Journal of Bacteriology最新文献

{"title":"<i>Vibrio cholerae</i> pathogenicity island 2 encodes two distinct types of restriction systems.","authors":"Grazia Vizzarro, Alexandre Lemopoulos, David William Adams, Melanie Blokesch","doi":"10.1128/jb.00145-24","DOIUrl":"10.1128/jb.00145-24","url":null,"abstract":"<p><p>In response to predation by bacteriophages and invasion by other mobile genetic elements such as plasmids, bacteria have evolved specialized defense systems that are often clustered together on genomic islands. The O1 El Tor strains of <i>Vibrio cholerae</i> responsible for the ongoing seventh cholera pandemic (7PET) contain a characteristic set of genomic islands involved in host colonization and disease, many of which contain defense systems. Notably, <i>Vibrio</i> pathogenicity island 2 contains several characterized defense systems as well as a putative type I restriction-modification (T1RM) system, which, interestingly, is interrupted by two genes of unknown function. Here, we demonstrate that the T1RM system is active, methylates the host genomes of a representative set of 7PET strains, and identify a specific recognition sequence that targets non-methylated plasmids for restriction. We go on to show that the two genes embedded within the T1RM system encode a novel two-protein modification-dependent restriction system related to the GmrSD family of type IV restriction enzymes. Indeed, we show that this system has potent anti-phage activity against diverse members of the <i>Tevenvirinae</i>, a subfamily of bacteriophages with hypermodified genomes. Taken together, these results expand our understanding of how this highly conserved genomic island contributes to the defense of pandemic <i>V. cholerae</i> against foreign DNA.</p><p><strong>Importance: </strong>Defense systems are immunity systems that allow bacteria to counter the threat posed by bacteriophages and other mobile genetic elements. Although these systems are numerous and highly diverse, the most common types are restriction enzymes that can specifically recognize and degrade non-self DNA. Here, we show that the <i>Vibrio</i> pathogenicity island 2, present in the pathogen <i>Vibrio cholerae</i>, encodes two types of restriction systems that use distinct mechanisms to sense non-self DNA. The first system is a classical Type I restriction-modification system, and the second is a novel modification-dependent type IV restriction system that recognizes hypermodified cytosines. Interestingly, these systems are embedded within each other, suggesting that they are complementary to each other by targeting both modified and non-modified phages.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411939/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141916733","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":"<i>N</i>-linked protein glycosylation in <i>Nanobdellati</i> (formerly DPANN) archaea and their hosts.","authors":"Satoshi Nakagawa, Hiroyuki D Sakai, Shigeru Shimamura, Yoshiki Takamatsu, Shingo Kato, Hirokazu Yagi, Saeko Yanaka, Maho Yagi-Utsumi, Norio Kurosawa, Moriya Ohkuma, Koichi Kato, Ken Takai","doi":"10.1128/jb.00205-24","DOIUrl":"10.1128/jb.00205-24","url":null,"abstract":"<p><p>Members of the kingdom <i>Nanobdellati</i>, previously known as DPANN archaea, are characterized by ultrasmall cell sizes and reduced genomes. They primarily thrive through ectosymbiotic interactions with specific hosts in diverse environments. Recent successful cultivations have emphasized the importance of adhesion to host cells for understanding the ecophysiology of <i>Nanobdellati</i>. Cell adhesion is often mediated by cell surface carbohydrates, and in archaea, this may be facilitated by the glycosylated S-layer protein that typically coats their cell surface. In this study, we conducted glycoproteomic analyses on two co-cultures of <i>Nanobdellati</i> with their host archaea, as well as on pure cultures of both host and non-host archaea. <i>Nanobdellati</i> exhibited various glycoproteins, including archaellins and hypothetical proteins, with glycans that were structurally distinct from those of their hosts. This indicated that <i>Nanobdellati</i> autonomously synthesize their glycans for protein modifications probably using host-derived substrates, despite the high energy cost. Glycan modifications on <i>Nanobdellati</i> proteins consistently occurred on asparagine residues within the N-X-S/T sequon, consistent with patterns observed across archaea, bacteria, and eukaryotes. In both host and non-host archaea, S-layer proteins were commonly modified with hexose, <i>N</i>-acetylhexosamine, and sulfonated deoxyhexose. However, the <i>N</i>-glycan structures of host archaea, characterized by distinct sugars such as deoxyhexose, nonulosonate sugar, and pentose at the nonreducing ends, were implicated in enabling <i>Nanobdellati</i> to differentiate between host and non-host cells. Interestingly, the specific sugar, xylose, was eliminated from the <i>N</i>-glycan in a host archaeon when co-cultured with <i>Nanobdella</i>. These findings enhance our understanding of the role of protein glycosylation in archaeal interactions.IMPORTANCE<i>Nanobdellati</i> archaea, formerly known as DPANN, are phylogenetically diverse, widely distributed, and obligately ectosymbiotic. The molecular mechanisms by which <i>Nanobdellati</i> recognize and adhere to their specific hosts remain largely unexplored. Protein glycosylation, a fundamental biological mechanism observed across all domains of life, is often crucial for various cell-cell interactions. This study provides the first insights into the glycoproteome of <i>Nanobdellati</i> and their host and non-host archaea. We discovered that <i>Nanobdellati</i> autonomously synthesize glycans for protein modifications, probably utilizing substrates derived from their hosts. Additionally, we identified distinctive glycosylation patterns that suggest mechanisms through which <i>Nanobdellati</i> differentiate between host and non-host cells. This research significantly advances our understanding of the molecular basis of microbial interactions in extreme environments.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411935/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142080391","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":"Physiological significance of the two isoforms of initiator tRNAs in <i>Escherichia coli</i>.","authors":"Amit Kumar Sahu, Riyaz Ahmad Shah, Divya Nashier, Prafful Sharma, Rajagopal Varada, Kuldeep Lahry, Sudhir Singh, Sunil Shetty, Tanweer Hussain, Umesh Varshney","doi":"10.1128/jb.00251-24","DOIUrl":"10.1128/jb.00251-24","url":null,"abstract":"<p><p><i>Escherichia coli</i> possesses four initiator tRNA (i-tRNA) genes, three of which are present together as <i>metZWV</i> and the fourth one as <i>metY</i>. In <i>E. coli</i> B, all four genes (<i>metZWV</i> and <i>metY</i>) encode i-tRNA^fMet1, in which the G at position 46 is modified to m⁷G46 by TrmB (m⁷G methyltransferase). However, in <i>E. coli</i> K, because of a single-nucleotide polymorphism, <i>metY</i> encodes a variant, i-tRNA^fMet2, having an A in place of m⁷G46. We generated <i>E. coli</i> strains to explore the importance of this polymorphism in i-tRNAs. The strains were sustained either on <i>metY</i>_A46 (<i>metY</i> of <i>E. coli</i> K origin encoding i-tRNA^fMet2) or its derivative <i>metY</i>_G46 (encoding i-tRNA^fMet1) in single (chromosomal) or plasmid-borne copies. We show that the strains sustained on i-tRNA^fMet1 have a growth fitness advantage over those sustained on i-tRNA^fMet2. The growth fitness advantages are more pronounced for the strains sustained on i-tRNA^fMet1 in nutrient-rich media than in nutrient-poor media. The growth fitness of the strains correlates well with the relative stabilities of the i-tRNAs <i>in vivo</i>. Furthermore, the atomistic molecular dynamics simulations support the higher stability of i-tRNA^fMet1 than that of i-tRNA^fMet2. The stability of i-tRNA^fMet1 remains unaffected upon the deletion of TrmB. These studies highlight how <i>metY</i>_G46 and <i>metY</i>_A46 alleles might influence the growth fitness of <i>E. coli</i> under certain nutrient-limiting conditions.</p><p><strong>Importance: </strong><i>Escherichia coli</i> harbors four initiator tRNA (i-tRNA) genes: three of these at <i>metZWV</i> and the fourth one at <i>metY</i> loci. In <i>E. coli</i> B, all four genes encode i-tRNA^fMet1. In <i>E. coli</i> K, because of a single-nucleotide polymorphism, metY encodes a variant, i-tRNA^fMet2, having an A in place of G at position 46 of i-tRNA sequence in metY. We show that G46 confers stability to i-tRNA^fMet1. The strains sustained on i-tRNA^fMet1 have a growth fitness advantage over those sustained on i-tRNA^fMet2. Strains harboring <i>metY</i>_G46 (B mimic) or <i>metY</i>_A46 (K mimic) show that while in the nutrient-rich media, the K mimic is outcompeted rapidly; in the nutrient-poor medium, the K mimic is outcompeted less rapidly.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411947/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142017522","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":"Nature should be the model for microbial sciences.","authors":"Brett J Baker, Emily Hyde, Pedro Leão","doi":"10.1128/jb.00228-24","DOIUrl":"10.1128/jb.00228-24","url":null,"abstract":"<p><p>Until recently, microbiologists have relied on cultures to understand the microbial world. As a result, model organisms have been the focus of research into understanding Bacteria and Archaea at a molecular level. Diversity surveys and metagenomic sequencing have revealed that these model species are often present in low abundance in the environment; instead, there are microbial taxa that are cosmopolitan in nature. Due to the numerical dominance of these microorganisms and the size of their habitats, these lineages comprise mind-boggling population sizes upward of 10²⁸ cells on the planet. Many of these dominant groups have cultured representatives and have been shown to be involved in mediating key processes in nature. Given their importance and the increasing need to understand changes due to climate change, we propose that members of Nitrosophaerota (<i>Nitrosopumilus maritimus</i>), SAR11 (<i>Pelagibacter ubique</i>), Hadesarchaeia, Bathyarchaeia, and others become models in the future. Abundance should not be the only measure of a good model system; there are other organisms that are well suited to advance our understanding of ecology and evolution. For example, the most well-studied symbiotic bacteria, like <i>Buchnera</i>, <i>Aliivibrio</i>, and <i>Rhizobium</i>, should be models for understanding host-associations. Also, there are organisms that hold new insights into major transitions in the evolution of life on the planet like the Asgard Archaea (Heimdallarchaeia). Innovations in a variety of <i>in situ</i> techniques have enabled us to circumvent culturing when studying everything from genetics to physiology. Our deepest understanding of microbiology and its impact on the planet will come from studying these microbes in nature. Laboratory-based studies must be grounded in nature, not the other way around.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411942/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142001725","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":"A <i>Vibrio cholerae</i> Type IV restriction system targets glucosylated 5-hydroxymethylcytosine to protect against phage infection.","authors":"Jasper B Gomez, Christopher M Waters","doi":"10.1128/jb.00143-24","DOIUrl":"10.1128/jb.00143-24","url":null,"abstract":"<p><p>A major challenge faced by <i>Vibrio cholerae</i> is constant predation by bacteriophage (phage) in aquatic reservoirs and during infection of human hosts. To overcome phage predation, <i>V. cholerae</i> has acquired and/or evolved a myriad of phage defense systems. Although several novel defense systems have been discovered, we hypothesized that more were encoded in <i>V. cholerae</i> given the low diversity of phages that have been isolated, which infect this species. Using a <i>V. cholerae</i> genomic library, we identified a Type IV restriction system consisting of two genes within a 16-kB region of the <i>Vibrio</i> pathogenicity island-2, which we name TgvA and TgvB (<b><u>T</u></b>ype I-embedded <b><i><u>g</u></i></b><i>mrSD</i>-like system of <b><u>V</u></b>PI-2). We show that both TgvA and TgvB are required for defense against T2, T4, and T6 by targeting glucosylated 5-hydroxymethylcytosine (5hmC). T2 or T4 phages that lose the glucose modifications are resistant to TgvAB defense but exhibit a significant evolutionary tradeoff, becoming susceptible to other Type IV restriction systems that target unglucosylated 5hmC. We also show that the Type I restriction-modification system that embeds the <i>tgvAB</i> genes protects against phage T3, secΦ18, secΦ27, and λ, suggesting that this region is a phage defense island. Our study uncovers a novel Type IV restriction system in <i>V. cholerae</i>, increasing our understanding of the evolution and ecology of <i>V. cholerae,</i> while highlighting the evolutionary interplay between restriction systems and phage genome modification.IMPORTANCEBacteria are constantly being predated by bacteriophage (phage). To counteract this predation, bacteria have evolved a myriad of defense systems. Some of these systems specifically digest infecting phage by recognizing unique base modifications present on the phage DNA. In this study, we discover a Type IV restriction system encoded in <i>V. cholerae,</i> which we name TgvAB, and demonstrate it recognizes and restricts phage that have 5-hydroxymethylcytosine glucosylated DNA. Moreover, the evolution of resistance to TgvAB render phage susceptible to other Type IV restriction systems, demonstrating a significant evolutionary tradeoff. These results enhance our understanding of the evolution of <i>V. cholerae</i> and more broadly how bacteria evade phage predation.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411926/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142125805","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":"Characterization of galactose catabolic pathways in <i>Streptococcus agalactiae</i> and identification of a major galactose: phosphotransferase importer.","authors":"Aurelia Hiron, Morgane Melet, Capucine Guerry, Ilona Dubois, Vanessa Rong, Philippe Gilot","doi":"10.1128/jb.00155-24","DOIUrl":"https://doi.org/10.1128/jb.00155-24","url":null,"abstract":"<p><p>We identified and characterized genomic regions of <i>Streptococcus agalactiae</i> that are involved in the Leloir and the tagatose-6-phosphate pathways for D-galactose catabolism. The accumulation of mutations in genes coding the Leloir pathway and the absence of these genes in a significant proportion of the strains suggest that this pathway may no longer be necessary for <i>S. agalactiae</i> and is heading toward extinction. In contrast, a genomic region containing genes coding for intermediates of the tagatose-6-phosphate pathway, a Gat family PTS transporter, and a DeoR/GlpR family regulator is present in the vast majority of strains. By deleting genes that code for intermediates of each of these two pathways in three selected strains, we demonstrated that the tagatose-6-phosphate pathway is their sole route for galactose catabolism. Furthermore, we showed that the Gat family PTS transporter acts as the primary importer of galactose in <i>S. agalactiae</i>. Finally, we proved that the DeoR/GlpR family regulator is a repressor of the tagatose-6-phosphate pathway and that galactose triggers the induction of this biochemical mechanism.IMPORTANCE<i>S. agalactiae</i>, a significant pathogen for both humans and animals, encounters galactose and galactosylated components within its various ecological niches. We highlighted the capability of this bacterium to metabolize D-galactose and showed the role of the tagatose-6-phosphate pathway and of a PTS importer in this biochemical process. Since <i>S. agalactiae</i> relies on carbohydrate fermentation for energy production, its ability to uptake and metabolize D-galactose could enhance its persistence and its competitiveness within the microbiome.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142287952","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":"Regulation of potassium uptake in <i>Caulobacter crescentus</i>.","authors":"Alex Quintero-Yanes, Loïc Léger, Madeline Collignon, Julien Mignon, Aurélie Mayard, Catherine Michaux, Régis Hallez","doi":"10.1128/jb.00107-24","DOIUrl":"10.1128/jb.00107-24","url":null,"abstract":"<p><p>Potassium (K⁺) is an essential physiological element determining membrane potential, intracellular pH, osmotic/turgor pressure, and protein synthesis in cells. Here, we describe the regulation of potassium uptake systems in the oligotrophic α-proteobacterium <i>Caulobacter crescentus</i> known as a model for asymmetric cell division. We show that <i>C. crescentus</i> can grow in concentrations from the micromolar to the millimolar range by mainly using two K⁺ transporters to maintain potassium homeostasis, the low-affinity Kup and the high-affinity Kdp uptake systems. When K⁺ is not limiting, we found that the <i>kup</i> gene is essential while <i>kdp</i> inactivation does not impact the growth. In contrast, <i>kdp</i> becomes critical but not essential and <i>kup</i> dispensable for growth in K⁺-limited environments. However, in the absence of <i>kdp</i>, mutations in <i>kup</i> were selected to improve growth in K⁺-depleted conditions, likely by increasing the affinity of Kup for K⁺. In addition, mutations in the KdpDE two-component system, which regulates <i>kdpABCDE</i> expression, suggest that the inner membrane sensor regulatory component KdpD mainly works as a phosphatase to limit the growth when cells reach late exponential phase. Our data therefore suggest that KdpE is phosphorylated by another non-cognate histidine kinase. On top of this, we determined the KdpE-dependent and independent K⁺ transcriptome. Together, our work illustrates how an oligotrophic bacterium responds to fluctuation in K⁺ availability.IMPORTANCEPotassium (K⁺) is a key metal ion involved in many essential cellular processes. Here, we show that the oligotroph <i>Caulobacter crescentus</i> can support growth at micromolar concentrations of K⁺ by mainly using two K⁺ uptake systems, the low-affinity Kup and the high-affinity Kdp. Using genome-wide approaches, we also determined the entire set of genes required for <i>C. crescentus</i> to survive at low K⁺ concentration as well as the full K⁺-dependent regulon. Finally, we found that the transcriptional regulation mediated by the KdpDE two-component system is unconventional since unlike <i>Escherichia coli</i>, the inner membrane sensor regulatory component KdpD seems to work rather as a phosphatase on the phosphorylated response regulator KdpE~P.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411941/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141916734","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":"TolC and EmrA1 contribute to <i>Francisella novicida</i> multidrug resistance and modulation of host cell death.","authors":"Erik J Kopping, P Todd Benziger, David G Thanassi","doi":"10.1128/jb.00246-24","DOIUrl":"10.1128/jb.00246-24","url":null,"abstract":"<p><p><i>Francisella</i> spp. are Gram-negative, facultative intracellular pathogens. <i>Francisella tularensis</i> causes the human disease tularemia and is considered a biological threat agent due to its high infectivity and virulence. A central aspect of <i>Francisella</i> virulence is its ability to dampen host immune responses. We previously identified the outer membrane channel (OMC) protein TolC as a critical <i>F. tularensis</i> virulence factor required for suppression of apoptotic and proinflammatory responses during macrophage infection. TolC functions as part of multidrug efflux systems and the type I secretion pathway that exports bacterial effector proteins. In these systems, TolC forms tripartite complexes together with an inner membrane transporter and periplasmic membrane fusion protein (MFP). To advance understanding of TolC function in <i>Francisella</i>, we analyzed OMC and MFP homologs in <i>Francisella novicida</i>, a widely used model species that causes a tularemia-like disease in mice. In agreement with the previous <i>F. tularensis</i> studies, all three OMCs present in <i>F. novicida</i> contributed to multidrug resistance, but only TolC was important for suppressing macrophage cell death. In addition, we identified the EmrA1 MFP as important for resisting antimicrobial compounds and dampening host cell death. In contrast to results obtained with <i>F. tularensis</i>, the cell death triggered during infection with the <i>F. novicida tolC</i> and <i>emrA1</i> mutants was dominated by pyroptosis rather than apoptosis. These data expand our understanding of TolC function in <i>Francisella</i> and underscore both conserved and differential aspects of <i>F. novicida</i> and <i>F. tularensis</i>.</p><p><strong>Importance: </strong><i>Francisella tularensis</i> is a Gram-negative intracellular bacterial pathogen and causative agent of tularemia. We previously identified the outer membrane channel protein TolC as contributing to antimicrobial resistance and subversion of host responses by <i>F. tularensis</i>. To advance understanding of TolC function in <i>Francisella</i> and to identify components that might work together with TolC, we took advantage of a transposon mutant library in <i>F. novicida</i>, a model species that causes a tularemia-like disease in mice. Our findings identify TolC and the membrane fusion protein EmrA1 as important for both antimicrobial resistance and suppression of macrophage cell death. This study also revealed differences in cell death pathways triggered by <i>F. novicida</i> versus <i>F. tularensis</i> infection that may relate to differences in virulence.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411944/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142080392","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":"Modulation of Vibrio cholerae gene expression through conjugative delivery of engineered regulatory small RNAs","authors":"Pilar Menendez-GilDiana VelevaMollie VirgoJige ZhangRita RamalheteBrian T. Ho1Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London, United Kingdom2Division of Biosciences, Institute of Structural and Molecular Biology, University College London, London, United KingdomLaurie E. Comstock","doi":"10.1128/jb.00142-24","DOIUrl":"https://doi.org/10.1128/jb.00142-24","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":"2024-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142267922","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 cell division protein FzlA performs a conserved function in diverse alphaproteobacteria","authors":"Isaac P. PayneBrody AubryJordan M. BarrowsPamela J. B. BrownErin D. Goley1Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA2Division of Biological Sciences, University of Missouri, Columbia, Missouri, USAConrad W. Mullineaux","doi":"10.1128/jb.00225-24","DOIUrl":"https://doi.org/10.1128/jb.00225-24","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":"2024-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142267974","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}