Molecular Microbiology最新文献

{"title":"Mycobacterial RadA Functions in Cyclic Di-AMP Mediated Homologous Recombination in Addition to Supporting RecA Activity","authors":"Nisha Goyal, Sudhanshu Mudgal, Rahul Saginela, Hanuman Singh Dagur, Rajakumara Eerappa, Krishna Murari Sinha","doi":"10.1111/mmi.70057","DOIUrl":"https://doi.org/10.1111/mmi.70057","url":null,"abstract":"<i>Mycobacterium</i> possesses unique DNA repair and recombination pathways that are absent in <i>E. coli</i>. The pathways are linked to mycobacterial virulence and survival within the host. Cyclic di-AMP, a secondary messenger present in <i>Mycobacterium</i> regulates DNA recombination, genome stability and SOS response. <i>radA</i> and <i>disA</i> exist in a conserved operon in several bacteria including <i>Mycobacterium</i> suggesting a role of RadA in cyclic di-AMP mediated DNA damage repair pathways. We show here that RadA is indeed involved in cyclic di-AMP mediated DSB repair pathways in <i>Mycobacterium</i> and has non-canonical function in DSB repair as well. Deletion of <i>radA</i> expectedly decreases HR efficiency but interestingly also results in illegitimate recombination outcome GC*. The illegitimate recombination GC* leads to increased stress induced mutagenesis giving rise to drug resistant mutants. We have also found that RadA influences NHEJ repair and in its absence the cells adopt alternative route of DNA repair. Our work shows active participation of RadA in several DNA repair and recombination pathways which could be targeted for potential therapeutics against <i>Mycobacterium</i>.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"51 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146160730","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The BosR Is Back!","authors":"D Scott Samuels, Meghan C Lybecker","doi":"10.1111/mmi.70046","DOIUrl":"10.1111/mmi.70046","url":null,"abstract":"<p><p>BosR is a novel nucleic acid-binding protein in the ferric uptake regulator (FUR) family that regulates gene expression in the Lyme disease spirochete Borrelia (Borreliella) burgdorferi. This issue of Molecular Microbiology contains a comprehensive transcriptomic study that keenly defines the regulatory swath of BosR in the vertebrate host of B. burgdorferi. Despite homology to Fur-like and PurR-like orthologs, BosR has traditionally been linked to regulation of RpoS, the alternative sigma factor that controls the regulon required for establishing a vertebrate infection. However, BosR regulates other genes through an RpoS-independent mechanism, which is elegantly elaborated in Grassmann et al., along with clearly demonstrating that BosR does not participate in the defense against oxidative and nitrosative stress in the vertebrate. However, the recently recognized role of BosR as an RNA-binding protein with RNA chaperone activity that regulates gene expression in a post-transcriptional fashion is not wholly appreciated, which clouds the results on determining the DNA-binding site in vivo. Regardless, this seminal study enshrines BosR as a major regulator of gene expression in B. burgdorferi and delineates a multitude of BosR-regulated cellular functions in the spirochete related to its ability to navigate between its tick vector and vertebrate host in nature as well as to persist in these two disparate environments.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"81-84"},"PeriodicalIF":3.1,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12871905/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145889806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An Improved Description of the Small RNA Landscape of the Human Fungal Pathogen Aspergillus fumigatus.","authors":"Xiaoqing Pan, Abdulrahman A Kelani, Lukas Schrettenbrunner, Swatika Prabakar, Bhawana Israni, Matthew G Blango","doi":"10.1111/mmi.70042","DOIUrl":"10.1111/mmi.70042","url":null,"abstract":"<p><p>Aspergillus fumigatus is a ubiquitous filamentous fungus and dangerous human pathogen that produces a limited pool of small RNAs under standard laboratory conditions. To better understand the rules of small RNA production in A. fumigatus, we induced canonical RNA interference (RNAi) via overexpression of two separate inverted-repeat transgenes. We observed production of predominantly 20-nt, 5' uridine-containing small RNAs from the 3' end of each transgene nearest to the loop region and dependent on dicer-like B RNase III enzyme. Using this refined knowledge, we assessed small RNA biogenesis by sRNA-seq in three double knockout strains of the RNAi pathway, namely the dicer-like proteins (ΔdclA/B), argonautes (ΔppdA/B), and RNA-dependent RNA polymerases (ΔrrpA/B). In each case, we found limited evidence for production of 5' U-containing small RNAs reliant on the RNAi machinery under standard laboratory conditions. We did observe 5' U-containing small RNAs amongst the abundant tRNA-derived RNAs (tDRs); however, biogenesis of tDRs was predominantly Dicer-like independent. To more accurately define the complex tDR repertoire, we employed a cutting-edge tDR-sequencing approach that improved tRNA-half detection and revealed qualitative morphotype-specific changes in the small RNA fraction of conidia relative to mycelium. Finally, leveraging the limited sRNA repertoire of A. fumigatus, we tested the consequences of inverted-repeat transgene overexpression in the ΔdclA/B double knockout, which revealed growth inhibition even in the absence of double-stranded RNA (dsRNA) processing and small RNA production. We hypothesize that the RNAi substrate-limited landscape of A. fumigatus facilitates sensitivity to increases in dsRNA, offering an intriguing system for future studies of dsRNA metabolism.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"133-144"},"PeriodicalIF":3.1,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12871901/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145889727","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bacterial Toxin Exploits Host Membrane Phospholipid as a Receptor for Binding, Entry, and Cytopathogenicity.","authors":"Alejandra M Kirkpatrick, Thirumalai R Kannan","doi":"10.1111/mmi.70044","DOIUrl":"10.1111/mmi.70044","url":null,"abstract":"<p><p>Mycoplasma pneumoniae is a leading cause of bacterial community-acquired pneumonia, responsible for severe respiratory and extrapulmonary diseases in children and adults. The Community Acquired Respiratory Distress Syndrome (CARDS) toxin is a key virulence factor that exerts ADP-ribosylating and vacuolating activities on host cells, recapitulating the inflammatory and histopathological damage seen in infected airways. Although the host proteins annexin-A2 (AnxA2) and surfactant protein-A were previously identified as toxin receptors, their absence did not abrogate CARDS toxin activity. Intriguingly, our subsequent work identified an interaction between CARDS toxin and the ubiquitous membrane phospholipids sphingomyelin (SM) and phosphatidylcholine (PC). This study investigated whether CARDS toxin uses these lipids as functional cell surface receptors. Using enzyme-linked immunosorbent assays, we demonstrated that the carboxy region of CARDS toxin binds to SM and PC in a dose-dependent manner, exhibiting higher affinity for SM. Depletion of SM from airway epithelial cell surface significantly reduced CARDS toxin binding, internalization and retrograde transport, as shown by immunoblot, pull-down, immunofluorescence, and live-cell imaging. Furthermore, SM depletion markedly decreased toxin-induced vacuolation and its stability, a phenotype rescued by adding exogenous SM. Notably, combining SM depletion with AnxA2 suppression nearly abolished toxin binding, entry, and subsequent vacuolation. These findings establish that CARDS toxin utilizes SM as a functional receptor to mediate its activity, highlighting a critical lipid-dependent mechanism for host cell targeting.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"145-158"},"PeriodicalIF":3.1,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12871915/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145892736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rop-Mediated Suppression of RpoS Production Increases Resistance to Nitric Oxide.","authors":"Takeshi Shimizu,Shin Suzuki,Ichiyou Fukumoto,Takashi Hamabata","doi":"10.1111/mmi.70051","DOIUrl":"https://doi.org/10.1111/mmi.70051","url":null,"abstract":"We identified the RNA-binding protein Rop, encoded on the pOSAK1 plasmid of enterohaemorrhagic Escherichia coli (EHEC), as a novel factor that enhances nitric oxide (NO) resistance, although it has previously been reported to regulate plasmid copy number. The Rop-induced increase in NO resistance was significantly reduced in several small noncoding RNA (sRNA) gene-deficient EHEC mutants. Among these sRNAs, DsrA, ArcZ, and RprA were directly involved in the translational regulation of rpoS expression, suggesting that Rop modulates rpoS expression through sRNAs. To examine this mechanism, we generated sRNA gene-deficient mutants with an additional deletion of the 5' untranslated region (5' UTR) of rpoS, which is required for translational regulation. The increase in NO resistance by Rop was restored in the double mutant, suggesting that this phenotype is mediated by Rop-dependent interactions between sRNAs and the 5' UTR of rpoS mRNA. Furthermore, Rop promoted rpoS mRNA degradation, an effect that likely suppresses RpoS production and may thereby enhance NO resistance. Finally, an hfq-deficient EHEC mutant exhibited no increase in NO resistance in the presence of Rop, indicating that Hfq is essential for Rop-mediated NO resistance.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"91 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146005352","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.","authors":"Dinh Quan Nhan,Karolina Michalska,Fernando Garza-Sánchez,Nicholas L Bartelli,Julia L E Willett,Lucy Stols,William H Eschenfeldt,Celia W Goulding,Andrzej Joachimiak,Christopher S Hayes","doi":"10.1111/mmi.70053","DOIUrl":"https://doi.org/10.1111/mmi.70053","url":null,"abstract":"Many Gram-negative bacterial species use contact-dependent growth inhibition (CDI) systems to deliver toxic proteins into neighboring competitors. CDI+ strains deploy CdiA effector proteins, which translocate their C-terminal toxin (CT) domains into target bacteria through a receptor-mediated delivery pathway. To protect against auto-intoxication, CDI+ bacteria also produce CdiI immunity proteins that neutralize CT toxin activity. Here, we present the crystal structure of the CT·CdiIO32:H37 complex from Escherichia coli O32:H37. CTO32:H37 adopts the same fold as the tRNase domain of colicin D, and the nucleases share similar catalytic centers. However, unlike colicin D, which cleaves the anticodon loops of tRNAArg isoacceptors, CTO32:H37 exhibits nonspecific RNase activity. Notably, we find that endogenous elongation factor Tu (EF-Tu) co-purifies with the over-produced CT·CdiIO32:H37 complex. Although EF-Tu does not bind stably to CTO32:H37 in the absence of CdiIO32:H37, the translation factor is required for toxic RNase activity in vitro. AlphaFold 3 modeling and site-directed mutagenesis indicate that CTO32:H37 interacts with the N-terminal GTPase domain of EF-Tu. EF-Tu appears to stabilize residue Trp52 within the hydrophobic core of the toxin, which in turn supports the RNase active site through an unusual hydrogen-bonding interaction with the catalytic His67 residue. Thus, EF-Tu is hijacked as an essential co-factor to organize the toxin's catalytic center.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"1 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146005351","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evolutionarily Diverged TRAPP Components in Giardia lamblia That Lacks a Classical Golgi.","authors":"Avishikta Chatterjee,Kuladip Jana,Sandipan Ganguly,Srimonti Sarkar","doi":"10.1111/mmi.70049","DOIUrl":"https://doi.org/10.1111/mmi.70049","url":null,"abstract":"The endomembrane system of the intestinal pathogen Giardia lamblia lacks a separate Golgi compartment. Without this sorting compartment, how cargo sorting to various subcellular destinations occurs within Giardia remains an open question. While the distribution of various Golgi-associated SNAREs and Rabs has been documented in this parasite, the TRAPP (TRAnsport Protein Particle) complex, a guanine nucleotide exchange factor for Golgi-associated Rabs, remained uncharacterized. Herein, we report that Giardia expresses a minimal set of TRAPP complex components, GlBet3, GlBet5, GlTrs23, and GlTrs31. Some of these components can interact with GlRab1a, GlRab11, and the COPII coat protein, GlSec23. Coupled with the colocalization and coimmunoprecipitation of GlBet3 and GlBet5, we propose the existence of a functional TRAPP complex in Giardia with an architecture that is different from that of yeast. While some interactions within this complex may be analogous to those in yeast, we find evidence of some unique interactions as well. The TRAPP genes are upregulated during encystation, and two components are associated with encystation-specific vesicles. Besides the endomembrane system, the presence of GlBet3 and GlBet5 at the plasma membrane, membrane wrapping ventral disc periphery, and the median body indicates that the TRAPP complex may support unique features and functions of Giardia.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"54 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145961271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Late Stage Mannan Metabolism in Cellvibrio japonicus Requires the Combined Action of a Mannosyl‐Glucose Phosphorylase and a Mannobiose Epimerase","authors":"Jessica K. Novak, Jeffrey G. Gardner","doi":"10.1111/mmi.70043","DOIUrl":"https://doi.org/10.1111/mmi.70043","url":null,"abstract":"Manno‐oligosaccharides and their metabolism play important roles in gut health, pharmaceutical development, and renewable chemical production. While the degradation of manno‐oligosaccharides has been previously studied, interest in bacterial mannobiose epimerases and mannoside phosphorylases is increasing because these enzymes provide a replacement for bacterial phosphotransferase systems as part of synthetic biology applications. In this report, we have physiologically and biochemically characterized the mannobiose epimerase and mannoside phosphorylase from the Gram‐negative saprophyte <jats:styled-content style=\"fixed-case\"> <jats:italic>Cellvibrio japonicus</jats:italic> </jats:styled-content> , which is a bacterium that does not possess a phosphotransferase system for sugar import. While the initial stages of mannan degradation by <jats:styled-content style=\"fixed-case\"> <jats:italic>C. japonicus</jats:italic> </jats:styled-content> have been studied, the physiological importance and biochemical activities of the mannosyl‐glucose phosphorylase (Mgp130A) and mannobiose epimerase (EpiA) predicted for latter stages of mannan metabolism were uncharacterized. After functional mutational analysis and biochemical assays of these two enzymes, we observed that both were essential for utilization of linear mannan, mannobiose, and mannotriose; however, only Mgp130A was critical for mannosyl‐glucose cleavage. A new plasmid (pJKN5) created during this study allowed for improved complementation analysis and uncovered a surprising toxic effect of galactose‐substituted manno‐oligosaccharides in strains lacking the <jats:italic>epiA</jats:italic> gene. Enzyme assay of Mgp130A revealed an enzyme with a high specific activity compared to other bacterial enzymes. Overall, this study advanced our understanding of <jats:styled-content style=\"fixed-case\"> <jats:italic>C. japonicus</jats:italic> </jats:styled-content> mannan metabolism and contributed to the growing characterization of bacterial glycoside phosphorylases and epimerases important for biotechnology.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"30 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145955163","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":" Bacillus subtilis RNase HII Is Inefficient at Processing Guanosine Monophosphate and Damaged Ribonucleotides","authors":"Julianna R. Cresti, Lyle A. Simmons","doi":"10.1111/mmi.70047","DOIUrl":"https://doi.org/10.1111/mmi.70047","url":null,"abstract":"During one round of DNA replication, nearly 2000 ribonucleoside monophosphates (rNMPs) are incorporated in place of their cognate deoxyribonucleoside monophosphates (dNMPs). Given their high rate of insertion, genomic DNA could contain rNMPs that are damaged or mismatched. Here, we test the activity of <jats:styled-content style=\"fixed-case\"> <jats:italic>Bacillus subtilis</jats:italic> </jats:styled-content> and <jats:styled-content style=\"fixed-case\"> <jats:italic>Escherichia coli</jats:italic> </jats:styled-content> RNase HII on canonical, mismatched, and damaged rNMPs. We show that <jats:styled-content style=\"fixed-case\"> <jats:italic>E. coli</jats:italic> </jats:styled-content> RNase HII is adept at incising most rNMP variants from DNA at similar frequencies, with the exception of an oxidized rNMP, where endoribonuclease activity is sharply reduced. In contrast, <jats:styled-content style=\"fixed-case\"> <jats:italic>B. subtilis</jats:italic> </jats:styled-content> RNase HII efficiently incises rAMP, rCMP, and rUMP but is inefficient at processing rGMP in both a canonical and mismatched base pair. We test damaged ribonucleotides and find that <jats:styled-content style=\"fixed-case\"> <jats:italic>B. subtilis</jats:italic> </jats:styled-content> RNase HII is refractory to processing abasic and oxidized ribonucleotide lesions. Our work shows that bacterial RNase HII enzymes have different intrinsic endoribonuclease activity toward the repair of canonical, mismatched, and damaged rNMPs, demonstrating that not all rNMP errors provoke efficient resolution. Our finding that <jats:styled-content style=\"fixed-case\"> <jats:italic>B. subtilis</jats:italic> </jats:styled-content> RNase HII is recalcitrant to repairing damaged rNMPs resembles what is observed for eukaryotic RNase H2 orthologs, suggesting that other repair processes are necessary to resolve damaged rNMPs.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"30 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145903603","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification of Specific Virulence Factors of Pseudomonas Strains in the Biocontrol of the Potato Pest Tecia solanivora","authors":"Luisa Pantoja, Pilar Vesga, Ziv Arbeli, Vivian Boyacá‐Vásquez, Javier Vanegas","doi":"10.1111/mmi.70041","DOIUrl":"https://doi.org/10.1111/mmi.70041","url":null,"abstract":"<jats:italic>Tecia solanivora</jats:italic> (The Guatemalan potato tuber moth) is a major potato pest, responsible for up to 20% of crop losses and a significant economic impact. Certain <jats:italic>Pseudomonas</jats:italic> exhibit insecticidal activity and produce virulence factors with cytotoxic and antimicrobial properties, positioning them as promising candidates for biological control. This study evaluated seven <jats:italic>Pseudomonas</jats:italic> strains with insecticidal activity and identified key virulence factors involved. The strains demonstrated varying degrees of insecticidal activity, with <jats:italic>Pseudomonas protegens</jats:italic> strains CHA0 and 59C being the most lethal, causing over 75% mortality and triggering a systemic melanization response in the insects. Genomic analysis revealed 175 virulence‐related genes shared across all strains and 16 genes specific to the highly insecticidal ones, including genes for antimicrobial compounds and insect toxins. Mutational analysis confirmed the roles of hydrogen cyanide, 2,4‐diacetylphloroglucinol, pyoluteorin, Fit toxin, and two‐partner secretion systems in <jats:italic>P. protegens</jats:italic> CHA0 insecticidal activity. This strain also exhibited insecticidal effects on adult <jats:italic>T. solanivora</jats:italic> and delayed egg hatching and pupal emergence. In microcosm assays, <jats:italic>P. protegens</jats:italic> CHA0 reduced tuber damage caused by <jats:italic>T. solanivora</jats:italic> larvae by up to 38%. These results suggest that <jats:italic>P. protegens</jats:italic> CHA0 is a promising biocontrol agent, providing a sustainable alternative to chemical pesticides to control <jats:italic>T. solanivora</jats:italic> .","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"183 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145903710","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}