Pub Date : 2025-12-19DOI: 10.1038/s41564-025-02209-y
Dashuang Shi,Rui Ma,Richi Gupta,Thayne H Dickey,Palak N Patel,Nichole D Salinas,Wai Kwan Tang,Alaysies Queen,Myesha Singleton,Nida Delbe,Solomon Conteh,Lynn E Lambert,Patrick E Duffy,Niraj H Tolia
Protein nanoparticles in infectious disease vaccines enable protection through the periodic arrangement of antigens on their surface. These nanoparticles arise from organisms unrelated to the target disease, limiting their role as presentation platforms. Nanoparticles may also be compromised by pre-existing immunity to the nanoparticle carrier and may induce autoimmunity if conserved epitopes exist. Here we developed a potent multivalent malaria vaccine using an engineered Plasmodium falciparum pyridoxal 5'-phosphate (PLP) synthase as a nanoparticle that presents a designed P. falciparum circumsporozoite protein (CSP) and the Plasmodium vivax cell-transversal protein for ookinetes and sporozoites (CelTOS). These engineered vaccines elicited high titres of anti-CSP and anti-CelTOS antibodies, and three doses provided complete sterile protection against malaria in a mouse model. Cryogenic electron microscopy resolved a 2.95-Å resolution structure of the PLP nanoparticle including amino acid changes engineered to stabilize the nanoparticle. PLP synthase has no identifiable human ortholog limiting its propensity for autoimmunity or pre-existing immunity, and the engineered nanoparticles possess desirable manufacturing characteristics. These studies established an effective nanoparticle platform for malaria and infectious disease vaccines.
{"title":"A Plasmodium-derived nanoparticle vaccine elicits sterile protection against malaria in mice.","authors":"Dashuang Shi,Rui Ma,Richi Gupta,Thayne H Dickey,Palak N Patel,Nichole D Salinas,Wai Kwan Tang,Alaysies Queen,Myesha Singleton,Nida Delbe,Solomon Conteh,Lynn E Lambert,Patrick E Duffy,Niraj H Tolia","doi":"10.1038/s41564-025-02209-y","DOIUrl":"https://doi.org/10.1038/s41564-025-02209-y","url":null,"abstract":"Protein nanoparticles in infectious disease vaccines enable protection through the periodic arrangement of antigens on their surface. These nanoparticles arise from organisms unrelated to the target disease, limiting their role as presentation platforms. Nanoparticles may also be compromised by pre-existing immunity to the nanoparticle carrier and may induce autoimmunity if conserved epitopes exist. Here we developed a potent multivalent malaria vaccine using an engineered Plasmodium falciparum pyridoxal 5'-phosphate (PLP) synthase as a nanoparticle that presents a designed P. falciparum circumsporozoite protein (CSP) and the Plasmodium vivax cell-transversal protein for ookinetes and sporozoites (CelTOS). These engineered vaccines elicited high titres of anti-CSP and anti-CelTOS antibodies, and three doses provided complete sterile protection against malaria in a mouse model. Cryogenic electron microscopy resolved a 2.95-Å resolution structure of the PLP nanoparticle including amino acid changes engineered to stabilize the nanoparticle. PLP synthase has no identifiable human ortholog limiting its propensity for autoimmunity or pre-existing immunity, and the engineered nanoparticles possess desirable manufacturing characteristics. These studies established an effective nanoparticle platform for malaria and infectious disease vaccines.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"180 1","pages":""},"PeriodicalIF":28.3,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145786267","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-19DOI: 10.1038/s41564-025-02184-4
Jessica Burnier,Clement Gallay,Kevin E Bruce,Elisabet Bjånes,Louise Martin,Kin Ki Jim,Ho-Ching Tiffany Tsui,Amelieke J H Cremers,Johann Mignolet,Daniela Vollmer,Jacob Biboy,Victor Nizet,Waldemar Vollmer,Malcolm E Winkler,Jan-Willem Veening
S protein is conserved among streptococci and contributes to group A Streptococcus virulence, but the mechanisms involved are unclear. Here we used genetic, biochemical, single-molecule, in vitro and in vivo analyses to show that S protein is crucial for resistance against host-derived antimicrobials by coordinating cell wall modification and repair. We observed that S protein was localized to the streptococcal septum dependent on its transmembrane domain, while S protein function was dependent on its peptidoglycan (PG)-binding LysM domain. Direct interactions between the pneumococcal S protein and the PG synthase PBP1a as well as the PG deacetylase PgdA were detected. Loss of S protein reduced the proportion of circumferentially moving PBP1a molecules, altered streptococcal morphology and increased susceptibility to cell-wall-targeting antibiotics, suggesting that S protein activates PBP1a. Streptococcus pneumoniae ess mutants lacking the gene encoding S protein were more susceptible to human antimicrobial peptide LL-37 and lysozyme, while their virulence was decreased compared with wild-type bacteria in zebrafish and mice. These data suggest that S protein activates the PG repair and modification complex, providing defence against host-derived and environmental antimicrobials.
{"title":"Pneumococcal S protein coordinates cell wall modification and repair to resist host antimicrobials.","authors":"Jessica Burnier,Clement Gallay,Kevin E Bruce,Elisabet Bjånes,Louise Martin,Kin Ki Jim,Ho-Ching Tiffany Tsui,Amelieke J H Cremers,Johann Mignolet,Daniela Vollmer,Jacob Biboy,Victor Nizet,Waldemar Vollmer,Malcolm E Winkler,Jan-Willem Veening","doi":"10.1038/s41564-025-02184-4","DOIUrl":"https://doi.org/10.1038/s41564-025-02184-4","url":null,"abstract":"S protein is conserved among streptococci and contributes to group A Streptococcus virulence, but the mechanisms involved are unclear. Here we used genetic, biochemical, single-molecule, in vitro and in vivo analyses to show that S protein is crucial for resistance against host-derived antimicrobials by coordinating cell wall modification and repair. We observed that S protein was localized to the streptococcal septum dependent on its transmembrane domain, while S protein function was dependent on its peptidoglycan (PG)-binding LysM domain. Direct interactions between the pneumococcal S protein and the PG synthase PBP1a as well as the PG deacetylase PgdA were detected. Loss of S protein reduced the proportion of circumferentially moving PBP1a molecules, altered streptococcal morphology and increased susceptibility to cell-wall-targeting antibiotics, suggesting that S protein activates PBP1a. Streptococcus pneumoniae ess mutants lacking the gene encoding S protein were more susceptible to human antimicrobial peptide LL-37 and lysozyme, while their virulence was decreased compared with wild-type bacteria in zebrafish and mice. These data suggest that S protein activates the PG repair and modification complex, providing defence against host-derived and environmental antimicrobials.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"30 1","pages":""},"PeriodicalIF":28.3,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145786265","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-19DOI: 10.1038/s41564-025-02210-5
Hugo Millat,Cassandra Falcou,Cassandra Lenoir,Nicholas S Briggs,Jack Stone,Pierre Simon Garcia,Sylvie Manuse,Caroline Cluzel,André Zapun,Cécile Morlot,David I Roper,Adrien Ducret,Christophe Grangeasse
Class A penicillin-binding proteins (aPBPs) are involved in the biosynthesis and remodelling of peptidoglycan (PG). The human bacterial pathogen Streptococcus pneumoniae produces three aPBPs, which are regulated to maintain the bacterium's ovoid shape. Evidence suggests that PBP1a and PBP2a activities are closely coordinated; however, their precise functions remain unclear. Here we characterized the pneumococcal S protein, which contains a LysM-PG-binding domain and a GpsB-interacting domain. Using S protein fusion constructs or mutant bacterial strains, we show that S protein localizes to the division ring and is required to prevent premature cell lysis and minicell formation due to aberrant division site placement. S protein interacts with PBP1a and activates its PG synthesis activity. Co-immunoprecipitation experiments combined with biochemical, genetic, structural prediction and microscopy analyses suggest that S protein is part of a larger multiprotein complex containing aPBPs and PG-modifying enzymes, and coordinated by the scaffolding protein GpsB. Together, these findings suggest that a GpsB-associated complex orchestrates PG biosynthesis and remodelling in S. pneumoniae.
{"title":"Streptococcus pneumoniae S protein activates PBP1a to regulate peptidoglycan remodelling and cell division.","authors":"Hugo Millat,Cassandra Falcou,Cassandra Lenoir,Nicholas S Briggs,Jack Stone,Pierre Simon Garcia,Sylvie Manuse,Caroline Cluzel,André Zapun,Cécile Morlot,David I Roper,Adrien Ducret,Christophe Grangeasse","doi":"10.1038/s41564-025-02210-5","DOIUrl":"https://doi.org/10.1038/s41564-025-02210-5","url":null,"abstract":"Class A penicillin-binding proteins (aPBPs) are involved in the biosynthesis and remodelling of peptidoglycan (PG). The human bacterial pathogen Streptococcus pneumoniae produces three aPBPs, which are regulated to maintain the bacterium's ovoid shape. Evidence suggests that PBP1a and PBP2a activities are closely coordinated; however, their precise functions remain unclear. Here we characterized the pneumococcal S protein, which contains a LysM-PG-binding domain and a GpsB-interacting domain. Using S protein fusion constructs or mutant bacterial strains, we show that S protein localizes to the division ring and is required to prevent premature cell lysis and minicell formation due to aberrant division site placement. S protein interacts with PBP1a and activates its PG synthesis activity. Co-immunoprecipitation experiments combined with biochemical, genetic, structural prediction and microscopy analyses suggest that S protein is part of a larger multiprotein complex containing aPBPs and PG-modifying enzymes, and coordinated by the scaffolding protein GpsB. Together, these findings suggest that a GpsB-associated complex orchestrates PG biosynthesis and remodelling in S. pneumoniae.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"29 1","pages":""},"PeriodicalIF":28.3,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145786402","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-16DOI: 10.1038/s41564-025-02243-w
Seyed Davoud Jazayeri, Lisa Borkner, Caroline E Sutton, Kingston H G Mills
{"title":"Author Correction: Respiratory immunization using antibiotic-inactivated Bordetella pertussis confers T cell-mediated protection against nasal infection in mice.","authors":"Seyed Davoud Jazayeri, Lisa Borkner, Caroline E Sutton, Kingston H G Mills","doi":"10.1038/s41564-025-02243-w","DOIUrl":"https://doi.org/10.1038/s41564-025-02243-w","url":null,"abstract":"","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":" ","pages":""},"PeriodicalIF":19.4,"publicationDate":"2025-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145768636","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-15DOI: 10.1038/s41564-025-02242-x
Alaina R Weinheimer, Julia M Brown, Brian Thompson, Greta Leonaviciene, Vaidotas Kiseliovas, Simonas Jocys, Jacob Munson-McGee, Gregory Gavelis, Corianna Mascena, Linas Mazutis, Nicole J Poulton, Rapolas Zilionis, Ramunas Stepanauskas
{"title":"Author Correction: Single-particle genomics uncovers abundant non-canonical marine viruses from nanolitre volumes.","authors":"Alaina R Weinheimer, Julia M Brown, Brian Thompson, Greta Leonaviciene, Vaidotas Kiseliovas, Simonas Jocys, Jacob Munson-McGee, Gregory Gavelis, Corianna Mascena, Linas Mazutis, Nicole J Poulton, Rapolas Zilionis, Ramunas Stepanauskas","doi":"10.1038/s41564-025-02242-x","DOIUrl":"https://doi.org/10.1038/s41564-025-02242-x","url":null,"abstract":"","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":" ","pages":""},"PeriodicalIF":19.4,"publicationDate":"2025-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145763418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Proliferation of the emerging zoonotic pathogen Streptococcus equi subsp. zooepidemicus in the meninges is linked to mortality in pigs and morbidity in humans. The mechanisms underlying the remarkable capacity of hypervirulent S. zooepidemicus to proliferate in cerebrospinal fluid (CSF) are largely undefined. Here, using genetically barcoded S. zooepidemicus, we found that following systemic infection of mice, only ~1–10 S. zooepidemicus clones invade the meninges where they subsequently replicate ~107-fold. Subsequent transposon insertion sequencing experiments, plus validation work with bacterial mannose phosphotransferase system (PTSman)-defective strains, identified the PTSman, which imports glucose, as essential for S. zooepidemicus proliferation in CSF. The S. zooepidemicus PTSman promoter confers species-specific constitutive transcription of PTSman, enabling glucose acquisition at low glucose concentrations and limiting activation of the stringent response, leading to pathogen replication in CSF. Our findings reveal how the rewiring of PTSman in the control of S. zooepidemicus metabolism enables this pathogen to adapt to and replicate in CSF during meningitis.
{"title":"Zoonotic Streptococcus imports glucose to inhibit stringent response and promote growth during meningitis","authors":"Chen Yuan, Karthik Hullahalli, Hao Huang, Siqi Zhao, Wenqing Wang, Xingyu Tian, Xin Li, Linya Xia, Yuchang Wang, Fei Pan, Ying Liang, Yurui Xie, Yue Li, Hongjie Fan, Matthew K. Waldor, Zhe Ma","doi":"10.1038/s41564-025-02194-2","DOIUrl":"https://doi.org/10.1038/s41564-025-02194-2","url":null,"abstract":"Proliferation of the emerging zoonotic pathogen Streptococcus equi subsp. zooepidemicus in the meninges is linked to mortality in pigs and morbidity in humans. The mechanisms underlying the remarkable capacity of hypervirulent S. zooepidemicus to proliferate in cerebrospinal fluid (CSF) are largely undefined. Here, using genetically barcoded S. zooepidemicus, we found that following systemic infection of mice, only ~1–10 S. zooepidemicus clones invade the meninges where they subsequently replicate ~107-fold. Subsequent transposon insertion sequencing experiments, plus validation work with bacterial mannose phosphotransferase system (PTSman)-defective strains, identified the PTSman, which imports glucose, as essential for S. zooepidemicus proliferation in CSF. The S. zooepidemicus PTSman promoter confers species-specific constitutive transcription of PTSman, enabling glucose acquisition at low glucose concentrations and limiting activation of the stringent response, leading to pathogen replication in CSF. Our findings reveal how the rewiring of PTSman in the control of S. zooepidemicus metabolism enables this pathogen to adapt to and replicate in CSF during meningitis.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"150 1","pages":""},"PeriodicalIF":28.3,"publicationDate":"2025-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145759745","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The innate immune response involves interferons (IFNs), antiviral cytokines that upregulate numerous IFN-stimulated genes, many of which have uncharacterized functions and mechanisms. Here we performed transcriptomic profiling of lung tissues from wild-type and IFNAR-/- mice infected with SARS-CoV-2 and single-cell RNA sequencing of bronchoalveolar lavage fluid and peripheral blood mononuclear cells from patients with COVID-19. We identified O-GalNAc transferase 2 (GALNT2), an N-acetylgalactosaminyltransferase, as an antiviral IFN-stimulated gene restricting the replication of multiple coronaviruses and influenza A viruses in vitro and in vivo, contributing to viral clearance and reducing disease severity. Mechanistically, GALNT2-dependent O-linked glycosylation may regulate viral glycoprotein proteolytic processing and impair viral growth by blocking virus-cell fusion. In addition, we found that serine residues at 810/813 in the viral spike protein undergo O-glycosylation and function as the primary genetic determinants of sensitivity or evasion towards GALNT2. Human genetic data analysis revealed that individuals with GALNT2 variants that lost antiviral function had elevated risk of hospitalization following SARS-CoV-2 infection. This study establishes GALNT2 as an antiviral factor against some respiratory virus infections.
{"title":"Interferon-stimulated gene GALNT2 restricts respiratory virus infections.","authors":"Wei Ran,Jinghong Yang,Shi Yu,Qingtao Hu,Yuqi He,Shengjun Wang,Cheng Wei,Jing Sun,Airu Zhu,Fang Li,Lu Zhang,Pengfei Li,Huina Hu,Ruangang Pan,Yanying Yu,Yanqiu Yuan,Lingyu Sun,Yanqun Wang,Zhaoyong Zhang,Zhao Chen,Donglan Liu,Qihong Yan,Dong Wang,Kuai Yu,Yiliang Wang,Jianfen Zhuo,Zhen Zhuang,Hua Tao,Qiuhui Zeng,Kaixin Zhou,Fenghua Chen,Wenxuan Tang,Yuzheng Zhou,Rong Bai,Yonghao Xu,Na Li,Jun Dai,Hongyu Zhao,Jung-Eun Park,Tao Wang,Qiang Ding,Stanley Perlman,Jingxian Zhao,Yang Mao,Shaobo Wang,Jincun Zhao","doi":"10.1038/s41564-025-02200-7","DOIUrl":"https://doi.org/10.1038/s41564-025-02200-7","url":null,"abstract":"The innate immune response involves interferons (IFNs), antiviral cytokines that upregulate numerous IFN-stimulated genes, many of which have uncharacterized functions and mechanisms. Here we performed transcriptomic profiling of lung tissues from wild-type and IFNAR-/- mice infected with SARS-CoV-2 and single-cell RNA sequencing of bronchoalveolar lavage fluid and peripheral blood mononuclear cells from patients with COVID-19. We identified O-GalNAc transferase 2 (GALNT2), an N-acetylgalactosaminyltransferase, as an antiviral IFN-stimulated gene restricting the replication of multiple coronaviruses and influenza A viruses in vitro and in vivo, contributing to viral clearance and reducing disease severity. Mechanistically, GALNT2-dependent O-linked glycosylation may regulate viral glycoprotein proteolytic processing and impair viral growth by blocking virus-cell fusion. In addition, we found that serine residues at 810/813 in the viral spike protein undergo O-glycosylation and function as the primary genetic determinants of sensitivity or evasion towards GALNT2. Human genetic data analysis revealed that individuals with GALNT2 variants that lost antiviral function had elevated risk of hospitalization following SARS-CoV-2 infection. This study establishes GALNT2 as an antiviral factor against some respiratory virus infections.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"13 1","pages":""},"PeriodicalIF":28.3,"publicationDate":"2025-12-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145732578","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-12DOI: 10.1038/s41564-025-02198-y
Ricardo Fróis-Martins,Kontxi Martinez de San Vicente,Corinne Maufrais,Sarah Mertens,Natacha Sertour,Emilie Sitterlé,Marie-Elisabeth Bougnoux,Christophe d'Enfert,Salomé LeibundGut-Landmann
Candida albicans is a common resident of the microbiota that supports host homeostasis but can cause disease when immune defences are impaired. Mucocutaneous candidiasis in individuals with IL-17 immune defects provides insights into the immune system's role in controlling C. albicans. Here, using a murine model of oral colonization, we show that IL-17 signalling maintains C. albicans in a non-pathogenic state. Loss of IL-17 leads to fungal filamentation and upregulation of hyphae-associated genes, which is accompanied by epithelial barrier disruption and inflammation, linked to aberrant IL-22 and IL-13 production. The emergence of pathogenic fungal traits was associated with impaired zinc chelation due to reduced calprotectin expression in the IL-17-deficient mice. Prolonged exposure to the immune-dysregulated tissue led to selection of stable, damage-inducing C. albicans variants, mirroring the evolution of isolates from a chronic mucocutaneous candidiasis patient. These findings reveal how IL-17 protects against fungal pathogenicity and how immune dysfunction fosters C. albicans adaptation and diversification within the host.
{"title":"IL-17-mediated antifungal immunity restricts Candida albicans pathogenicity in the oral cavity.","authors":"Ricardo Fróis-Martins,Kontxi Martinez de San Vicente,Corinne Maufrais,Sarah Mertens,Natacha Sertour,Emilie Sitterlé,Marie-Elisabeth Bougnoux,Christophe d'Enfert,Salomé LeibundGut-Landmann","doi":"10.1038/s41564-025-02198-y","DOIUrl":"https://doi.org/10.1038/s41564-025-02198-y","url":null,"abstract":"Candida albicans is a common resident of the microbiota that supports host homeostasis but can cause disease when immune defences are impaired. Mucocutaneous candidiasis in individuals with IL-17 immune defects provides insights into the immune system's role in controlling C. albicans. Here, using a murine model of oral colonization, we show that IL-17 signalling maintains C. albicans in a non-pathogenic state. Loss of IL-17 leads to fungal filamentation and upregulation of hyphae-associated genes, which is accompanied by epithelial barrier disruption and inflammation, linked to aberrant IL-22 and IL-13 production. The emergence of pathogenic fungal traits was associated with impaired zinc chelation due to reduced calprotectin expression in the IL-17-deficient mice. Prolonged exposure to the immune-dysregulated tissue led to selection of stable, damage-inducing C. albicans variants, mirroring the evolution of isolates from a chronic mucocutaneous candidiasis patient. These findings reveal how IL-17 protects against fungal pathogenicity and how immune dysfunction fosters C. albicans adaptation and diversification within the host.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"231 1","pages":""},"PeriodicalIF":28.3,"publicationDate":"2025-12-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145732579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-10DOI: 10.1038/s41564-025-02199-x
James C. Kosmopoulos, William Pallier, Ashish A. Malik, Karthik Anantharaman
Peatlands hold up to one-third of Earth’s soil carbon but are increasingly turning from being carbon sinks to becoming carbon sources due to human impacts. Restoration efforts aim to reverse this trend, but viral influences on peatland recovery remain unclear, despite viruses being potent regulators of microbiomes and ecosystem function. Here we sequenced soil metagenomes to study viral communities across seven UK peatlands, each encompassing areas representing three peatland ecosystem health statuses: natural, damaged and restored. We found that viral diversity and community structure were shaped by both geography and ecosystem health. Viruses were geographically widespread, yet exhibited ecosystem health-specific endemism and functional adaptation, highlighting their sensitivity to restoration. Virus–host dynamics ranged from stable ‘piggyback-the-winner’ relationships to decoupled dynamics in those infecting keystone aerobes, sulfate reducers, carbohydrate degraders and fermenters. These findings position viruses as dynamic drivers of peatland ecosystem recovery and could unlock pathways to bolster carbon retention and accelerate climate mitigation.
{"title":"Ecosystem health shapes viral ecology in peatland soils","authors":"James C. Kosmopoulos, William Pallier, Ashish A. Malik, Karthik Anantharaman","doi":"10.1038/s41564-025-02199-x","DOIUrl":"https://doi.org/10.1038/s41564-025-02199-x","url":null,"abstract":"Peatlands hold up to one-third of Earth’s soil carbon but are increasingly turning from being carbon sinks to becoming carbon sources due to human impacts. Restoration efforts aim to reverse this trend, but viral influences on peatland recovery remain unclear, despite viruses being potent regulators of microbiomes and ecosystem function. Here we sequenced soil metagenomes to study viral communities across seven UK peatlands, each encompassing areas representing three peatland ecosystem health statuses: natural, damaged and restored. We found that viral diversity and community structure were shaped by both geography and ecosystem health. Viruses were geographically widespread, yet exhibited ecosystem health-specific endemism and functional adaptation, highlighting their sensitivity to restoration. Virus–host dynamics ranged from stable ‘piggyback-the-winner’ relationships to decoupled dynamics in those infecting keystone aerobes, sulfate reducers, carbohydrate degraders and fermenters. These findings position viruses as dynamic drivers of peatland ecosystem recovery and could unlock pathways to bolster carbon retention and accelerate climate mitigation.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"6 1","pages":""},"PeriodicalIF":28.3,"publicationDate":"2025-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145711541","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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