Pub Date : 2025-12-29DOI: 10.1038/s41564-025-02203-4
Alexander Perfilyev, Anastasiya Gæde, Steve Hooton, Sara A. Zahran, Panos G. Kalatzis, Caroline Sophie Winther-Have, Rodrigo Ibarra Chavez, Rachael C. Wilkinson, Anisha M. Thanki, Zhengjie Liu, Qing Zhang, Qianghua Lv, Yuqing Liu, Adriano M. Gigante, Robert J. Atterbury, Bent Petersen, Andrew D. Millard, Martha R. J. Clokie, Thomas Sicheritz-Pontén
Phages are typically classified as temperate, integrating into host genomes, or lytic, replicating and killing bacteria; for this reason, lytic phages are not expected in bacterial genome sequences. Here we analyse 3.6 million bacterial genome assemblies from 1,226 species and find 119,510 lytic phage genomes, which we term bacterial assembly-associated phage sequences. This represents a ~5-fold increase in the number of phages with associated hosts and raises questions about fundamental aspects of phage biology. Our analyses of bacterial assembly-associated phage sequences revealed previously undescribed phage clusters, including clusters distantly related to Salmonella Goslarviruses in Escherichia coli and Shigella, while also substantially expanding known genera such as Seoulvirus (from 16 to >300 members). Close relatives of lytic phages used therapeutically were also detected, suggesting clinical isolate sequencing unknowingly archives potential phage candidates. The discovery of complete, lytic phage genomes within bacterial assemblies challenges assumptions about the nature of the lytic lifestyle and reveals an untapped reservoir of phages. Diverse genomes of lytic phages are found in bacterial assemblies, challenging assumptions about the nature of the lytic lifestyle.
{"title":"Large-scale analysis of bacterial genomes reveals thousands of lytic phages","authors":"Alexander Perfilyev, Anastasiya Gæde, Steve Hooton, Sara A. Zahran, Panos G. Kalatzis, Caroline Sophie Winther-Have, Rodrigo Ibarra Chavez, Rachael C. Wilkinson, Anisha M. Thanki, Zhengjie Liu, Qing Zhang, Qianghua Lv, Yuqing Liu, Adriano M. Gigante, Robert J. Atterbury, Bent Petersen, Andrew D. Millard, Martha R. J. Clokie, Thomas Sicheritz-Pontén","doi":"10.1038/s41564-025-02203-4","DOIUrl":"10.1038/s41564-025-02203-4","url":null,"abstract":"Phages are typically classified as temperate, integrating into host genomes, or lytic, replicating and killing bacteria; for this reason, lytic phages are not expected in bacterial genome sequences. Here we analyse 3.6 million bacterial genome assemblies from 1,226 species and find 119,510 lytic phage genomes, which we term bacterial assembly-associated phage sequences. This represents a ~5-fold increase in the number of phages with associated hosts and raises questions about fundamental aspects of phage biology. Our analyses of bacterial assembly-associated phage sequences revealed previously undescribed phage clusters, including clusters distantly related to Salmonella Goslarviruses in Escherichia coli and Shigella, while also substantially expanding known genera such as Seoulvirus (from 16 to >300 members). Close relatives of lytic phages used therapeutically were also detected, suggesting clinical isolate sequencing unknowingly archives potential phage candidates. The discovery of complete, lytic phage genomes within bacterial assemblies challenges assumptions about the nature of the lytic lifestyle and reveals an untapped reservoir of phages. Diverse genomes of lytic phages are found in bacterial assemblies, challenging assumptions about the nature of the lytic lifestyle.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 1","pages":"42-52"},"PeriodicalIF":19.4,"publicationDate":"2025-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41564-025-02203-4.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145857394","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-23DOI: 10.1038/s41564-025-02189-z
Trinh Phan-Canh, Cristina Coman, Michaela Lackner, Nina Troppmair, Christoph Müller, Diana Cerbu, Saskia Seiser, Philipp Penninger, Irina Tsymala, Narakorn Khunweeraphong, Tamires Bitencourt, Andrej Knarr, Sabrina Jenull, Hossein Arzani, Lisa-Maria Zenz, Giuseppe Ianiri, Weiqiang Chen, Anuradha Chowdhary, Harry L. T. Mobley, Markus Hartl, Doris Moser, Robert Ahrends, Adelheid Elbe-Bürger, Karl Kuchler
The pronounced skin tropism and pan-antifungal resistance of Candida auris pose a serious global health threat. A key question in C. auris biology is how clinical isolates acquire amphotericin B resistance. Here we demonstrate that a carbonic sensing pathway (CSP) contributes to amphotericin B resistance by modulating mitochondrial energy functions in clinical C. auris isolates. Integrated transcriptomics and proteomics identify the carbonic anhydrase Nce103 and its transcription factors Rca1 and Efg1 as important regulatory components of the CSP. The conversion of CO2 into bicarbonate sustains energy metabolism required for colonization and fitness on human skin and in nutrient-limited microenvironments. We also show that bacterial skin colonizers engage urease to release CO2 that sustains C. auris fitness and skin colonization. These findings highlight therapeutic options to re-sensitize C. auris to antifungal treatments, as well as to prevent skin colonization by blocking the CSP. Candida auris can scavenge carbon dioxide from microenvironments through Nce103 to sustain fitness when colonizing human skin.
{"title":"Candida auris skin tropism and antifungal resistance are mediated by carbonic anhydrase Nce103","authors":"Trinh Phan-Canh, Cristina Coman, Michaela Lackner, Nina Troppmair, Christoph Müller, Diana Cerbu, Saskia Seiser, Philipp Penninger, Irina Tsymala, Narakorn Khunweeraphong, Tamires Bitencourt, Andrej Knarr, Sabrina Jenull, Hossein Arzani, Lisa-Maria Zenz, Giuseppe Ianiri, Weiqiang Chen, Anuradha Chowdhary, Harry L. T. Mobley, Markus Hartl, Doris Moser, Robert Ahrends, Adelheid Elbe-Bürger, Karl Kuchler","doi":"10.1038/s41564-025-02189-z","DOIUrl":"10.1038/s41564-025-02189-z","url":null,"abstract":"The pronounced skin tropism and pan-antifungal resistance of Candida auris pose a serious global health threat. A key question in C. auris biology is how clinical isolates acquire amphotericin B resistance. Here we demonstrate that a carbonic sensing pathway (CSP) contributes to amphotericin B resistance by modulating mitochondrial energy functions in clinical C. auris isolates. Integrated transcriptomics and proteomics identify the carbonic anhydrase Nce103 and its transcription factors Rca1 and Efg1 as important regulatory components of the CSP. The conversion of CO2 into bicarbonate sustains energy metabolism required for colonization and fitness on human skin and in nutrient-limited microenvironments. We also show that bacterial skin colonizers engage urease to release CO2 that sustains C. auris fitness and skin colonization. These findings highlight therapeutic options to re-sensitize C. auris to antifungal treatments, as well as to prevent skin colonization by blocking the CSP. Candida auris can scavenge carbon dioxide from microenvironments through Nce103 to sustain fitness when colonizing human skin.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 2","pages":"461-475"},"PeriodicalIF":19.4,"publicationDate":"2025-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41564-025-02189-z.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145808173","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-23DOI: 10.1038/s41564-025-02249-4
Shaobo Yang, Zongqi Wang, Chengyuan Fang, Mengdi Yang, Saleh Khawaled, Shanna Bonanno, Neel S Joshi, Yun Wei, Ke Zhang, Valeria Márquez-Pellegrin, Ming Guan, Songqi Zhang, Anna Clara Bader, Ningyuan Ye, Amber E Haley, Michael K Dame, Jason R Spence, Xuesong He, James G Fox, Ömer H Yilmaz, Yatrik M Shah, Rizwan Romee, Jiahe Li
{"title":"Publisher Correction: Surface expression of antitoxin on engineered bacteria neutralizes genotoxic colibactin in the gut.","authors":"Shaobo Yang, Zongqi Wang, Chengyuan Fang, Mengdi Yang, Saleh Khawaled, Shanna Bonanno, Neel S Joshi, Yun Wei, Ke Zhang, Valeria Márquez-Pellegrin, Ming Guan, Songqi Zhang, Anna Clara Bader, Ningyuan Ye, Amber E Haley, Michael K Dame, Jason R Spence, Xuesong He, James G Fox, Ömer H Yilmaz, Yatrik M Shah, Rizwan Romee, Jiahe Li","doi":"10.1038/s41564-025-02249-4","DOIUrl":"10.1038/s41564-025-02249-4","url":null,"abstract":"","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":" ","pages":""},"PeriodicalIF":19.4,"publicationDate":"2025-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145820383","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 : 2025-12-22DOI: 10.1038/s41564-025-02256-5
Chahat Mehra, Jesús Alvarado Valverde, Ana Margarida Nogueira Matias, Francesca Torelli, Tânia Catarina Medeiros, Julian Straub, James D. Asaki, Peter J. Bradley, Katja Luck, Steffen Lawo, Moritz Treeck, Lena Pernas
{"title":"Publisher Correction: Toxoplasma effector TgROP1 establishes membrane contact sites with the endoplasmic reticulum during infection","authors":"Chahat Mehra, Jesús Alvarado Valverde, Ana Margarida Nogueira Matias, Francesca Torelli, Tânia Catarina Medeiros, Julian Straub, James D. Asaki, Peter J. Bradley, Katja Luck, Steffen Lawo, Moritz Treeck, Lena Pernas","doi":"10.1038/s41564-025-02256-5","DOIUrl":"10.1038/s41564-025-02256-5","url":null,"abstract":"","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 2","pages":"610-610"},"PeriodicalIF":19.4,"publicationDate":"2025-12-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41564-025-02256-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145810689","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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. Plasmodium falciparum proteins were engineered to create a nanoparticle vaccine platform capable of displaying multiple antigens at 48 sites. Displaying a designed malaria circumsporozoite protein immunogen on this platform achieves full sterile protection in mice.
{"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":"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. Plasmodium falciparum proteins were engineered to create a nanoparticle vaccine platform capable of displaying multiple antigens at 48 sites. Displaying a designed malaria circumsporozoite protein immunogen on this platform achieves full sterile protection in mice.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 1","pages":"67-80"},"PeriodicalIF":19.4,"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/s41564-025-02230-1
Richard E. Lenski
Richard Lenski traces the legacy of Escherichia coli and how science is evolving to use this model organism in new ways.
理查德·伦斯基追溯了大肠杆菌的遗产，以及科学如何以新的方式利用这种模式生物。
{"title":"The changing roles of Escherichia coli","authors":"Richard E. Lenski","doi":"10.1038/s41564-025-02230-1","DOIUrl":"10.1038/s41564-025-02230-1","url":null,"abstract":"Richard Lenski traces the legacy of Escherichia coli and how science is evolving to use this model organism in new ways.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 1","pages":"2-3"},"PeriodicalIF":19.4,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145786266","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. Streptococcal S protein activates a peptidoglycan cell wall repair and modification complex to promote resistance of Streptococcus pneumoniae to lysozyme and LL-37, and increase virulence during infection.
{"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":"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. Streptococcal S protein activates a peptidoglycan cell wall repair and modification complex to promote resistance of Streptococcus pneumoniae to lysozyme and LL-37, and increase virulence during infection.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 1","pages":"282-300"},"PeriodicalIF":19.4,"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. S protein interacts with and activates PBP1a during cell division, as part of a larger GpsB-associated multiprotein complex that coordinates peptidoglycan remodelling in Streptococcus 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":"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. S protein interacts with and activates PBP1a during cell division, as part of a larger GpsB-associated multiprotein complex that coordinates peptidoglycan remodelling in Streptococcus pneumoniae.","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 1","pages":"301-316"},"PeriodicalIF":19.4,"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":"10.1038/s41564-025-02243-w","url":null,"abstract":"","PeriodicalId":18992,"journal":{"name":"Nature Microbiology","volume":"11 2","pages":"612-612"},"PeriodicalIF":19.4,"publicationDate":"2025-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41564-025-02243-w.pdf","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":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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