Journal of Bacteriology最新文献

{"title":"Resistance and germination of spores of <i>Bacillus</i> species lacking members of a spore integral inner membrane protein family and locations of these proteins in spores.","authors":"Shermeen Khan, James Wicander, George Korza, Rebecca Caldbeck, Ann E Cowan, Graham Christie, Peter Setlow","doi":"10.1128/jb.00217-25","DOIUrl":"https://doi.org/10.1128/jb.00217-25","url":null,"abstract":"<p><p>Spores of <i>Bacillus</i> species are dormant and resistant to heat and chemicals but \"return to life\" in germination, and cells of some species/strains can cause food spoilage or disease. Recently, two members of a family of five spore integral inner membrane (IM) small protein homologs were found to be important in <i>B. subtilis</i> spore resistance and germination. Among these IM proteins, YetF is the most abundant. In the current work, we show that loss of any of these five homologs decreased spore resistance to heat and chemicals, with greater decreases when multiple homologs were absent. In addition, <i>B. subtilis</i> spores' loss of YetF and its homologs decreased the rates of spore germination, whereas loss of the second most abundant homolog, YrbG, increased germination rates. Surprisingly, <i>B. subtilis</i> spores lacking YetF and YrbG germinated spontaneously early in sporulation. Although this spontaneous germination did not involve normal germinant receptors or cortex peptidoglycan lytic enzymes, it was accelerated by overexpression of the IM channel for CaDPA release in germination. Loss of various homologs increased IM fluidity significantly, perhaps important in the effects of these proteins on spore resistance and germination. Notably, a functional YetF-GFP fusion was located in 5-7 IM spots in wild-type <i>B. subtilis</i> spores and in spores lacking the coat and outer membrane, although the function of these YetF spots is not clear. Similar spots were observed in <i>Bacillus megaterium</i> YetF-GFP spores, whereas <i>ydfS</i> null spores showed decreased wet heat resistance. Clearly, these novel proteins may have more surprises in store!IMPORTANCESpores of <i>Bacillota</i> are vectors for food spoilage and disease, and are hard to kill, as <i>B. subtilis</i> spores are killed only slowly by wet heat at 90°C. Multiple factors contribute to spores' wet heat resistance, including low spore core water content and DNA-protective proteins. Recently, a group of spore-specific inner membrane (IM) proteins was identified as increasing IM rigidity and spore wet heat resistance. <i>B. subtilis</i> has five of these proteins, with multiple homologs in all <i>Bacillus</i> and <i>Clostridium</i> species. These proteins increase IM rigidity, which increases spore wet heat resistance and can either increase or decrease the rates of spore germination, with similar effects on <i>B. megaterium</i> spores. These proteins are thus a new factor important in spore properties.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0021725"},"PeriodicalIF":3.0,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145040229","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":"A new family of small ArdA proteins reveals antirestriction activity.","authors":"A A Utkina, A A Kudryavtseva, O E Melkina, S M Rastorguev, A V Vlasov, K S Pustovoit, I V Manukhov","doi":"10.1128/jb.00318-25","DOIUrl":"https://doi.org/10.1128/jb.00318-25","url":null,"abstract":"<p><p>Antirestriction proteins protect mobile genetic elements from the host's restriction-modification (RM) systems. In our study, we identified a new family of small proteins, which we named sArdA. The sArdA proteins are homologous to DNA-mimicking ArdA proteins but differ in size, being approximately one-third the length of full ArdAs. Moreover, the sArdA family contains two subgroups, one of which is structurally similar to the N-terminal end of ArdA, whereas the other one matches the C-terminal end. Both the N-terminal and C-terminal domains of ArdA appear capable of independent expression. Phylogenetic analysis demonstrated that genes encoding these proteins evolved into evolutionarily stable subfamilies, named sArdN and sArdC, respectively. AlphaFold structure prediction of sArdA interaction with RM systems revealed four states of EcoKI, which differ in the angle between its two M-subunits while interacting with different ArdAs or DNA. Interestingly, both sArdN and sArdC triggered the same intermediate closed state of EcoKI, indicating possible new interaction pathways of Ards with RM systems. For phenotypic studies in <i>Escherichia coli</i> cells, we cloned the <i>sardN</i> gene from the chromosome of <i>Corynebacterium pilbarense</i> and the <i>sardC</i> gene from <i>Lactococcus cremoris</i>. Both genes protected λ phage DNA from restriction by the type I RM system. However, they revealed specificities to different restriction-modification systems. Specifically, <i>sArdC</i> was more effective against EcoR124II, whereas <i>sArdN</i> was more potent against EcoKI. Furthermore, both genes demonstrated antimethylation activity against EcoKI. Our current findings suggest the idea that the binding specificity of DNA-mimicking proteins to their targets could also be achieved by very short proteins.IMPORTANCEOur current findings suggest that the binding specificity of DNA-mimicking proteins to their targets could also be achieved by very short proteins. The ability of these DNA-mimicking proteins to specifically inhibit different DNA-binding proteins makes them a promising tool for regulating a range of intracellular processes, including gene expression.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0031825"},"PeriodicalIF":3.0,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145040282","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":"Translational coupling of neighboring genes in prokaryotes.","authors":"Kerry M Brown, Joseph T Wade","doi":"10.1128/jb.00255-25","DOIUrl":"https://doi.org/10.1128/jb.00255-25","url":null,"abstract":"<p><p>Prokaryotic genomes are gene-dense, so genes in the same orientation are often separated by short intergenic sequences or even overlap. Many mechanisms of regulation depend on open reading frames (ORFs) being spatially close to one another. Here, we describe one such mechanism, translational coupling, where translation of one gene promotes translation of a co-oriented neighboring gene. Translational coupling has been observed across the prokaryotic kingdom. Coupling is most efficient when the intergenic distance between ORFs is small. Coupling efficiency is influenced by RNA secondary structure, the presence of a Shine-Dalgarno (SD) sequence, and potentially by other <i>cis</i>-acting elements. While the mechanism of translational coupling has not been firmly established, two models have been proposed. In the RNA unfolding model, translation of the upstream gene in a pair disrupts inhibitory RNA secondary structure around the start codon of the downstream gene. Alternatively, the reinitiation model proposes that the same ribosome-either the 30S or complete 70S-translates both genes in a coupled pair. We describe evidence in support of each model, and we discuss the functional implications of translational coupling.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0025525"},"PeriodicalIF":3.0,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145015439","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":"Analysis of essential genes in <i>Clostridioides difficile</i> by CRISPRi and Tn-seq.","authors":"Maia E Alberts, Micaila P Kurtz, Ute Müh, Jonathon P Bernardi, Kevin W Bollinger, Horia A Dobrila, Leonard Duncan, Hannah M Laster, Andres J Orea, Anthony G Pannullo, Juan G Rivera-Rosado, Facundo V Torres, Craig D Ellermeier, David S Weiss","doi":"10.1128/jb.00220-25","DOIUrl":"10.1128/jb.00220-25","url":null,"abstract":"<p><p>Essential genes are interesting in their own right and as potential antibiotic targets. To date, only one report has identified essential genes on a genome-wide scale in <i>Clostridioides difficile</i>, a problematic pathogen for which treatment options are limited. That foundational study used large-scale transposon mutagenesis to identify 404 protein-encoding genes as likely to be essential for vegetative growth of the epidemic strain R20291. Here, we revisit the essential genes of strain R20291 using a combination of CRISPR interference (CRISPRi) and transposon insertion site sequencing (Tn-seq). First, we targeted 181 of the 404 putatively essential genes with CRISPRi. We confirmed essentiality for >90% of the targeted genes and observed morphological defects for >80% of them. Second, we conducted a new Tn-seq analysis, which identified 346 genes as essential, of which 283 are in common with the previous report and might be considered a provisional essential gene set that minimizes false positives. We compare the list of essential genes to those of other bacteria, especially <i>Bacillus subtilis</i>, highlighting some noteworthy differences. Finally, we used fusions to red fluorescent protein (RFP) to identify 18 putative new cell division proteins, 3 of which are conserved in Bacillota but of largely unknown function. Collectively, our findings provide new tools and insights that advance our understanding of <i>C. difficile</i>.IMPORTANCE<i>Clostridioides difficile</i> is an opportunistic pathogen for which better antibiotics are sorely needed. Most antibiotics target pathways that are essential for viability. Here, we use saturation transposon mutagenesis and gene silencing with CRISPR interference to identify and characterize genes required for growth on laboratory media. Comparison to the model organism <i>Bacillus subtilis</i> revealed many similarities and a few striking differences that warrant further study and may include opportunities for developing antibiotics that kill <i>C. difficile</i> without decimating the healthy microbiota needed to keep <i>C. difficile</i> in check.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0022025"},"PeriodicalIF":3.0,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145015488","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":"A <i>trans</i>-translation inhibitor that targets ribosomal protein bL12 kills <i>Mycobacterium tuberculosis</i>.","authors":"Akanksha Varshney, John N Alumasa, Amber Miller, Kenneth C Keiler","doi":"10.1128/jb.00236-25","DOIUrl":"10.1128/jb.00236-25","url":null,"abstract":"<p><p>New antibiotics with novel mechanisms of action are needed to treat infections by multidrug-resistant strains of <i>Mycobacterium tuberculosis</i>. Here, we show that KKL-1005, an anti-tubercular triazole-based molecule, binds to ribosomal protein bL12 and specifically inhibits the <i>trans</i>-translation ribosome rescue pathway, a process essential for the survival of <i>M. tuberculosis</i>. Our data demonstrate that KKL-1005 binds to the N-terminal domain of bL12, both <i>in vitro</i> and in bacterial cells, and specifically inhibits <i>trans</i>-translation and not normal translation. These results suggest that tmRNA-SmpB interacts with bL12 differently from tRNA and raise the possibility of developing antibiotics targeting bL12.IMPORTANCETuberculosis continues to be a leading cause of death worldwide, and antibiotics that target new pathways are urgently needed. <i>trans</i>-Translation is a ribosome rescue pathway required for the survival of <i>Mycobacterium tuberculosis</i>. We identified a small molecule, KKL-1005, that specifically inhibits <i>trans</i>-translation without affecting translation from a library of compounds that prevent the growth of <i>M. tuberculosis</i>. KKL-1005 targets bacterial ribosomal protein bL12, which is essential for the recruitment and activation of GTPase translation factors. The specificity of KKL-1005 for <i>trans</i>-translation indicates that bL12 interacts differently with the translation machinery during <i>trans</i>-translation than during canonical translation. KKL-1005 is bactericidal against <i>M. tuberculosis</i>, suggesting that inhibiting <i>trans</i>-translation by targeting bL12 is a new strategy for developing antibiotics against drug-resistant infections.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0023625"},"PeriodicalIF":3.0,"publicationDate":"2025-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144955272","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":"Role of thioredoxin reductase (TrxB) in oxidative stress response of <i>Francisella tularensis</i> live vaccine strain.","authors":"Matthew Higgs, Zhuo Ma, Anthony Centone, Chandra Shekhar Bakshi, Meenakshi Malik","doi":"10.1128/jb.00173-25","DOIUrl":"10.1128/jb.00173-25","url":null,"abstract":"<p><p><i>Francisella tularensis</i> is an important human pathogen responsible for causing tularemia in the Northern Hemisphere. <i>Francisella</i> has been developed as a biological weapon in the past due to its extremely high virulence. <i>F. tularensis</i> is a gram-negative, intracellular pathogen that primarily infects macrophages. <i>F. tularensis</i> encodes a repertoire of antioxidant enzymes to counteract the reactive oxygen and nitrogen species (ROS/RNS) produced by macrophages in response to infection. Among these, the thioredoxin system is critical for maintaining cellular redox homeostasis by regulating the balance between oxidation and reduction within bacterial cells. This system includes thioredoxins, thioredoxin reductase, and NADPH. Despite its potential importance, the thioredoxin system of <i>F. tularensis</i> remains understudied. <i>F. tularensis</i> live vaccine strain (LVS) possesses two thioredoxin genes, <i>trxA1</i> (<i>FTL_0611</i>) and <i>trxA2</i> (<i>FTL_1224</i>), and a single thioredoxin reductase gene, <i>trxB</i> (<i>FTL_1571</i>). In this study, we characterized the role of <i>trxB</i> of <i>F. tularensis</i> LVS in oxidative stress resistance. Our findings demonstrate that <i>trxB</i> is essential for oxidative stress resistance in <i>F. tularensis</i> and that its loss increases susceptibility to several antibiotics. However, unlike other bacterial species, TrxB in <i>F. tularensis</i> is not a functional target of the gold-containing antimicrobial agent auranofin. We also show that OxyR, the master regulator of oxidative stress responses, directly controls <i>trxB</i> expression under oxidative stress conditions. Furthermore, TrxB contributes to intramacrophage survival by enabling the bacterium to withstand ROS-induced oxidative stress. Collectively, this study highlights a critical, previously uncharacterized antioxidant defense mechanism in <i>F. tularensis</i> and its importance in oxidative stress resistance and intramacrophage survival.</p><p><strong>Importance: </strong>This study elucidates the function of the <i>trxB</i> gene, which encodes a thioredoxin reductase, in overcoming oxidative stress by <i>Francisella tularensis</i>. Loss of the <i>trxB</i> gene results in enhanced susceptibility to oxidants, diminished intracellular survival, and antibiotic resistance. Unlike other bacterial species, <i>F. tularensis</i> TrxB is not a functional target of auranofin, a gold-containing antimicrobial compound, suggesting divergence in thioredoxin system interactions. Furthermore, transcriptional regulation of <i>trxB</i> by OxyR in response to oxidative stress highlights an adaptive control mechanism essential to resist oxidative stress. These findings provide a mechanistic understanding of <i>F. tularensis</i> antioxidant defenses and their role in intramacrophage survival.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0017325"},"PeriodicalIF":3.0,"publicationDate":"2025-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12478593/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144955201","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 Wan et al., \"Biological characteristics of mechanosensitive channels MscS and MscL in <i>Actinobacillus pleuropneumoniae</i>\".","authors":"Jiajia Wan, Lu Dai, Huasong Xiao, Wendie Zhang, Rui Zhang, Tingting Xie, Yizhen Jia, Xuejun Gao, Jing Huang, Feng Liu","doi":"10.1128/jb.00237-25","DOIUrl":"https://doi.org/10.1128/jb.00237-25","url":null,"abstract":"","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0023725"},"PeriodicalIF":3.0,"publicationDate":"2025-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144955250","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":"Pyrimidine sufficiency is required for Sae two-component system signaling in <i>Staphylococcus aureus</i>.","authors":"Dennis A DiMaggio, Won-Sik Yeo, Shaun R Brinsmade","doi":"10.1128/jb.00115-25","DOIUrl":"10.1128/jb.00115-25","url":null,"abstract":"<p><p>Nucleotide metabolism in pathogens is essential for their virulence, supporting their growth, survival, and immune evasion during infection. Virulence in <i>Staphylococcus aureus</i> is driven by the production of virulence factors that facilitate nutrient acquisition and promote immune evasion and subversion. One key virulence regulatory system is the Sae two-component system, which upregulates the production of various virulence factors. The sensor histidine kinase SaeS, a member of the intramembrane family of histidine kinases (HKs), lacks a signal-binding domain, leaving the mechanisms by which these HKs sense signals and regulate gene expression unclear. We report that pyrimidine sufficiency is essential for maintaining Sae activity. Disruption of genes involved in pyrimidine biosynthesis reduces Sae-dependent promoter activity under pyrimidine-limited conditions. Phos-tag electrophoresis confirmed that pyrimidine limitation impacts SaeS kinase activity directly. The effect of pyrimidine limitation on SaeS was abrogated in a strain producing only the catalytic domain, suggesting that pyrimidines regulate SaeS activity at the membrane. Additionally, pyrimidine limitation results in cell envelope defects, specifically increased lipoteichoic acids, and incorporation of free fatty acids into the membrane. While both cell envelope aberrations are detrimental to Sae activity, we found that removal of the accumulated free fatty acids restored Sae activity. Our study highlights the interplay between nucleotide metabolism and membrane integrity in regulating virulence factor expression through signal transduction systems in pathogens.IMPORTANCEVirulence is often correlated with nutrient depletion, but our understanding of this coordination is incomplete. In <i>Staphylococcus aureus</i>, the Sae two-component system is a major regulator of virulence factor production and secretion, but as the sensor histidine kinase SaeS lacks an obvious domain to perceive its inducing signal, basic questions surrounding how the kinase is triggered persist. Here, we aimed to investigate the mechanism by which pyrimidines act to promote the activity of the SaeS kinase in <i>S. aureus</i> and further expand on the importance of the roles of pyrimidines in regulating envelope biogenesis. Understanding this intersection between nucleotide metabolism and virulence regulation opens up the possibility for the development of targeted anti-virulence strategies against <i>S. aureus</i> infections.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0011525"},"PeriodicalIF":3.0,"publicationDate":"2025-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12369341/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144674888","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 urinary microbiome: the next frontier of bacterial ecology.","authors":"Seth A Reasoner, Jamisha Francis, Maria Hadjifrangiskou","doi":"10.1128/jb.00105-25","DOIUrl":"10.1128/jb.00105-25","url":null,"abstract":"<p><p>The human urinary tract, once presumed to be sterile, has emerged as a new frontier of microbial ecology. Recent advancements in high-throughput sequencing technologies have revealed the complexity and diversity of microbial communities that reside within the urinary tract. This mini-review discusses the prominent bacteria identified in the urinary microbiome and their correlations with various urologic conditions. This review serves to summarize the current state of urobiome research and chart a path for ongoing discovery. Additionally, we address the methodological challenges in urinary microbiome research, emphasizing the need for standardization in study protocols and the refinement of bioinformatics tools. We highlight that although differences in urobiome composition have been described for various urologic diseases. Similarly, the pathophysiologic source and consequences of those differences remain uncertain. We outline the steps to move urobiome research from descriptive to mechanistic studies, emphasizing rigorous study design, integrating multi-omics approaches, and developing robust model systems for experimental investigation. Finally, we outline critical questions for future investigation aimed at elucidating the intricate connections between the urinary microbiome and host health.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0010525"},"PeriodicalIF":3.0,"publicationDate":"2025-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12369349/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144698612","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 emerging role of DNA methylation in the pathogenicity of bacterial pathogens.","authors":"Ya-Xuan Ma, Xiu-Dan Wang, Xin-Min Li","doi":"10.1128/jb.00108-25","DOIUrl":"10.1128/jb.00108-25","url":null,"abstract":"<p><p>Uncovering the mechanisms regulating the pathogenicity of bacterial pathogens can help improve diagnostic capabilities and aid the development of new drugs, both of which are crucial for reducing the burden caused by bacterial infections. In recent years, with advancements in third-generation sequencing technologies, increasing evidence has shown that DNA methylation plays a pivotal role in the pathogenicity of bacterial pathogens. We believe that the key DNA methyltransferases involved in pathogenicity represent promising targets for antimicrobial therapies and that the DNA methylation sites involved in bacterial pathogenicity are important biomarkers for diagnosing bacterial infections. In this review, we summarize the following topics: (i) methods for DNA methylation sequencing; (ii) the involvement of DNA methylation in antibacterial drug resistance; (iii) the influence of DNA methylation on the expression of bacterial virulence genes; (iv) the impact of DNA methylation on bacterial biofilm formation, adhesion, and motility; and (v) the role of DNA methylation in bacterial adaptation. We hope to provide insights into bacterial pathogenicity from the perspective of bacterial epigenetics.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0010825"},"PeriodicalIF":3.0,"publicationDate":"2025-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12369329/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144649569","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}