Journal of Bacteriology最新文献

{"title":"Regulation of bacterial virulence genes by PecS family transcription factors","authors":"George C. NwokochaArpita GhoshAnne Grove1Corteva Agriscience, Johnston, Iowa, USA2Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana, USAGeorge O'Toole","doi":"10.1128/jb.00302-24","DOIUrl":"https://doi.org/10.1128/jb.00302-24","url":null,"abstract":"Journal of Bacteriology, Ahead of Print. <br/>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142267973","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In vivo and in vitro analyses of the role of the Prc protease in inducing mucoidy in Pseudomonas aeruginosa","authors":"Alexis G. SommerfieldMichelle WangJulia MamanaAndrew J. Darwin1Department of Microbiology, NYU Grossman School of Medicine, New York, New York, USAJoseph Bondy-Denomy","doi":"10.1128/jb.00222-24","DOIUrl":"https://doi.org/10.1128/jb.00222-24","url":null,"abstract":"Journal of Bacteriology, Ahead of Print. <br/>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142267923","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Flagellar point mutation causes social aggregation in laboratory-adapted <i>Bacillus subtilis</i> under conditions that promote swimming.","authors":"Safiya Alvi, V Denise Mondelo, Jacqueline Boyle, Amanda Buck, Justin Gejo, Molly Mason, Shriya Matta, Abigail Sheridan, Mark A B Kreutzberger, Edward H Egelman, Anna McLoon","doi":"10.1128/jb.00199-24","DOIUrl":"10.1128/jb.00199-24","url":null,"abstract":"<p><p>Motility allows microbes to explore and maximize success in their environment; however, many laboratory bacterial strains have a reduced or altered capacity for motility. Swimming motility in <i>Bacillus subtilis</i> depends on peritrichous flagella and is carried out individually as cells move by biased random walks toward attractants. Previously, we adapted <i>Bacillus subtilis</i> strain 3610 to the laboratory for 300 generations in lysogeny broth (LB) batch culture and isolated lab-adapted strains. Strain SH2 is motility-defective and in broth culture forms large, frequently spherical aggregates of cells. A single point mutation in the flagellin gene <i>hag</i> that causes amino acid 259 to switch from A to T is necessary and sufficient to cause these social cell aggregates, and aggregation occurs between flagellated cells bearing this point mutation regardless of the strain background. Cells associate when bearing this mutation, but flagellar rotation is needed to pull associating cells into spherical aggregates. Using electron microscopy, we are able to show that the SH2 flagellar filament has limited polymorphism when compared to other flagellar structures. This limited polymorphism hinders the flagellum's ability to function as a motility apparatus but appears to alter its function to that of cell aggregation/adhesion. We speculate that the genotype-specific aggregation of cells producing Hag^A259T flagella could have increased representation in a batch-culture experiment by allowing similar cells to go through a transfer together and also that this mutation could serve as an early step to evolve sociality in the natural world.IMPORTANCEThe first life forms on this planet were prokaryotic, and the earliest environments were aquatic, and from these relatively simple starting conditions, complex communities of microbes and ultimately multicellular organisms were able to evolve. Usually, motile cells in aqueous environments swim as individuals but become social by giving up motility and secreting extracellular substances to become a biofilm. Here, we identify a single point mutation in the flagellum that is sufficient to allow cells containing this mutation to specifically form large, suspended groups of cells. The specific change in the flagellar filament protein subunits causes a unique change in the flagellar structure. This could represent a distinct way for closely related cells to associate as an early precursor to sociality.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142154076","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The relationship between <i>pqs</i> gene expression and acylhomoserine lactone signaling in <i>Pseudomonas aeruginosa</i>.","authors":"Martín P Soto-Aceves, Nicole E Smalley, Amy L Schaefer, E Peter Greenberg","doi":"10.1128/jb.00138-24","DOIUrl":"10.1128/jb.00138-24","url":null,"abstract":"<p><p>The opportunistic pathogen <i>Pseudomonas aeruginosa</i> has complex quorum sensing (QS) circuitry, which involves two acylhomoserine lactone (AHL) systems, the LasI AHL synthase and LasR AHL-dependent transcriptional activator system and the RhlI AHL synthase-RhlR AHL-responsive transcriptional activator. There is also a quinoline signaling system [the <i>Pseudomonas</i> quinolone signal (PQS) system]. Although there is a core set of genes regulated by the AHL circuits, there is strain-to-strain variation in the non-core QS regulon. A size reduction of the QS regulon occurs in laboratory evolution experiments with the model strain PAO1. We used transcriptomics to test the hypothesis that reductive evolution in the PAO1 QS regulon can in large part be explained by a null mutation in <i>pqsR</i>, the gene encoding the transcriptional activator of the <i>pqs</i> operon. We found that PqsR had very little influence on the AHL QS regulon. This was a surprising finding because the last gene in the PqsR-dependent <i>pqs</i> operon, <i>pqsE</i>, codes for a protein, which physically interacts with RhlR, and this interaction is required for RhlR-dependent activation of some genes. We used comparative transcriptomics to examine the influence of a <i>pqsE</i> mutation on the QS regulon and identified only three transcripts, which were strictly dependent on PqsE. By using reporter constructs, we showed that the PqsE influence on other genes was dependent on experimental conditions and we have gained some insight about those conditions. This work adds to our understanding of the plasticity of the <i>P. aeruginosa</i> QS regulon and to the role PqsE plays in RhlR-dependent gene activation.IMPORTANCEOver many generations of growth in certain conditions, <i>Pseudomonas aeruginosa</i> undergoes a large reductive evolution in the number of genes activated by quorum sensing. Here, we rule out one plausible route of the reductive evolution: that a mutation in a transcriptional activator PqsR or the PqsR activation of <i>pqsE</i>, which codes for a chaperone for the quorum sensing signal-responsive transcription factor RhlR, explains the finding. We further provide information about the influence of PqsR and PqsE on quorum sensing in <i>P. aeruginosa</i>.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142132849","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Interspecies surfactants serve as public goods enabling surface motility in <i>Pseudomonas aeruginosa</i>.","authors":"Delayna L Warrell, Tiffany M Zarrella, Christopher Machalek, Anupama Khare","doi":"10.1128/jb.00281-24","DOIUrl":"10.1128/jb.00281-24","url":null,"abstract":"<p><p>In most natural environments, bacteria live in polymicrobial communities where secreted molecules from neighboring species alter bacterial behaviors, including motility, but such interactions are understudied. <i>Pseudomonas aeruginosa</i> is a motile opportunistic pathogen that exists in diverse multispecies environments, such as the soil, and is frequently found in human wound and respiratory tract co-infections with other bacteria, including <i>Staphylococcus aureus</i>. Here, we show that <i>P. aeruginosa</i> can co-opt secreted surfactants from other species for flagellar-based surface motility. We found that exogenous surfactants from <i>S. aureus</i>, other bacteria, and interkingdom species enabled <i>P. aeruginosa</i> to switch from swarming to an alternative surface spreading motility on semi-solid surfaces and allowed for the emergence of surface motility on hard agar where <i>P. aeruginosa</i> was otherwise unable to move. Although active flagellar function was required for surface spreading, known motility regulators were not essential, indicating that surface spreading may be regulated by an as yet unknown mechanism. This motility was distinct from the response of most other motile bacterial species in the presence of exogenous surfactants. Mutant analysis indicated that this <i>P. aeruginosa</i> motility was similar to a previously described mucin-based motility, \"surfing,\" albeit with divergent regulation. Thus, our study demonstrates that secreted surfactants from the host as well as neighboring bacterial and interkingdom species act as public goods facilitating <i>P. aeruginosa</i> flagella-mediated surfing-like surface motility, thereby allowing it to access different environmental niches.</p><p><strong>Importance: </strong>Bacterial motility is an important determinant of bacterial fitness and pathogenesis, allowing expansion and invasion to access nutrients and adapt to new environments. Here, we demonstrate that secreted surfactants from a variety of foreign species, including other bacterial species, infection hosts, fungi, and plants, facilitate surface spreading motility in the opportunistic pathogen <i>Pseudomonas aeruginosa</i> that is distinct from established motility phenotypes. This response to foreign surfactants also occurs in <i>Pseudomonas putida</i>, but not in more distantly related bacterial species. Our systematic characterization of surfactant-based surface spreading shows that these interspecies surfactants serve as public goods to enable <i>P. aeruginosa</i> to move and explore environmental conditions when it would be otherwise immotile.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142132848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Differential effects of inosine monophosphate dehydrogenase (IMPDH/GuaB) inhibition in <i>Acinetobacter baumannii</i> and <i>Escherichia coli</i>.","authors":"Yutian Peng, John G Moffat, Cory DuPai, Eric M Kofoed, Elizabeth Skippington, Zora Modrusan, Susan L Gloor, Kevin Clark, Yiming Xu, Shuxuan Li, Liuxi Chen, Xingrong Liu, Ping Wu, Seth F Harris, Shumei Wang, Terry D Crawford, Chun Sing Li, Zhiguo Liu, John Wai, Man-Wah Tan","doi":"10.1128/jb.00102-24","DOIUrl":"https://doi.org/10.1128/jb.00102-24","url":null,"abstract":"<p><p>Inosine 5'-monophosphate dehydrogenase (IMPDH), known as GuaB in bacteria, catalyzes the rate-limiting step in <i>de novo</i> guanine biosynthesis and is conserved from humans to bacteria. We developed a series of potent inhibitors that selectively target GuaB over its human homolog. Here, we show that these GuaB inhibitors are bactericidal, generate phenotypic signatures that are distinct from other antibiotics, and elicit different time-kill kinetics and regulatory responses in two important Gram-negative pathogens: <i>Acinetobacter baumannii</i> and <i>Escherichia coli</i>. Specifically, the GuaB inhibitor G6 rapidly kills <i>A. baumannii</i> but only kills <i>E. coli</i> after 24 h. After exposure to G6, the expression of genes involved in purine biosynthesis and stress responses change in opposite directions while siderophore biosynthesis is downregulated in both species. Our results suggest that different species respond to GuaB inhibition using distinct regulatory programs and possibly explain the different bactericidal kinetics upon GuaB inhibition. The comparison highlights opportunities for developing GuaB inhibitors as novel antibiotics.IMPORTANCE<i>A. baumannii</i> is a priority bacterial pathogen for which development of new antibiotics is urgently needed due to the emergence of multidrug resistance. We recently developed a series of specific inhibitors against GuaB, a bacterial inosine 5'-monophosphate dehydrogenase, and achieved sub-micromolar minimum inhibitory concentrations against <i>A. baumannii</i>. GuaB catalyzes the rate-limiting step of <i>de novo</i> guanine biosynthesis and is highly conserved across bacterial pathogens. This study shows that inhibition of GuaB induced a bacterial morphological profile distinct from that of other classes of antibiotics, highlighting a novel mechanism of action. Moreover, our transcriptomic analysis showed that regulation of <i>de novo</i> purine biosynthesis and stress responses of <i>A. baumannii</i> upon GuaB inhibition differed significantly from that of <i>E. coli</i>.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142132833","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Overexpression of diglucosyldiacylglycerol synthase leads to daptomycin resistance in <i>Bacillus subtilis</i>.","authors":"Ryogo Yamamoto, Kazuya Ishikawa, Yusuke Miyoshi, Kazuyuki Furuta, Shin-Ichi Miyoshi, Chikara Kaito","doi":"10.1128/jb.00307-24","DOIUrl":"https://doi.org/10.1128/jb.00307-24","url":null,"abstract":"<p><p>The lipopeptide antibiotic daptomycin exhibits bactericidal activity against Gram-positive bacteria by forming a complex with phosphatidylglycerol (PG) and lipid II in the cell membrane, causing membrane perforation. With the emergence of daptomycin-resistant bacteria, understanding the mechanisms of bacterial resistance to daptomycin has gained great importance. In this study, we aimed to identify the genetic factors contributing to daptomycin resistance in <i>Bacillus subtilis</i>, a model Gram-positive bacterium. Our findings demonstrated that overexpression of <i>ugtP</i>, which encodes diglucosyldiacylglycerol synthase, induces daptomycin resistance in <i>B. subtilis</i>. Specifically, overexpression of <i>ugtP</i> resulted in increased levels of diglucosyldiacylglycerol (Glc₂DAG) and decreased levels of acidic phospholipids cardiolipin and PG, as well as the basic phospholipid lysylphosphatidylglycerol. However, <i>ugtP</i> overexpression did not alter the cell surface charge and the susceptibility to the cationic antimicrobial peptide nisin or the cationic surfactant hexadecyltrimethylammonium bromide. Furthermore, by serial passaging in the presence of daptomycin, we obtained daptomycin-resistant mutants carrying <i>ugtP</i> mutations. These mutants showed increased levels of Glc₂DAG and a >4-fold increase in the minimum inhibitory concentration of daptomycin. These results suggest that increased Glc₂DAG levels, driven by <i>ugtP</i> overexpression, modify the phospholipid composition and confer daptomycin resistance in <i>B. subtilis</i> without altering the cell surface charge of the bacteria.IMPORTANCEDaptomycin is one of the last-resort drugs for the treatment of methicillin-resistant <i>Staphylococcus aureus</i> infections, and the emergence of daptomycin-resistant bacteria has become a major concern. Understanding the mechanism of daptomycin resistance is important for establishing clinical countermeasures against daptomycin-resistant bacteria. In the present study, we found that overexpression of <i>ugtP</i>, which encodes diglucosyldiacylglycerol synthase, induces daptomycin resistance in <i>B. subtilis</i>, a model Gram-positive bacteria. The overexpression of <i>UgtP</i> increased diglucosyldiacylglycerol levels, resulting in altered phospholipid composition and daptomycin resistance. These findings are important for establishing clinical strategies against daptomycin-resistant bacteria, including their detection and management.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142140172","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An exopolysaccharide pathway from a freshwater <i>Sphingomonas</i> isolate.","authors":"Alexandra G Goetsch, Daniel Ufearo, Griffin Keiser, Christian Heiss, Parastoo Azadi, David M Hershey","doi":"10.1128/jb.00169-24","DOIUrl":"10.1128/jb.00169-24","url":null,"abstract":"<p><p>Bacteria embellish their cell envelopes with a variety of specialized polysaccharides. Biosynthesis pathways for these glycans are complex, and final products vary greatly in their chemical structures, physical properties, and biological activities. This tremendous diversity comes from the ability to arrange complex pools of monosaccharide building blocks into polymers with many possible linkage configurations. Due to the complex chemistry of bacterial glycans, very few biosynthetic pathways have been defined in detail. As part of an initiative to characterize novel polysaccharide biosynthesis enzymes, we isolated a bacterium from Lake Michigan called <i>Sphingomonas</i> sp. LM7 that is proficient in exopolysaccharide (EPS) production. We identified genes that contribute to EPS biosynthesis in LM7 by screening a transposon mutant library for colonies displaying altered colony morphology. A gene cluster was identified that appears to encode a complete <i>wzy/wzx-</i>dependent polysaccharide assembly pathway. Deleting individual genes in this cluster caused a non-mucoid phenotype and a corresponding loss of EPS secretion, confirming the role of this gene cluster in polysaccharide production. We extracted EPS from LM7 cultures and determined that it contains a linear chain of 3- and 4-linked glucose, galactose, and glucuronic acid residues. Finally, we show that the EPS pathway in <i>Sphingomonas</i> sp. LM7 diverges from that of sphingan-family EPSs and adhesive polysaccharides such as the holdfast that are present in other <i>Alphaproteobacteria</i>. Our approach of characterizing complete biosynthetic pathways holds promise for engineering polysaccharides with valuable properties.</p><p><strong>Importance: </strong>Bacteria produce complex polysaccharides that serve a range of biological functions. These polymers often have properties that make them attractive for industrial applications, but they remain woefully underutilized. In this work, we studied a novel polysaccharide called promonan that is produced by <i>Sphingomonas</i> sp. LM7, a bacterium we isolated from Lake Michigan. We extracted promonan from LM7 cultures and identified which sugars are present in the polymer. We also identified the genes responsible for polysaccharide production. Comparing the promonan genes to those of other bacteria showed that promonan is distinct from previously characterized polysaccharides. We conclude by discussing how the promonan pathway could be used to produce new polysaccharides through genetic engineering.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11340318/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141616486","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The role of <i>Listeria monocytogenes</i> PstA in β-lactam resistance requires the cytochrome <i>bd</i> oxidase activity.","authors":"Zepeng Tu, David M Stevenson, Darrel McCaslin, Daniel Amador-Noguez, TuAnh N Huynh","doi":"10.1128/jb.00130-24","DOIUrl":"10.1128/jb.00130-24","url":null,"abstract":"<p><p>c-di-AMP is an essential second messenger that binds and regulates several proteins of different functions within bacterial cells. Among those, PstA is a structurally conserved c-di-AMP-binding protein, but its function is largely unknown. PstA is structurally similar to PII signal transduction proteins, although it specifically binds c-di-AMP rather than other PII ligands such as ATP and α-ketoglutarate. In <i>Listeria monocytogenes</i>, we found that PstA increases β-lactam susceptibility at normal and low c-di-AMP levels, but increases β-lactam resistance upon c-di-AMP accumulation. Examining a PstA mutant defective for c-di-AMP binding, we found the apo form of PstA to be toxic for β-lactam resistance, and the c-di-AMP-bound form to be beneficial. Intriguingly, a role for PstA in β-lactam resistance is only prominent in aerobic cultures, and largely diminished under hypoxic conditions, suggesting that PstA function is linked to aerobic metabolism. However, PstA does not control aerobic growth rate, and has a modest influence on the tricarboxylic acid cycle and membrane potential-an indicator of cellular respiration. The regulatory role of PstA in β-lactam resistance is unrelated to reactive oxygen species or oxidative stress. Interestingly, during aerobic growth, PstA function requires the cytochrome <i>bd</i> oxidase (CydAB), a component of the respiratory electron transport chain. The requirement for CydAB might be related to its function in maintaining a membrane potential, or redox stress response activities. Altogether, we propose a model in which apo-PstA diminishes β-lactam resistance by interacting with an effector protein, and this activity can be countered by c-di-AMP binding or a by-product of redox stress.</p><p><strong>Importance: </strong>PstA is a structurally conserved c-di-AMP-binding protein that is broadly present among Firmicutes bacteria. Furthermore, PstA binds c-di-AMP at high affinity and specificity, indicating an important role in the c-di-AMP signaling network. However, the molecular function of PstA remains elusive. Our findings reveal contrasting roles of PstA in β-lactam resistance depending on c-di-AMP-binding status. We also define physiological conditions for PstA function during aerobic growth. Future efforts can exploit these conditions to identify PstA interaction partners under β-lactam stress.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11340317/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141590415","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Erratum for Danhorn et al., \"Phosphorus Limitation Enhances Biofilm Formation of the Plant Pathogen <i>Agrobacterium tumefaciens</i> through the PhoR-PhoB Regulatory System\".","authors":"Thomas Danhorn, Morten Hentzer, Michael Givskov, Matthew R Parsek, Clay Fuqua","doi":"10.1128/jb.00238-24","DOIUrl":"10.1128/jb.00238-24","url":null,"abstract":"","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11340304/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141590414","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}