mSphere最新文献

{"title":"Damage response signaling by the extracellular adenosine pathway: control of infection outcome during host aging.","authors":"Manmeet Bhalla, Shaunna R Simmons, Alexsandra Lenhard, Anagha Betadpur, Michael C Battaglia, Elsa N Bou Ghanem","doi":"10.1128/msphere.00640-23","DOIUrl":"10.1128/msphere.00640-23","url":null,"abstract":"<p><p>In response to damage triggered by various stimuli including infections, ATP is released from damaged cells and converted to adenosine in the extracellular space by the ectonucleotidases CD39 and CD73. Extracellular adenosine is an immune modulatory molecule that signals via four G-protein receptors: A1, A2A, A2B, and A3, which can have opposing downstream effects on immune responses. In this minireview, we follow up on our mSphere of Influence commentary that focused on the A2B receptor (2019) to give a broader view of the role of the extracellular adenosine signaling pathway in host defense against infections. Studies demonstrate that extracellular adenosine serves as a key signaling molecule regulating the balance between effective pathogen clearance and immunopathology during infection. Extracellular adenosine displays dose- and time-dependent roles during infection, with individual adenosine receptors playing specific roles in controlling immune responses. Age-driven changes in this pathway contribute to the increased susceptibility of older hosts to certain infections, although there are several key unanswered questions about the role of the extracellular adenosine pathway in immunosenescence. Clinical and translational findings reveal a role for extracellular adenosine production and signaling in infections in humans, and there have been recent advances, but several ongoing challenges remain in pharmacologically targeting this pathway to reshape host immune responses.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0064023"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12487761/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144962222","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":"<i>De novo</i> generation of viruses in animals: from infection models to vaccine development.","authors":"Maxime Cochin, Jean-Sélim Driouich, Léa Luciani, Antoine Nougairède","doi":"10.1128/msphere.00742-24","DOIUrl":"10.1128/msphere.00742-24","url":null,"abstract":"<p><p>Reverse genetics is a valuable research tool in the field of virology with numerous applications. Primarily employed to recover viral strains <i>in vitro</i>, these approaches have also been used to generate viral strains directly in animals. This review presents a historical and technical overview of publications describing the rescue of viruses from injection of nucleic acids directly into animals since the 1950s. The injection of purified or cloned viral genomes <i>in vivo</i> has enabled the generation of many pathogens in a wide range of animal models. Recent advances in the delivery process of nucleic acid into cells have also contributed to this field of virology research, which currently focuses on creating a new generation of vaccines called DNA-launched live attenuated vaccines (LAVs). This new approach simplifies the administration of existing or newly created LAV strains, while providing better control of the inoculated material.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0074224"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482153/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144817189","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":"mSphere of Influence: From pixels to parasite insight-cryo-EM is rewiring apicomplexan cell biology.","authors":"Li-Av Segev-Zarko","doi":"10.1128/msphere.00231-25","DOIUrl":"10.1128/msphere.00231-25","url":null,"abstract":"<p><p>Li-av Segev Zarko studies the nanomachines that apicomplexan parasites deploy to break into host cells. In this mSphere of Influence article, she reflects on how breakthrough cryo-electron microscopy studies published between 2018 and 2021 reshaped her view of what the ever-advancing field of structural biology can reveal about molecular and cellular parasitology.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0023125"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482150/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144817203","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":"mSphere of Influence: Population-level thinking to unravel microbial pathogenicity.","authors":"Amelia E Barber","doi":"10.1128/msphere.00588-24","DOIUrl":"10.1128/msphere.00588-24","url":null,"abstract":"<p><p>Amelia E. Barber works in the field of fungal genomics and pathogenesis. In this mSphere of Influence article, she reflects on how the paper \"Strain heterogeneity in a non-pathogenic <i>Aspergillus</i> fungus highlights factors associated with virulence\" from the group of Antonis Rokas changed her view on the binary characterization of microbes as pathogens or non-pathogens. The work highlights the overlapping virulence traits shared between the two groups and encourages the use of a population-based framework. To understand the full spectrum of microbial pathogenic potential, virulence phenotypes are characterized across a strain population of isolates from \"pathogenic\" species and closely related \"non-pathogens,\" in this case revealing a continuum rather than a clear distinction.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0058824"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482144/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144822116","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":"A dual-mechanism antimicrobial peptide with antimutagenic activity targets the replisome and induces cell envelope stress.","authors":"Amanda Holstad Singleton, Olaug Elisabeth Torheim Bergum, Jana Scheffold, Synnøve Brandt Ræder, Lilja Brekke Thorfinnsdottir, Lisa Marie Røst, Caroline Krogh Søgaard, Per Bruheim, Marit Otterlei","doi":"10.1128/msphere.00068-25","DOIUrl":"10.1128/msphere.00068-25","url":null,"abstract":"<p><p>To combat the growing threat of multidrug-resistant bacteria, we need to develop novel antibiotics with unique modes of action. This study investigates the antibacterial properties of BTP-001 toward <i>Escherichia coli</i>. BTP-001 targets the β-clamp subunit of the DNA Pol III holoenzyme and is composed of the binding motif APIM linked to a cell-penetrating part composed of 11 arginine residues (R11). Our data indicate that R11 facilitates energy-dependent transport of BTP-001 across the cell membrane, possibly via iron transport systems such as the TonB system. The full-length BTP-001 peptide rapidly disturbs membrane integrity, inducing expression and activation of the Cpx cell envelope stress response. This response likely triggers the production of reactive oxygen species (ROS), contributing to the rapid bactericidal effect, as evidenced by increased short-term survival by addition of a ROS scavenger. Furthermore, this study confirms that BTP-001 targets DNA replication and reduces resistance development by inhibiting translesion synthesis. In addition, our data suggest that the β-clamp is associated with ribosomal complexes and that BTP-001 disrupts translational processes. In conclusion, BTP-001 exhibits a multifaceted mode of action, which strengthens its potential as a novel therapeutic drug against antibiotic-resistant bacteria.IMPORTANCEAs antimicrobial resistance (AMR) increases, the world needs new antibiotics with new modes of action to avoid cross-resistance. In this study, we investigated how BTP-001, a novel cell-penetrating peptide that contains a protein-binding motif for the essential DNA replication protein β-clamp, kills bacteria. We demonstrate that BTP-001 has a dual mode of action in which it i) targets the β-clamp and inhibits replication and mutagenesis and ii) disrupts the bacterial cell envelope, causing ROS accumulation and rapid cell death. In addition, our data indicate that BTP-001 affects translation, suggesting that the β-clamp may have unknown roles beyond replication. Our data also suggest that the bacterial import of BTP-001, via the cell-penetrating part of the peptide, is dependent on active transport and involves iron uptake mechanisms. BTP-001 has many properties that could be useful for further development as a new antibiotic.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0006825"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482183/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144962287","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":"KilR of <i>E. coli</i> Rac prophage is a dual inhibitor of bacterial cell division and elongation machineries.","authors":"Anusha Marepalli, Muruganandam Nandhakumar, Sutharsan Govindarajan","doi":"10.1128/msphere.01029-24","DOIUrl":"10.1128/msphere.01029-24","url":null,"abstract":"<p><p>Bacterial cryptic prophages not only encode genes that reduce the viability of the host upon induction but also contribute to host survival during stressful conditions. Rac is a cryptic prophage of <i>Escherichia coli</i>, and it encodes a toxic protein KilR, which causes morphological defects to the host. However, the mechanistic basis of its action is not well understood. In this study, we provide evidence that KilR is a dual inhibitor that affects cell division and cytoskeletal organization. We show that KilR expression is highly toxic, as demonstrated previously, and its predicted C-terminal unstructured region plays a crucial role in its function via a length-dependent manner. Low levels of KilR expression lead to cell filamentation and disruption of Z-rings, while high levels result in rod-shaped defects and mislocalization of the MreB cytoskeletal protein. Using fluorescent fusions, we observed that KilR is diffusively localized in the cytoplasm. When MreBCD proteins are overexpressed, KilR co-localizes with them, forming membrane-associated filaments, indicating a physical association. However, overexpressed MreBCD proteins do not alleviate the KilR-associated growth defect, unlike FtsZ. Finally, we present evidence that chromosomal KilR contributes to the co-inhibition of FtsZ and MreB localization in response to oxidative stress. Our data indicate that KilR inhibits MreB-associated cytoskeletal system, in addition to its effect on FtsZ-associated cell division system. We propose that the dual inhibition activity of KilR contributes to its high level of toxicity and to its function in SOS-independent DNA damage tolerance during oxidative stress.IMPORTANCEKilR is a Rac cryptic prophage-encoded toxic protein, which contributes to host survival during oxidative stress conditions. It is known to inhibit cell division by targeting the tubulin homolog, FtsZ. In this study, we show that KilR affects FtsZ-mediated cell division and MreB-mediated cell elongation. The simultaneous inhibition of cell division and cell elongation is known to be crucial for bacterial survival during stress conditions like oxidative stress. Our study identifies KilR as a cell division and cell elongation inhibitor, offering insights into how bacterial-phage coevolution drives the emergence of cryptic prophage elements, with specific genes enhancing bacterial fitness.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0102924"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482147/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144799735","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":"GCN5a is a telomeric lysine acetyltransferase whose loss primes <i>Toxoplasma gondii</i> for latency.","authors":"Vishakha Dey, Michael J Holmes, Sandeep Srivastava, Emma H Wilson, William J Sullivan","doi":"10.1128/msphere.00026-25","DOIUrl":"10.1128/msphere.00026-25","url":null,"abstract":"<p><p><i>Toxoplasma gondii</i> is a protozoan parasite that causes persistent infection in warm-blooded vertebrates by undergoing differentiation from a replicative stage (tachyzoites) to a latent encysted stage (bradyzoites). Stage differentiation is critical for transmission and pathogenesis and relies on gene regulation driven by a network of transcription and epigenetic factors. We previously found in non-cystogenic type I RH strain parasites that the lysine acetyltransferase (KAT), GCN5a, is dispensable in tachyzoites but required to upregulate stress-response genes, suggesting a link with bradyzoite conversion. To address this possibility, we generated endogenously tagged GCN5a parasites and a genetic knockout in cystogenic type II Pru strain. We show that GCN5a protein, but not mRNA, increases during differentiation and complexes with unique protein partners, most of which contain AP2 domains. Pru strain tachyzoites lacking GCN5a augment bradyzoite-specific gene expression in the absence of stress. Loss of <i>GCN5a</i> slowed tachyzoite replication and heightened sensitivity to bradyzoite conversion but resulted in smaller cyst sizes compared to wild type. Using CUT&Tag, we delineated the chromosomal occupancy of GCN5a relative to the essential KAT, GCN5b. While GCN5b localizes to coding regions, GCN5a surprisingly localizes exclusively to telomeres. These findings suggest that the loss of GCN5a leads to telomere dysfunction, which slows replication and promotes the transition to latency.IMPORTANCE<i>Toxoplasma gondii</i> is a single-celled parasite that persists in warm-blooded hosts, including humans, because it converts into latent tissue cysts. Switching from its replicating form into dormant cysts is a tightly regulated process that involves epigenetic factors such as lysine acetyltransferases GCN5a and GCN5b. This study is the first to examine the role of GCN5a in a cyst-forming <i>Toxoplasma</i> strain. We found that GCN5a protein, but not mRNA, increases during cyst development. Additionally, parasites lacking GCN5a replicate more slowly and are quicker to form cysts when stressed. We show that GCN5a and GCN5b work in different multi-protein complexes and localize to different areas of the genome; while GCN5b targets promoters of gene coding regions, GCN5a is exclusively found at telomeric regions. Our findings suggest a novel role for GCN5a in telomere biology that, when depleted, produces a fitness defect that favors development of latent stages.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0002625"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482187/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144962467","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":"Dissecting antimicrobial logic: species-specific strategies for intracellular pathogen defense.","authors":"Bryan D Bryson","doi":"10.1128/msphere.00091-25","DOIUrl":"10.1128/msphere.00091-25","url":null,"abstract":"<p><p>Control of intracellular pathogens is a critical element of host defense. Defining the molecular mechanisms by which the host restricts or eliminates these pathogens may inform the development of novel immunotherapeutics and antimicrobial strategies, particularly in the face of rising antibiotic resistance. In parallel, understanding how pathogens subvert these immune responses may yield new approaches to disrupt virulence rather than viability. Yet, the precise mechanisms by which primates-and especially humans-achieve intracellular pathogen control remain poorly understood. Five years ago, I reflected on the complexity of interferon-induced control of <i>Legionella pneumophila</i> in a murine infection model. In this review, I revisit those questions considering emerging evidence, highlighting how cross-species comparisons and context-specific immune programs are reshaping our understanding of host-pathogen interactions and the logic of antimicrobial defense.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0009125"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482154/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145030296","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":"Investigation of the global translational response to oxidative stress in the model archaeon <i>Haloferax volcanii</i> reveals untranslated small RNAs with ribosome occupancy.","authors":"Emma Dallon, Haley M Moran, Sadhana R Chidambaran, Arman Kian, Betty Y H Huang, Stephen D Fried, Jocelyne DiRuggiero","doi":"10.1128/msphere.00343-25","DOIUrl":"10.1128/msphere.00343-25","url":null,"abstract":"<p><p>Oxidative stress induces a wide range of cellular damage, often causing disease and cell death. While many organisms are susceptible to the effects of oxidative stress, haloarchaea have adapted to be highly resistant. Several aspects of the haloarchaeal oxidative stress response have been characterized; however, little is known about the impacts of oxidative stress at the translation level. Using the model archaeon <i>Haloferax volcanii</i>, we performed RNA-seq and ribosome profiling (Ribo-seq) to characterize the global translation landscape during oxidative stress. We identified 281 genes with differential translation efficiency (TE). Downregulated genes were enriched in ribosomal and translation proteins, in addition to peroxidases and genes involved in the TCA cycle. We also identified 42 small noncoding RNAs (sRNAs) with ribosome occupancy. Size distributions of ribosome footprints revealed distinct patterns for coding and noncoding genes, with 12 sRNAs matching the pattern of coding genes, and mass spectrometry confirming the presence of seven small proteins encoded by these sRNAs. However, the majority of sRNAs with ribosome occupancy had no evidence of coding potential. Of these ribosome-associated sRNAs, 12 had differential ribosome occupancy or TE during oxidative stress, suggesting that they may play a regulatory role during the oxidative stress response. Our findings on ribosomal regulation during oxidative stress, coupled with potential roles for ribosome-associated noncoding sRNAs and sRNA-derived small proteins in <i>H. volcanii</i>, revealed additional regulatory layers and underscored the multifaceted architecture of stress-responsive regulatory networks.IMPORTANCEArchaea are found in diverse environments, including as members of the human microbiome, and are known to play essential ecological roles in major geochemical cycles. The study of archaeal biology has expanded our understanding of the evolution of eukaryotes, uncovered novel biological systems, and revealed new opportunities for applications in biotechnology and bioremediation. Many archaeal systems, however, remain poorly characterized. Using <i>Haloferax volcanii</i> as a model, we investigated the global translation landscape during oxidative stress. Our findings expand current knowledge of translational regulation in archaea and further illustrate the complexity of stress-responsive gene regulation.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0034325"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482152/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145015820","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":"Characterization of PPE19 as a novel mediator of <i>Mycobacterium tuberculosis</i>-macrophage interactions.","authors":"Christopher J De Voss, Sean N Riek, Miljan Stupar, Lendl Tan, Brian M Forde, Nicholas P West","doi":"10.1128/msphere.00036-25","DOIUrl":"10.1128/msphere.00036-25","url":null,"abstract":"<p><p><i>Mycobacterium tuberculosis</i> (Mtb) is a highly adapted human pathogen capable of manipulating host immunity. This study demonstrates that PPE19, a member of the PE/PPE protein family, facilitates Mtb adhesion to, and invasion of murine macrophages. PPE19-coated microspheres showed enhanced uptake by macrophages compared to control beads, while Mtb overexpressing <i>ppe19</i> (Rv1361c) was phagocytosed at a significantly greater rate than WT Mtb. <i>ppe19</i> is identified as pH responsive and displays reduced expression following macrophage entry. CRISPR interference-mediated knockdown of two highly related PPE proteins, <i>ppe18</i> (Rv1196) and <i>ppe60</i> (Rv3478), revealed an additive reduction in Mtb's ability to invade host macrophages, indicating a potential functional relationship. Furthermore, the absence of an <i>in vivo</i> phenotype following murine infection with a <i>ppe19</i> knockout strain suggests functional redundancy within this PPE protein family. Finally, PE13 has been identified here as a binding partner for PPE19, characterizing another relationship presumed important for successful PPE secretion. These findings reveal PPE19 as a secreted effector protein used by Mtb to modulate important early interactions with the innate immune system, enhancing entry into host macrophages.IMPORTANCETuberculosis remains a leading infectious disease killer worldwide, with approximately one-quarter of the global population infected with <i>Mycobacterium tuberculosis</i> (Mtb). Understanding how this pathogen initially establishes infection is crucial for developing more effective vaccines and treatments. This study identifies PPE19, a previously uncharacterized bacterial protein, as a key factor that helps Mtb invade and colonize human immune cells called macrophages during the earliest stages of infection. The research shows that PPE19 acts like a molecular \"key\" that facilitates bacterial entry into host cells but is then downregulated once the bacteria are safely inside. Importantly, PPE19 belongs to a family of similar proteins that can compensate for each other, explaining why targeting individual members may not be sufficient for treatment. These findings provide new insights into tuberculosis pathogenesis and suggest that early infection factors like PPE19 could serve as targets for next-generation vaccines designed to prevent initial infection rather than just disease progression.</p>","PeriodicalId":19052,"journal":{"name":"mSphere","volume":" ","pages":"e0003625"},"PeriodicalIF":3.1,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12482190/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144817202","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}