Microbiology-Sgm最新文献

{"title":"Microbial Primer: Bacterial energy metabolism.","authors":"Qonita Afinanisa, Alexander Brooks, Iremide Sanyaolu, Ashwathi Valiyaparambil, Tim W Overton","doi":"10.1099/mic.0.001694","DOIUrl":"10.1099/mic.0.001694","url":null,"abstract":"<p><p>All cells need energy to perform their functions. This primer introduces energy metabolism in bacteria, with a focus on key pathways and examples from model organisms, while acknowledging that bacterial diversity means that species such as <i>Escherichia coli</i> are not always 'typical' in terms of energy metabolism. It finishes by looking at how metabolism underpins important bacterial behaviours.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 4","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13095032/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147730499","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Phages for One Health: regulatory and product life cycle considerations.","authors":"Liberty Duignan, Evelien M Adriaenssens, Rosanna C T Wright, Annette Sansom, Ian MacLeod, Tobi E Nagel, Joshua D Jones, Joanne L Fothergill, Carmen H Coxon","doi":"10.1099/mic.0.001626","DOIUrl":"10.1099/mic.0.001626","url":null,"abstract":"<p><p>There is growing interest in bacteriophage (phage) technologies across the One Health spectrum. The UK Parliament's Science, Technology and Innovation Select Committee recently published the results of its inquiry into 'the antimicrobial potential of bacteriophages' with recommendations on clarity on regulatory matters to support research and innovation. Products developed for different sectors will have different regulatory requirements. Here, we discuss how phage technology is applied across human, veterinary and food sectors, highlighting key regulatory considerations and the technical challenges that must be addressed to assure the quality, safety and efficacy of phage products. We also highlight the potential impact of phages in areas where they are most needed (low- and middle-income countries).</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 4","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13128281/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147787334","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identifying markers of biofilm formation on medical-grade stainless steel as a representative medical device material.","authors":"Gregory G Anderson, Sravya Kovvali, Francis W Dang, Ryan M Singh, Apoorva Vishwakarma, Jon W Weeks, Ruchi Pandey","doi":"10.1099/mic.0.001684","DOIUrl":"10.1099/mic.0.001684","url":null,"abstract":"<p><p>Reusable medical devices are reprocessed between uses, including cleaning and, as necessary, disinfection or sterilization. Healthcare-associated infections have been attributed to reusable medical devices and linked to inadequate reprocessing, which can result in residual soil on the device, insufficient disinfection, microbial resistance to used disinfectants and biofilm-related contamination. These factors can lead to microbial proliferation on and biofouling of reusable medical devices, increasing the risk of patient infection. While there are FDA-recognized standards for cleaning validation (including artificial test soils), there is a lack of standards or guidance documents available to advise on determining whether biofilm has been adequately cleaned off reusable devices after reprocessing. Additionally, relatively few studies report reproducible models of biofilm formation on medical devices or device materials; such models are necessary to begin the identification of the microbial biofilm burden present before and after reprocessing. Moreover, appropriate analytes to quantify that biofilm burden, and the endpoints of those analytes after reprocessing, need to be determined. The study described herein utilized a drip flow reactor (DFR) to develop single-species biofilms of two Gram-negative (<i>Pseudomonas aeruginosa</i> and <i>Klebsiella pneumoniae</i>) and two Gram-positive (<i>Staphylococcus aureus</i> and <i>Enterococcus faecalis</i>) bacterial species that are prone to contaminate medical devices as biofilms. Biofilm was extracted at early and late biofilm stages and then tested for several analytes, including protein, ATP, endotoxin, peptidoglycan and total organic carbon. The levels of these analytes were compared to c.f.u. and metabolic activity to qualitatively compare analyte levels with biofilm burden. The results presented demonstrate that the DFR can be used to model biofilm formation of several medically relevant micro-organisms on stainless steel. Furthermore, the analytical data obtained with this study indicate that the analytes used can be a good starting point for informing the selection of endpoints in future studies that evaluate the efficacy of cleaning and disinfection within the context of biofilm reduction.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 4","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13043183/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147595843","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Atypical catabolite repression of <i>Geobacillus kaustophilus iol</i> operons in the presence of ribose.","authors":"Ken-Ichi Yoshida, Kaho Fukui, Takuma Osawa, Moeka Tsuji, Miyuki Kado-Matsushita, Nao Asahi, Shu Ishikawa, Yuh Shiwa, Hirofumi Yoshikawa","doi":"10.1099/mic.0.001702","DOIUrl":"10.1099/mic.0.001702","url":null,"abstract":"<p><p><i>Geobacillus kaustophilus</i> HTA426 is a thermophilic Gram-positive bacterium that encodes the <i>myo</i>-inositol-inducible <i>iol</i> operons, the products of which form the <i>myo</i>-inositol catabolic pathway. Strain PS8 is a mutant of HTA426 that is defective in <i>myo</i>-inositol catabolism due to constitutive repression of the <i>iol</i> operons. Several spontaneous suppressor mutants of PS8, which restored growth on <i>myo</i>-inositol, were obtained. These suppressors had mutations that may affect the translation of <i>crh</i>. Inclusion of a plasmid-based copy of <i>crh</i> into the suppressor mutants concomitantly restored the repression of the <i>iol</i> operons. PS8 and its suppressor mutants shared a mutated allele of <i>hprK</i>(G268R) that may encode a defective HPr kinase/phosphorylase, which could lead to the accumulation of the phosphorylated form of Crh. Inclusion of a plasmid-based copy of the wild-type <i>hprK</i> gene into PS8 restored the induction of the <i>iol</i> operons. Conversely, inclusion of a plasmid-based copy of <i>hprK</i>(G268R) into HTA426 significantly repressed the <i>iol</i> operons. In HTA426, ribose, rather than glucose, repressed the <i>iol</i> operons. During the growth on ribose, the expression of <i>ptsH</i>, which encodes HPr, was kept at a low level, while that of <i>crh</i> was elevated. Deletion of <i>hprK</i>, <i>ccpA</i> (encoding global regulator CcpA) or the <i>rbs</i> operon (encoding the components for ribose catabolism) abolishes the ribose-induced repression of <i>iol</i> operons. These results suggest an atypical catabolite repression of the <i>iol</i> operons of <i>G. kaustophilus</i> HTA426, where HPrK phosphorylates Crh in the presence of ribose, and the phosphorylated form of Crh cooperates with CcpA to repress the transcription of the <i>iol</i> operons.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 4","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13130090/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147787272","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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 Omp85 family protein, TamA, exhibits characteristics of a suitable drug target against <i>Pseudomonas aeruginosa</i>.","authors":"Rachael Duodu, David J Boocock, Lesley Hoyles, Jack C Leo","doi":"10.1099/mic.0.001674","DOIUrl":"https://doi.org/10.1099/mic.0.001674","url":null,"abstract":"<p><p>The outer membrane (OM) of Gram-negative bacteria is crucial for cell stability and virulence and acts as a permeability barrier. The biogenesis, assembly and regulation of proteins in the OM are, therefore, attractive areas of study that could lead to identifying novel drug targets. The translocation and assembly module (TAM), composed of TamA and TamB, facilitates the insertion of some <i>β</i>-barrel proteins into the OM of <i>Escherichia coli</i> and <i>Klebsiella pneumoniae</i> and has also been implicated in lipid homeostasis. However, its role in <i>Pseudomonas aeruginosa</i> remains mostly uncharacterized. To investigate the TAM's function and drug target potential in <i>P. aeruginosa</i>, we generated both single- and double-gene TAM knockouts and assessed their fitness using competition growth assays against WT strains. The WT significantly outcompeted the TAM mutants, indicating a fitness defect. Proteomic analysis revealed surprisingly similar profiles between WT and the double-knockout strains, while single-knockout strains showed changes in OM proteins and reduced expression of flagellar components consistent with attenuated swimming motility observed in ∆<i>tamA</i>. Single-knockout mutants exhibited differential levels of expression of lipoproteins of the <i>β</i>-barrel assembly machinery, suggesting compensatory OM remodelling. <i>In vivo</i> infection assays using <i>Galleria mellonella</i> larvae demonstrated significantly higher survival rates when infected with TAM mutants, with <i>tamA</i> mutants showing the greatest attenuation in virulence. Our findings demonstrate a role the TAM plays in <i>P. aeruginosa</i> virulence and identify TamA as a potential drug target for the development of new antimicrobial therapies against <i>P. aeruginosa</i>.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 4","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13098762/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147787259","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification of a core set of <i>Campylobacter jejuni</i> flagella modification genes and a reversible non-motile <i>maf3</i> phenotype.","authors":"Lickson Munjoma, Christopher D Bayliss","doi":"10.1099/mic.0.001698","DOIUrl":"10.1099/mic.0.001698","url":null,"abstract":"<p><p>Assembly of flagella filaments in <i>Campylobacter jejuni</i> requires post-translational O-glycosylation of the flagellin proteins with pseudaminic acid, legionaminic acid and related derivatives. This species is unusual as the addition of pseudaminic acid replaces the requirements for toll-like receptor 5 motifs present in most bacterial flagellin proteins. The distribution and functions of the motility accessory factor genes, encoding glycosyltransferases, responsible for the modification of <i>C. jejuni</i> flagellin across this species, are not fully understood. Disruption of these genes can affect autoaggregation, motility, colonization and biofilm formation. Bioinformatic analyses for the presence/absence of biosynthetic and transferase genes were performed across 16,130 <i>C</i>. <i>jejuni</i> genomes for homologues of genes contained in the <i>C. jejuni</i> strain NCTC11168 flagella locus. The presence of four putative transferases - <i>cj1295</i>, <i>maf7</i>, <i>cj1305</i> and <i>cj1306</i> - correlated with pseudaminic acid biosynthetic genes, whereas legionaminic acid biosynthetic genes were correlated with another five <i>maf</i> genes. A full NCTC11168-like <i>maf</i> gene set was present in 42.7% of isolates, with three genes, <i>maf3</i>, <i>maf4</i> and <i>maf5</i>, being present in >80% of isolates. Mutagenesis of <i>maf3</i> in <i>C. jejuni</i> strain NCTC11168 resulted in a reversible, non-motile phenotype. Motile revertants of this mutant had <i>maf4</i> and <i>maf7</i> in the ON phase variation state and/or possessed a single-nucleotide alteration in <i>maf5</i>. These findings are indicative of specific <i>maf</i> genes being responsible for the addition or modification of major flagella glycans in large groups of <i>C. jejuni</i> strains and of redundant or compensatory gene functions.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 4","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13130089/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147787327","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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>Pseudomonas aeruginosa</i> gene expression changes during established biofilm infection in a cystic fibrosis lung model.","authors":"Niamh E Harrington, Freya Allen, Ramón Garcia Maset, Freya Harrison","doi":"10.1099/mic.0.001678","DOIUrl":"10.1099/mic.0.001678","url":null,"abstract":"<p><p>The opportunistic pathogen <i>Pseudomonas aeruginosa</i> forms biofilm infections in the lungs of people with the genetic condition cystic fibrosis (CF) that can persist for decades. There are numerous <i>P. aeruginosa</i> lifestyle changes associated with chronic biofilm infection that are cued by the CF lung environment. These include a loss of virulence, metabolic changes and increased antimicrobial tolerance. We have investigated <i>P. aeruginosa</i> PA14 biofilm infection over 7 days in an <i>ex vivo</i> pig lung (EVPL) model for CF, previously shown to facilitate formation of a clinically relevant <i>P. aeruginosa</i> biofilm structure with expression of key genes comparable to human infection. We have compared <i>P. aeruginosa</i> gene expression between sequential time points: 24 h, 48 h and 7 days post-infection, and investigated tolerance to polymyxins. Our results demonstrate that the EVPL model can maintain a <i>P. aeruginosa</i> biofilm population, which exhibits increased antibiotic tolerance, for at least 7 days. Differential expression of antimicrobial resistance-associated genes was not observed; however, there was significant upregulation of sulphur metabolism and maintenance of a structured biofilm. Our findings demonstrate that 7 days is a viable time point for studying established, chronic biofilm infection in the EVPL model and provide insight into the accompanying gene expression changes.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 3","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12962550/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147357378","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Expression of the VapD protein by <i>Helicobacter pylori</i> during intracellular infection.","authors":"Alejandro Flores-Alanis, Gabriela Delgado, Carlos Santiago-Olivares, María Luisa Escobar-Sánchez, Nayeli Torres-Ramírez, Victor Manuel Luna-Pineda, Armando Cruz-Rangel, Karen Cortés-Sarabia, José Luis Méndez, Fernando Espinosa-Camacho, Alejandro Cravioto, Rosario Morales-Espinosa","doi":"10.1099/mic.0.001683","DOIUrl":"10.1099/mic.0.001683","url":null,"abstract":"<p><p><i>Helicobacter pylori</i> can persist intracellularly, offering protection against the immune system and antimicrobial treatments, which promote chronic infection. Previous studies revealed that the virulence-associated protein D (<i>vapD</i>) gene is transcriptionally induced during <i>H. pylori</i> intracellular infection and was associated with bacterial persistence, as deletion of <i>vapD</i> impairs bacterial intracellular survival. However, whether VapD protein is expressed and localized during intracellular infection had not been demonstrated. The aim of this study was to detect the VapD protein when <i>H. pylori</i> is inside eukaryotic cells. Polyclonal antibodies against VapD and immunofluorescence microscopy were used to detect the VapD expression in co-cultures of <i>H. pylori</i> strain 26695 and AGS cells. The <i>H. pylori</i> strain Tx30a, which lacks the <i>vapD</i> gene, was used as a negative control. VapD expression was detected exclusively in AGS cells infected with strain 26695. Confocal microscopy confirmed the intracellular localization of the VapD signal, which coincided with the localization of <i>H. pylori</i> within AGS cells. In addition, a high proportion of <i>H. pylori</i>-infected AGS cells were positive for VapD signal. Together, these results provide first direct evidence of VapD expression during <i>H. pylori</i> intracellular infection and extend previous transcriptional and genetic studies by confirming VapD production at the protein level, supporting its association with the intracellular state of <i>H. pylori</i>.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 3","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13008275/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147505385","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transplantation of <i>Saccharomyces cerevisiae</i> Rmd9p peptide into mammalian mitochondrial IF2 substitutes for the IF1 function in <i>Escherichia coli</i>.","authors":"Jitendra Singh, Amit Kumar Sahu, Umesh Varshney","doi":"10.1099/mic.0.001689","DOIUrl":"10.1099/mic.0.001689","url":null,"abstract":"<p><p>Mitochondrial translation machinery exhibits similarities with the bacterial translation apparatus. Of the three bacterial translation initiation factors (IF1, IF2 and IF3), two (IF2 and IF3) have homologues in mitochondria (mtIF2 and mtIF3). A high conservation of decoding nucleotides in the ribosomal A-site suggests relevance of IF1-like proteins in mitochondria. The mitochondrial translation machineries have evolved with different solutions for the IF1 function. However, in <i>Saccharomyces cerevisiae</i>, the identity of such a protein remains unknown. Here, based on sequence alignment with human mtIF2, we deduced that Rmd9p may contribute to an IF1-like function in <i>S. cerevisiae</i>. Our genetic analyses show that Rmd9p is required for mitochondrial translation. In addition, we show that a sequence from Rmd9p, pivotal for its mitochondrial function, when inserted into mtIF2, substitutes for both the IF2 and IF1 functions in an established model of <i>Escherichia coli</i>. Interestingly, while the mutations at the critical residues in the Rmd9p peptide compromise the IF1 function, the mutant peptide is still able to support <i>E. coli</i> growth, suggesting that the structure (rather than the precise sequence) of the IF1-like insert domain in mitochondrial IF2 plays a major role in the recognition of the decoding nucleotides in the ribosomal A-site.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 3","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13030852/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147534166","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mucin stimulates the growth of <i>Legionella pneumophila</i>.","authors":"Alexis Vargas, Hunter J Kuhlemeier, Nicholas P Cianciotto","doi":"10.1099/mic.0.001682","DOIUrl":"10.1099/mic.0.001682","url":null,"abstract":"<p><p>Previously, it was demonstrated that a chitinase (ChiA) secreted by the <i>Legionella pneumophila</i> type II secretion system (T2SS) degrades mucin, thereby facilitating bacterial movement through a mucin layer. Here, we discovered that the addition of mucin to a chemically defined medium (CDM) greatly stimulates the growth of <i>L. pneumophila</i>, indicating that the bacterium can very effectively utilize mucin as a food source. This growth-stimulatory effect was evident in broth and agar media and for all WT strains tested. Remarkably, the growth of <i>L. pneumophila</i> on mucin-containing CDM agar rivalled the growth of the bacterium on buffered charcoal yeast extract (BCYE) agar, the standard medium used for cultivating legionellae. A <i>L. pneumophila</i> mutant lacking the T2SS was majorly impaired for growth in mucin-containing CDM, suggesting that exoenzymes are needed for mucin assimilation. In support of this hypothesis, mutants lacking either ChiA or the secreted protease ProA were also impaired for growth in the presence of added mucin. Finally, we observed that <i>L. pneumophila</i>, but not a mutant lacking secreted surfactant, exhibits a marked spreading phenotype (i.e. sliding motility) when grown on CDM agar vs. BCYE agar. However, WT bacteria grown on CDM agar containing mucin did not show this spreading, suggesting that sliding motility is induced under low-nutrient conditions but repressed by mucin byproducts. Taken together, these results provide new insight into the versatility of <i>L. pneumophila</i> physiology and suggest that <i>L. pneumophila</i> may grow well in extracellular spaces in the lungs that contain mucin.</p>","PeriodicalId":49819,"journal":{"name":"Microbiology-Sgm","volume":"172 3","pages":""},"PeriodicalIF":3.5,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12952804/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147327928","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}