, this study highlights the potential of drug repurposing as an effective strategy to combat antimicrobial resistance and provides a foundation for the development of combination therapies against multidrug-resistant pathogens.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":"15 1","pages":"2623697"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12903943/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146164763","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dual resistance to carbapenems and colistin in <i>Enterobacter</i>: Taiwan surveillance of antimicrobial resistance, 2010-2020.","authors":"Ying-Chi Huang, Tzu-Wen Huang, Praveen Rahi, Shu-Chen Kuo, Yan-Ru Chen, Chi-Tai Fang","doi":"10.1080/22221751.2026.2623693","DOIUrl":"10.1080/22221751.2026.2623693","url":null,"abstract":"<p><p>Extensively drug-resistant gram-negative bacteria harbouring dual resistance to carbapenems and colistin represent a critical global health threat. A total of 929 population-representative <i>Enterobacter</i> isolates were systematically collected from 29 hospitals across four regions of Taiwan between 2010 and 2020. Forty-one isolates (4.4%) were nonsusceptible to carbapenems and underwent whole-genome sequencing, resistance gene profiling, plasmid analysis, and antimicrobial susceptibility testing (AST). Among them, 35 isolates (85.4%) exhibited dual resistance to carbapenems and colistin; however, only half (17/35) were detectable by standard phenotypic AST. Colistin resistance was primarily mediated by activation of the chromosomal <i>arnBCADTEF</i> operon, which was frequently inducible and often undetected by standard testing, rather than by <i>mcr-9</i> or <i>mcr-10</i>. A conserved IncHI2 plasmid carrying <i>bla</i>_IMP-8 and <i>mcr-9</i> persisted and circulated across <i>Enterobacter</i> species for over a decade. Species-specific resistance patterns were observed: <i>E. roggenkampii</i> typically exhibited colistin resistance despite lacking carbapenemases, whereas <i>E. hormaechei</i> commonly carried <i>bla</i>_IMP-8 and occasionally lacked the <i>arn</i> operon. Both species exhibited comparable imipenem nonsusceptibility, complicating therapeutic decision-making. The convergence of carbapenem and colistin resistance in a substantial proportion of <i>Enterobacter</i> isolates at the population level makes this genus an emerging priority for hospital infection control and antimicrobial resistance surveillance. These findings underscore the urgent need for improved diagnostics, strengthened antimicrobial resistance surveillance, and optimized treatment strategies.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":"15 1","pages":"2623693"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12893162/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146149374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Post-mortem surveillance: an innovative strategy to detect and prevent spread of Nipah virus infection in humans.","authors":"Wasik Rahman Aquib, Dewan Imtiaz Rahman, Fawzia Akhtar Jahan, Nabila Nujhat Chowdhury, Sunanda Bosu, Fateha Akther Ema, Smita Sarker, Md Nazmul Sakib, Faruq Abdulla, Anika Farzin, Pronesh Dutta, Ariful Islam, Shah Jawad Bin Mahmood, Shadman Sakib Choudhury, Ayesha Siddika, Md Mahfuzur Rahman, Muhammad Rashedul Alam, Mintu Chowdhury, Md Sazzad Hossain, Tonmoy Sarkar, Kamal Ibne Amin Chowdhury, Mohammad Enayet Hossain, Sharmin Sultana, Ahmed Nawsher Alam, Mahbubur Rahman, Ariful Islam, John D Klena, Christina Spiropoulou, Mohammed Ziaur Rahman, Jonathan H Epstein, Sayera Banu, Emily S Gurley, Stephen P Luby, Joel M Montgomery, Tahmina Shirin, Syed Moinuddin Satter","doi":"10.1080/22221751.2026.2613510","DOIUrl":"10.1080/22221751.2026.2613510","url":null,"abstract":"<p><p>Nipah virus (NiV) remains a persistent public-health threat in Bangladesh. The national sentinel surveillance system has operated since 2006, yet fatal infections that occur before assessment often go untested. We piloted a post-mortem surveillance component at three sentinel hospitals (December 2023-April 2024). Trained anthropologists obtained written informed consent from the next of kin. Oral swabs were collected non-invasively shortly after death and tested for NiV RNA by qRT-PCR at the national reference laboratory, using standard controls and established protocols. Specimens were handled in BSL-2 plus conditions on site and transported in liquid-nitrogen dry shippers per national SOPs. Where indicated by epidemiologic risk, shipments were prioritized for rapid testing. Of 246 deceased individuals screened, 10 met the suspected NiV case definition and were enrolled; all died after admission. One decedent tested NiV-positive (Ct value of 27.3), which activated same-day outbreak investigation by IEDCR's National Rapid Response Team. Contacts (close contacts and one same-source exposed individual) were traced and tested (RT-qPCR/IgM acutely; IgG at 6 weeks); no secondary cases were detected. Operational timelines (death → enrolment → collection → testing) demonstrated that post-mortem sampling and confirmation can be completed rapidly within routine hospital workflows. Post-mortem oral-swab testing is feasible, acceptable, and operationally compatible with Bangladesh's national surveillance system. While not intended to improve detection among living patients, this non-invasive approach closes a critical gap by identifying previously untested fatal infections and providing a trigger for timely public-health response. Scaling this approach across sentinel sites could strengthen early detection and outbreak control in NiV-affected regions.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":"15 1","pages":"2613510"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12821353/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146003345","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"TOR3A represses type I interferon production and limits viral clearance during respiratory syncytial virus infection.","authors":"Xiaoping Li, Zhengrong Chen, Mengyun Wu, Peijie Zhu, Guodong Qiao, Jiaoyang Li, Yunfei Ye, Jiamin Cai, Ying Zhou, Xiaoqiu Dai, Yufeng Wang, Cancheng Li, Jiaqi Huang, Ji Zhou, Fei Xu, Chensheng Tan, Yu Shao, Xiu Gao, Jingjing Hu, Xuena Xu, Chunsheng Dong, Chuangli Hao, Yi Yang, Jinping Zhang","doi":"10.1080/22221751.2026.2637961","DOIUrl":"10.1080/22221751.2026.2637961","url":null,"abstract":"<p><p>Type I interferons (IFN-I) are essential for antiviral immunity, and precise regulation of IFN-I production is crucial to balance viral clearance and immunopathology. Here, we demonstrate that the interferon-stimulated gene <i>TOR3A</i> negatively regulates type I IFN signalling during respiratory syncytial virus (RSV) infection. <i>TOR3A</i> expression was upregulated in macrophages and RSV-infected patients, and its deficiency enhanced antiviral responses, leading to reduced viral load. Mechanistically, RSV infection induced <i>TOR3A</i> expression through the IFN-STAT1 pathway, which in turn suppressed IFN-I production. Furthermore, TOR3A recruited the E3 ubiquitin ligase STUB1 to mediate K48-linked ubiquitination and proteasomal degradation of RIG-I at lysine 146, thereby promoting RSV immune evasion. Our study identifies TOR3A as a novel suppressor of antiviral immunity and uncovers a mechanism by which RSV exploits host ISGs to dampen IFN-I responses, providing new insights into viral pathogenesis and potential therapeutic strategies.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":" ","pages":"2637961"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12990277/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147289884","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Receptor binding domain-independent pancoronavirus vaccine design by fusion of conserved T/B Epitopes.","authors":"Yunru Yang, Yetian Chen, Mengyu Hong, Ronghua Zou, Jingxue Yao, Entao Li, Jiayi Wang, Xiaodong Ye, Yixiang Xing, Yangming Tang, Xiaojie Lu, Chengchao Ding, Hongliang He, Dali Tong, Yuhua Shang, Jian Wang, Guangyu Zhao, Xiaoxue Huang, Fuli Feng, Qingyu Cheng, Bofeng Li, Baoying Huang, Wenjie Tan, Sandra Chiu, Tengchuan Jin","doi":"10.1080/22221751.2026.2631206","DOIUrl":"10.1080/22221751.2026.2631206","url":null,"abstract":"<p><p>The persistent emergence of SARS-CoV-2 variants continues to compromise current vaccine efficacy, driving the development of broad-spectrum coronavirus vaccines to address variant evasion and future outbreaks. To develop a pan-coronavirus vaccine, we identified some conserved T/B epitopes across spike proteins of human-infecting coronaviruses, focusing on two conserved long peptides, VV and VS, which demonstrated broad immunogenicity in PBMCs from COVID-19 convalescent patients. By structurally fusing the VV and VS long peptides with heptad repeat 1/2 (HR1/2) domains from the S2 subunit, we engineered a trimeric immunogen HR1-VV-HR2-VS. This design induced superior cellular and humoral immune responses compared to individual peptide components in immunized mice. The vaccine also significantly reduced viral loads and attenuated lung pathology in mice challenged with HCoV-229E, SARS-CoV-2 prototype strain, and the KP.2 variant, demonstrating cross-protective immunity. Therefore, these results indicated that HR1-VV-HR2-VS vaccine elicits cross-protective immunity, highlighting its potential as a universal coronavirus vaccine. In addition, we developed an innovative peptide vaccine platform based on the HR1-HR2 trimeric structural protein, which serves as a potent polypeptide fusion scaffold to significantly enhance peptide immunogenicity.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":" ","pages":"2631206"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12927409/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146164725","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A CRISPR activation screen identifies CH25H as a restriction factor against influenza viruses by targeting accessible cholesterol.","authors":"Jinyu Huang, Kaixiong Ma, Shiping Ding, Yunmeng Wang, Junlong Xiong, Jiahui Yi, Jiahao Zhang, Zhuoliang He, Lihong Huang, Xingxing Ren, Jiangtao Zhou, Xiaona Chen, Lele Liu, Wenbao Qi, Shaobo Wang, Ming Liao","doi":"10.1080/22221751.2026.2651464","DOIUrl":"10.1080/22221751.2026.2651464","url":null,"abstract":"<p><p>Influenza A viruses (IAVs) cause severe outbreaks with high mortality in birds and humans. A deeper understanding of cell-intrinsic defense mechanisms against influenza viruses is therefore crucial for developing novel antiviral strategies. Herein, we perform a genome-wide CRISPR activation screen to systematically elucidate host restriction factors against influenza A (H7N9) virus. Among multiple candidates, cholesterol 25-hydroxylase (CH25H) is shown to be induced by influenza virus infection and inhibit viral membrane fusion. Notably, our previous work demonstrated that CH25H blocks the entry of plasma membrane-fusing viruses such as coronaviruses. This inhibition occurs by relocating accessible cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER). Here, we extend this finding and show that the same mechanism works against endocytosis-dependent viruses such as influenza viruses. The exogenous supplementation of cholesterol can restore depleted accessible cholesterol and reverse the CH25H-mediated restriction. Additionally, we prove that acyl-CoA:cholesterol acyltransferase (ACAT) is required to recruit the accessible cholesterol in this process. However, how hydrophobic accessible cholesterol is transported remains unclear. Here, we demonstrate that GRAMD1/Aster-mediated non-vesicular cholesterol transport is utilized to mobilize accessible cholesterol upon stimulation of CH25H. 25-hydroxycholesterol (25HC), the catalytic product of CH25H, is a natural metabolite that potently inhibits influenza virus infection both <i>in vitro</i> and <i>in vivo</i>. These findings underscore the promising therapeutic potential of 25HC against influenza viruses.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":" ","pages":"2651464"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13215439/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147927521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The mouse-lethal H5N1 influenza virus carrying the PB2-384L/443R/460M characteristics acquired in avian hosts can effectively utilize human ANP32A/B proteins.","authors":"Weipeng Lin, Guohua Deng, Xin Xing, Jianzhong Shi, Huihui Kong, Liling Liu, Xianying Zeng, Li Jiang, Chengjun Li, Yuntao Guan, Pengfei Cui, Hualan Chen","doi":"10.1080/22221751.2026.2685917","DOIUrl":"10.1080/22221751.2026.2685917","url":null,"abstract":"<p><p>The species-specific acidic nuclear phosphoprotein 32 kDa members (ANP32A/B) play a key role in restricting the function of avian influenza virus polymerase in mammalian host. Avian influenza viruses, upon replicating in humans, may acquire critical amino acid substitutions in the polymerase basic 2 (PB2) protein (e.g. E627 K and D701N) that enhance the viral polymerase's functional compatibility with human ANP32A and ANP32B proteins, thereby augmenting viral replication efficiency and increasing pathogenic potential in humans. However, certain H5N1 avian influenza viruses have demonstrated the capacity to establish productive human infections in the absence of the canonical PB2-627 K or PB2-701N adaptive mutations; the underlying molecular mechanism remains incompletely characterized. In this study, we found that the two H5N1 viruses, namely A/chicken/LN/SD035/2018 (LN35) and A/duck/JL/S1261/2019 (JL261), were genetically similar, but their pathogenicity for mice was different. By evaluating a series of single-gene reassortant viruses and mutants in mice, we confirmed that the PB2-384L/443R/460M characteristics are crucial for LN35 to maintain high lethality in mice. We further revealed that the polymerase of H5N1 avian virus bearing PB2-384L/443R/460M signature could efficiently utilize human ANP32A/B. Moreover, we found that this PB2-384L/443R/460M signature positively regulates H5N1 vRNP-human ANP32A/B interaction and vRNP assembly. Our findings indicate that key amino acid substitutions in the PB2 gene of the H5N1 virus may emerge in avian host and then augment its capacity to interact with human ANP32A/B protein, underscoring the substantial zoonotic and public health risks associated with continued circulation and evolution of H5N1 in avian populations.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":" ","pages":"2685917"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13288910/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148162130","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Zoonotic <i>Bordetella bronchiseptica</i> infection at the swine-human interface: unveiling the evolutionary path from an animal to a human pathogen.","authors":"Junqi Liu, Xiaofeng Zheng, Chenghao Jia, Zhiliang Sun, Wangping Zhou, Jie Zhang, Yifeng Chen, Zijing Zhou, Yao Tian, Gang Xiao, Lifei Du, Chengming Fan, Leisheng Sun, Min Yue","doi":"10.1080/22221751.2026.2637286","DOIUrl":"10.1080/22221751.2026.2637286","url":null,"abstract":"<p><p><i>Bordetella bronchiseptica</i>, long regarded as a veterinary pathogen, is now emerging as a zoonotic threat to humans, particularly in immunocompromised individuals. We report a sentinel event involving a synchronized <i>B. bronchiseptica</i> outbreak in swine and their human caretaker, providing a unique opportunity to examine cross-species transmission and adaptation at the genomic level. Comparative genomics revealed that the human-adapted isolate (RL57) and its swine progenitor (XX35) share an identical chromosome, with XX35 harbouring an extra conjugative plasmid. Remarkably, RL57 did not simply lose this plasmid; instead, the entire plasmid was integrated into the chromosome via site-specific recombination. This integration allowed permanent retention of plasmid-encoded virulence and fitness genes, after which the plasmid was discarded to eliminate its replicative burden - a \"capture-and-discard\" mechanism of evolution. Following plasmid loss, the RL57 strain exhibited hypervirulence, faster growth, enhanced thermotolerance, and increased biofilm formation, indicating successful adaptation to the human host. Plasmid loss paradoxically rewired bacterial metabolism: sulfur assimilation and sulfonate utilization pathways were upregulated to fuel host adaptation. Strikingly, despite a collapse in transcription of specific metabolic modules, translational compensation maintained high protein levels, driving robust biofilm formation and thermal tolerance. These findings reveal a previously unrecognized evolutionary strategy in which plasmid integration followed by subsequent plasmid loss amplifies pathogenicity and host adaptability. Finally, we propose a One Health surveillance triad - metagenomic tracking of plasmid-chromosome dynamics, recombination hotspot screening, and metabolic shift monitoring - to proactively identify and mitigate such zoonotic events.</p>","PeriodicalId":11602,"journal":{"name":"Emerging Microbes & Infections","volume":" ","pages":"2637286"},"PeriodicalIF":7.0,"publicationDate":"2026-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12973838/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147270014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}