PLoS Pathogens最新文献

{"title":"Viral hijacking of host DDX60 promotes Crimean-Congo haemorrhagic fever virus replication via G-quadruplex unwinding.","authors":"Yutong Sui, Qi Xu, Mingsheng Liu, Xiaomei Liu, Xinpeng Liu, Yujie Wang, Xiangyuan Meng, Zinan Liu, Quanshun Li, Jinyu Liu","doi":"10.1371/journal.ppat.1013278","DOIUrl":"https://doi.org/10.1371/journal.ppat.1013278","url":null,"abstract":"<p><p>Crimean-Congo haemorrhagic fever virus (CCHFV) is the most prevalent tick-borne zoonotic bunyavirus, causing severe hemorrhagic fever and fatality in humans. Currently, the absence of approved vaccines or therapeutics for CCHFV infection necessitates the development of innovative therapeutic strategies. Here, we identify a guanine (G)-rich sequence located within the mRNA of the glycoprotein precursor in the medium (M) segment of the CCHFV genome, designated as M-PQS-1664(+). M-PQS-1664(+) can form stable G-quadruplex (G4) structure and functions as a negative regulatory element for viral replication. Host DDX60 is up-regulated in response to CCHFV infection, thereby it is hijacked to unwind M-PQS-1664(+) G4 for facilitating viral replication. The FDA-approved drug Cepharanthine (CEP), which competes with DDX60 to specifically stabilize M-PQS-1664(+) G4 without a global induction of host cellular G4s formation, exhibits remarkable antiviral activity in vitro and in vivo. More importantly, CEP possesses antiviral activity (50% inhibitory concentration ~ 0.2 μM) that having ~ 88 × the potency of ribavirin. Our findings underscore the CCHFV G4s as a promising target for drug development and highlight the significant potential of CEP in combating CCHFV.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013278"},"PeriodicalIF":5.5,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144512633","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Strain-specific galactose utilization by commensal E. coli mitigates Salmonella establishment in the gut.","authors":"Christopher Schubert, Jana Näf, Lisa Petukhov, Leanid Laganenka, Yassine Cherrak, Wolf-Dietrich Hardt","doi":"10.1371/journal.ppat.1013232","DOIUrl":"10.1371/journal.ppat.1013232","url":null,"abstract":"<p><p>Salmonella enterica serovar Typhimurium (S. Tm) is a major cause of gastrointestinal diseases worldwide. To date, options for prevention or curative therapy remain limited. The gut microbiota plays a protective role against enteric diseases, particularly in preventing establishment and proliferation of S. Tm. While most research has focused on microbiota-mediated pathogen exclusion during the later, inflammation-dominated stages of infection, little is known about how microbiota members mitigate S. Tm early gut colonization. To address this gap, we conducted 24 h in vivo competitive experiments using S. Tm and different commensal E. coli strains. We observed a significant reduction in pathogen load, which was strain-specific and particularly evident with E. coli 8178. To investigate the underlying molecular mechanisms, we performed an in vivo screen using a rationally designed S. Tm library-which includes a wide range of carbohydrate utilization mutants-both in the absence and presence of E. coli strains. Our findings revealed that E. coli 8178-mediated S. Tm competition was driven by the exploitation of galactose during the early stage of infection. Identifying galactose as a key metabolite in pathogen exclusion by gut microbiota members enhances our mechanistic understanding of microbiota-mediated protection and opens new avenues for developing microbiota- and dietary-based strategies to better control intestinal infections.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013232"},"PeriodicalIF":5.5,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12204579/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144512632","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Polysaccharide synthesis operon modulates Rickettsia-endothelial cell interactions.","authors":"Smruti Mishra, Luke Helminiak, Hwan Keun Kim","doi":"10.1371/journal.ppat.1013277","DOIUrl":"10.1371/journal.ppat.1013277","url":null,"abstract":"<p><p>Pathogenic Rickettsia species target vascular endothelial cells and cause systemic vasculitis. As obligate intracellular bacterial pathogens, Rickettsia must secure nutritional resources within the cytoplasm of endothelial cells while simultaneously subverting the innate immune defense system. With advances in rickettsial and host genetics, recent studies have identified novel molecular mechanisms involved in the complex interactions between Rickettsia and endothelial cells. However, it remains unclear how Rickettsia shields pathogen-derived immune stimulants, such as lipopolysaccharides (LPS) and peptidoglycan fragments, from immune recognition during intracellular replication. Prior work described two Rickettsia conorii variants with kkaebi transposon insertions in the polysaccharide synthesis operon (pso). Biochemical and immunological analyses revealed that pso is responsible for the biosynthesis of O-antigen (O-Ag) and the proper assembly of surface proteins. In the present work, we document that pso variant HK2 exhibits reduced capacities to adhere to and invade microvascular endothelial cells. Despite the low intracellular abundance, HK2 induced significantly higher levels of proinflammatory cytokines and chemokines, leading to premature cell death. Notably, HK2 exhibited defective intracellular survival in bone marrow-derived macrophages. This inability to dampen endothelial cell-mediated immune stimulation and resist macrophage-induced bactericidal activities resulted in the rapid elimination of viable Rickettsia in the mouse model of spotted fever. Further, when tested as a live-attenuated vaccine, HK2 elicited robust protective immunity against lethal spotted fever pathogenesis. Our work highlights the crucial role of pso in enabling Rickettsia to evade immune surveillance during intracellular replication within endothelial cells, ultimately delaying pathogen-induced programmed cell death and escaping immune defense mechanisms.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013277"},"PeriodicalIF":5.5,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12201665/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144508960","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Natural self-attenuation of pathogenic viruses by deleting the silencing suppressor coding sequence for long-term plant-virus coexistence.","authors":"Li Qin, Xiaoqing Wang, Zhaoji Dai, Wentao Shen, Fangfang Li, Aiming Wang, Adrián A Valli, Hongguang Cui","doi":"10.1371/journal.ppat.1013012","DOIUrl":"https://doi.org/10.1371/journal.ppat.1013012","url":null,"abstract":"<p><p>Potyviridae is the largest family of plant-infecting RNA viruses. All members of the family (potyvirids) have single-stranded positive-sense RNA genomes, with polyprotein processing as the expression strategy. The 5'-proximal regions of all potyvirids, except bymoviruses, encode two types of leader proteases: the serine protease P1 and the cysteine protease HCPro. However, their arrangement and sequence composition vary greatly among genera or even species. The leader proteases play multiple important roles in different potyvirid-host combinations, including RNA silencing suppression and virus transmission. Here, we report that viruses in the genus Arepavirus, which encode two HCPro leader proteases in tandem (HCPro1-HCPro2), can naturally lose the coding sequences for these two proteins during infection. Notably, this loss is associated with a shift in foliage symptoms from severe necrosis to mild chlorosis or even asymptomatic infections. Further analysis revealed that the deleted region is flanked by two short repeated sequences in the parental isolates, suggesting that recombination during virus replication likely drives this genomic deletion. Reverse genetic approaches confirmed that the loss of leader proteases weakens RNA silencing suppression and other critical functions. A field survey of areca palm trees displaying varied symptom severity identified a transitional stage in which full-length viruses and deletion mutants coexist in the same tree. Based on these findings, we propose a scenario in which full-length isolates drive robust infections and facilitate plant-to-plant transmission, eventually giving rise to leader protease-less variants that mitigate excessive damage to host trees, allowing long-term coexistence with the perennial host. To our knowledge, this is the first report of potyvirid self-attenuation via coding sequence loss.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013012"},"PeriodicalIF":5.5,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144508959","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tibetan PHD2D4E;C127S variant protects from viral diseases in hypoxia, but predispose to infections in normoxia via HIFα:IFN axis.","authors":"Riya Ghosh, Garima Joshi, Nishith M Shrimali, Kanchan Bhardwaj, Tsewang Chorol, Tashi Thinlas, Parvaiz A Koul, Josef T Prchal, Prasenjit Guchhait","doi":"10.1371/journal.ppat.1013296","DOIUrl":"https://doi.org/10.1371/journal.ppat.1013296","url":null,"abstract":"<p><p>We previously reported that Tibetan-specific variant of prolyl-hydroxylase-2 (PHD2)D4E;C127S protects highlanders from hypoxia-triggered pathologies by destabilizing hypoxia-inducible factor (HIF)-1α. Others have reported that stabilized HIF1α negatively regulates interferon (IFN)-regulating factor (IRF)-3 under hypoxia. We examined the role of PHD2D4E;C127S variant in IFN synthesis in immune cells during viral infections. Primary monocytes and cells engineered to express the PHD2D4E;C127S variant displayed protection against dengue virus (DENV)-2 infection by suppressing HIF1α, in turn promoting IRF-3 and IFNα/β synthesis in hypoxia (3% O2) in vitro. However, under normoxia (21% O2), these mutant cells increased reactive oxygen species (ROS) generation following DENV2 infection. Increased ROS then suppressed PHD2D4E;C127S activity, reflected by reduced hydroxylation and concomitant stabilization of HIF1α, resulting in suppressed IFN synthesis and higher DENV2 replication. The PHD2WT cells demonstrated the opposite trend. Our data further confirmed the inverse correlation between HIF1α and IFN pathways. CAY10585, an HIF1α-inhibitor, decreased the DENV2 infection by increasing IFN-A/B and IRF-3/7/9 expression. HIF1α-depleted monocytes also showed a similar response to the infection. We extended our findings to COVID-19 infection. The CD4/CD8 T-cells collected from Tibetans with PHD2D4E;C127S variant and exposed to SARS-CoV-2 infection showed elevated expression of IFN-γ in response to exposure to SARS-CoV-2 receptor-binding domain (RBD) peptide under hypoxia, and a lesser expression under normoxia. The study thus highlights a unique crosstalk of PHD2D4E;C127S variant with HIF1α-IFN axis under environmental pO2 in protecting or predisposing Tibetans to viral infections.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013296"},"PeriodicalIF":5.5,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144508961","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery of functional factorless internal ribosome entry site-like structures through virome mining.","authors":"Subash Chapagain, Nicolas Salcedo-Porras, Amir Abdolahzadeh, Yaohua Zhang, Higor Sette Pereira, Stephane Flibotte, Kevin Low, Christina Young, Yuhang Wu, Shao Wang, Soh Ishiguro, Nozomu Yachie, Trushar Patel, Artem Babaian, Eric Jan","doi":"10.1371/journal.ppat.1013255","DOIUrl":"https://doi.org/10.1371/journal.ppat.1013255","url":null,"abstract":"<p><p>All viruses must co-opt the host translational machinery for viral protein synthesis. The dicistrovirus intergenic region internal ribosome entry site (IGR-IRES) utilizes the most streamlined translation mechanism by adopting a triple pseudoknot structure that directly recruits and binds within the intersubunit space of the ribosome and initiates translation from a non-AUG codon. The origin of this unprecedented mechanism is not known. Using a bioinformatics pipeline to examine the diversity and function of IRESs across RNA viromes, we searched for IRES-like RNA structures using RNA covariance models for multiple IRES sub-types, and tested functional IRES by using a dual-fluorescent lentiviral library reporter screen. We identified over >4,700 dicistro-like genomes with ~32% containing putative IRES structures, including novel viral genome arrangements with multiple IRESs and IRESs embedded within open-reading frames (ORFs). Predicted IRESs bound directly to purified ribosomes and supported internal ribosome entry activity in vitro and in vivo. Moreover, internal IRESs embedded within an ORF of monocistronic genomes were functional and operated simultaneously to produce the downstream ORF. We also identified IRES-like structures within non-dicistrovirus viral genomes, including in the families Tombusviridae and Narnaviridae that bound to ribosomes directly and a subset can direct internal ribosome entry. This study provides a framework to map the origin of factorless IRES mechanisms and study the diverse viral strategies utilizing RNA-based mechanisms.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013255"},"PeriodicalIF":5.5,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144508957","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"IRF6 controls Epstein-Barr virus (EBV) lytic reactivation and differentiation in EBV-infected epithelial cells.","authors":"Stuart A Fogarty, Deo R Singh, Scott E Nelson, Maria E Calandranis, Yitao Zhang, Abigail S Pawelski, Alisha S Kansra, Sophie White, Shannon C Kenney","doi":"10.1371/journal.ppat.1013236","DOIUrl":"10.1371/journal.ppat.1013236","url":null,"abstract":"<p><p>Latent Epstein-Barr virus (EBV) infection promotes undifferentiated nasopharyngeal carcinoma (NPC) and gastric carcinoma (GC), while EBV infection of normal differentiated oropharyngeal epithelial cells is lytic and kills the cell. Establishment of viral latency within epithelial cells is likely essential for the development of EBV-induced NPCs and GCs, but the mechanism(s) by which EBV latency is maintained in epithelial cells are not fully understood. Here we demonstrate that the cellular tumor suppressor protein IRF6, a master regulator of squamous cell epithelial cell differentiation, plays a critical role in promoting TPA-induced lytic EBV reactivation in vitro in both EBV-infected NPC cells and EBV-infected GC cells. Using a telomerase-immortalized normal oral keratinocyte cell line (NOKs) model which retains the ability to differentiate in response to TPA treatment, we show that TPA-induced lytic EBV reactivation requires the PKCδ-RIPK4-IRF6 signaling pathway. RIPK4 is a PKCδ (PRKCD)-activated cellular S/T kinase that phosphorylates and activates the IRF6 transcription factor. We demonstrate that inhibition of PKCδ, RIPK4 or IRF6 expression is sufficient to suppress TPA-induced epithelial cell differentiation, as well as lytic EBV reactivation, in NOKs. Furthermore, we find that latent EBV infection in NOKs inhibits the expression of IRF6. Importantly, we show that inducible expression of a constitutively active (phospho-mimetic) IRF6 mutant is sufficient to activate the lytic form of EBV infection in both EBV-infected NOKs and EBV-infected SNU719 GC cells. Finally, we demonstrate that the ability of constitutively active IRF6 to promote lytic EBV infection in NOKs is at least partially mediated by IRF6-induced expression of the BLIMP1 transcription factor, which we previously showed synergistically activates expression of the two EBV immediate-early proteins, BZLF1 and BRLF1, in conjunction with KLF4. Thus, suppression of IRF6 expression may promote NPC and GC tumors by blocking lytic EBV reactivation and differentiation.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013236"},"PeriodicalIF":5.5,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12200665/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144508958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Direct and indirect pathways linking the Lon protease to motility behaviors in the pathogen Pseudomonas aeruginosa.","authors":"Aswathy Kallazhi, Anamika Rahman, Ute Römling, Kristina Jonas","doi":"10.1371/journal.ppat.1013288","DOIUrl":"https://doi.org/10.1371/journal.ppat.1013288","url":null,"abstract":"<p><p>The ATP-dependent cytoplasmic protease Lon has critical functions in protein quality control and cellular regulation in organisms across the three domains of life. In the opportunistic pathogen Pseudomonas aeruginosa, lon loss-of-function mutants exhibit multiple phenotypic defects in motility, virulence, antibiotic tolerance and biofilm formation. However, only a couple of native substrate proteins of Lon are described in P. aeruginosa until now and most of the phenotypes associated with Lon remain unexplained. Here, we searched for novel Lon substrates in P. aeruginosa by analyzing proteome-wide changes in protein levels and stabilities following lon overexpression. Our search yielded a large number of putative Lon substrates with diverse cellular functions, including metabolic enzymes, stress proteins and a significant fraction of motility-related proteins. In vitro degradation assays confirmed the metabolic protein SpeH, the heat shock protein IbpA as well as seven proteins involved in flagella- and type IV pilus-mediated motility as novel substrates of Lon. The new motility-associated substrates include both key regulators of motility (FliA, RpoN, AmrZ) as well as structural flagellar components (FliG, FliS and FlgE). Further, by isolating suppressor mutations bypassing the motility defect of lon- cells, we reveal that Lon-dependent degradation of the specific substrate SulA, a cell division inhibitor, is crucial for ensuring proper cell division and motility under optimal conditions. In sum, our work highlights Lon's regulatory role in degrading functional proteins involved in critical cellular processes and contributes to a better molecular understanding of the pathways underlying Pseudomonas pathogenicity.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013288"},"PeriodicalIF":5.5,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144498807","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A comprehensive phylogeny of mammalian PRNP gene reveals no influence of prion misfolding propensity on the evolution of this gene.","authors":"Cristina Sampedro-Torres-Quevedo, Hasier Eraña, Jorge M Charco, Carlos M Díaz-Domínguez, Maitena San-Juan-Ansoleaga, Eva Fernández-Muñoz, Nuno Gonçalves-Anjo, Josu Galarza-Ahumada, Ana R Cortazar, Roberto F Nespolo, Julian F Quintero-Galvis, Africa Manero-Azua, Diego Polanco-Alonso, Adrián Gaite-Reguero, Íñigo Olalde, Urko M Marigorta, Guiomar Perez de Nanclares, Ana M Aransay, Joaquín Castilla","doi":"10.1371/journal.ppat.1013257","DOIUrl":"https://doi.org/10.1371/journal.ppat.1013257","url":null,"abstract":"<p><p>Prion diseases are invariably fatal neurodegenerative diseases that affect some mammalian species, including humans. These diseases are caused by the misfolding of the cellular prion protein (PrPC) into a pathologic isoform (PrPSc). The prion protein is highly conserved across mammals. However, some species present lower susceptibility to prion diseases than others. This behavior is likely explained by the resistance of these animal species' prion proteins to acquire a pathological conformation. Therefore, the tertiary structure and interspecific variations encoded in the primary structure determine a PrP proneness to misfolding. For this reason, we studied the PRNP gene from a phylogenetic perspective, potentially unveiling evolutionary events related to prion diseases. We generated a database of mammalian PRNP sequences and constructed phylogenetic trees based on nucleotide sequence variations. We aligned 1146 PRNP gene sequences from 900 different mammalian species and built a PRNP gene-based phylogenetic tree. Classical phylogenetic orders tend to maintain their clustering in the PRNP gene tree. Nonetheless, the few differences found may shed some light on potential evolutionary constraints posed by prion disorders. Moreover, this phylogenetic study was combined with an in vitro misfolding study. Protein Misfolding Shaking Amplification (PMSA) was used to evaluate the tendency of many of these proteins to misfold. This comprehensive analysis spanned a wide range of mammalian prion protein sequences and included analysis of different variants with a focus on the human rs1799990 locus (c.385A > G, p.Met129Val). This variant, widely linked to prion disease susceptibility in humans, is explored in the context of its evolutionary origins. All in all, our PRNP gene-based tree, despite showing some topological differences with the reference species tree that could be in some cases related to prion disease susceptibility, is not significantly distinct. Indicating that the proneness of a PrP variant to misfold spontaneously has not shaped the evolution of this gene.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013257"},"PeriodicalIF":5.5,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144498806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Infectome analysis of bat kidneys from Yunnan province, China, reveals novel henipaviruses related to Hendra and Nipah viruses and prevalent bacterial and eukaryotic microbes.","authors":"Guopeng Kuang, Tian Yang, Weihong Yang, Jing Wang, Hong Pan, Yuanfei Pan, Qin-Yu Gou, Wei-Chen Wu, Juan Wang, Lifeng Yang, Xi Han, Yao-Qing Chen, John-Sebastian Eden, Edward C Holmes, Mang Shi, Yun Feng","doi":"10.1371/journal.ppat.1013235","DOIUrl":"10.1371/journal.ppat.1013235","url":null,"abstract":"<p><p>Bats are natural reservoirs for a wide range of microorganisms, including many notable zoonotic pathogens. However, the composition of the infectome (i.e., the collection of viral, bacterial and eukaryotic microorganisms) within bat kidneys remains poorly understood. To address this gap, we performed meta-transcriptomic sequencing on kidney tissues from 142 bats, spanning ten species sampled at five locations in Yunnan province, China. This analysis identified 22 viral species, including 20 novel viruses, two of which represented newly discovered henipaviruses closely related to the highly pathogenic Hendra and Nipah viruses. These henipaviruses were found in the kidneys of bats inhabiting an orchard near villages, raising concerns about potential fruit contamination via bat urine and transmission risks to livestock or humans. Additionally, we identified a novel protozoan parasite, tentatively named Klossiella yunnanensis, along with two highly abundant bacterial species, one of which is a newly discovered species-Flavobacterium yunnanensis. These findings broaden our understanding of the bat kidney infectome, underscore critical zoonotic threats, and highlight the need for comprehensive, full-spectrum microbial analyses of previously understudied organs to better assess spillover risks from bat populations.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013235"},"PeriodicalIF":5.5,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12187171/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144486750","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}