PLoS Pathogens最新文献

{"title":"PHD3-VHL axis controls HIV-2 infection through oxygen-dependent hydroxylation and degradation of Vpx.","authors":"Kei Miyakawa, Kiho Tanaka, Yoko Ino, Yayoi Kimura, Taichi Kameya, Fuminori Mizukoshi, Mayuko Nishi, Masaru Yokoyama, Jun Nakabayashi, Masako Nomaguchi, Hironori Sato, Hirokazu Kimura, Hirofumi Akari, Tomoyuki Miura, Akinori Takaoka, Hideki Hasegawa, Tetsuro Matano, Yoji Andrew Minamishima, Akihide Ryo","doi":"10.1371/journal.ppat.1013241","DOIUrl":"10.1371/journal.ppat.1013241","url":null,"abstract":"<p><p>HIV-2 viral protein X (Vpx) plays a pivotal role in antagonizing the host restriction factors, including SAMHD1 and components of the HUSH complex, to facilitate viral replication. However, the regulatory mechanisms controlling Vpx stability remain unclear. In this study, we identify the von Hippel-Lindau (VHL) tumor suppressor as a novel E3 ubiquitin ligase that specifically targets Vpx for proteasomal degradation. Mechanistically, we demonstrate that VHL-mediated degradation depends on the oxygen-dependent hydroxylation of Vpx at proline residue 41 (Pro41), a modification catalyzed by prolyl hydroxylase domain-containing protein 3 (PHD3). Using an integrated approach combining crosslinking mass spectrometry and molecular modeling analyses, we elucidate the structural architecture of the PHD3-Vpx complex, revealing the spatial orientation of the catalytic domain of PHD3 required for Pro41 hydroxylation. Furthermore, we establish the physiological significance of this pathway in human macrophages, where pharmacological inhibition or genetic ablation of VHL or PHD3 enhances HIV-2 infection by facilitating Vpx-mediated SAMHD1 degradation. Collectively, our findings unveil a previously unrecognized oxygen-sensitive regulatory mechanism influencing HIV-2 infection and suggest novel therapeutic strategies targeting Vpx stability through modulation of its prolyl hydroxylation status.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013241"},"PeriodicalIF":5.5,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12201638/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144310668","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The zinc metalloprotein MigC impacts cell wall biogenesis through interactions with an essential Mur ligase in Acinetobacter baumannii.","authors":"Jeanette M Critchlow, Joseph S Rocchio, Melanie C McKell, Courtney J Campbell, Juan P Barraza, Evan S Krystofiak, Erin R Green, Tae Akizuki, Walter J Chazin, Michael S VanNieuwenhze, Timothy L Stemmler, David P Giedroc, Eric P Skaar","doi":"10.1371/journal.ppat.1013209","DOIUrl":"10.1371/journal.ppat.1013209","url":null,"abstract":"<p><p>To colonize and survive in the host, bacterial pathogens like Acinetobacter baumannii must acquire zinc (Zn). To maintain Zn homeostasis, A. baumannii synthesizes proteins of the COG0523 family which are predicted to chaperone Zn to metalloproteins. Bioinformatic tools identified A. baumannii A1S_0934 as a COG0523 protein, and yeast two-hybrid screening revealed that MurD, an essential muramyl ligase, interacts with A1S_0934. As such, we have named A1S_0934 MurD interacting GTPase COG0523 (MigC). Here we show that MigC is a GTPase whose activity is stimulated upon Zn coordination to a characteristic CxCC (C = Cys; x = Leu/Ile/Met) motif to form a S3(N/O) complex. MigC-deficient strains (ΔmigC) display sensitivity to Zn depletion and exhibit altered cell wall architecture in vitro. Biochemical and functional assays confirm the MigC-MurD interaction, which inhibits the catalytic activity of MurD. CRISPRi knockdowns of murD reduce A. baumannii fitness and increase filamentation during Zn depletion, a phenotype reversed in ΔmigC strains, suggesting that MigC also inhibits MurD activity in cells. ΔmigC cells are elongated and sensitized to ceftriaxone, a cephalosporin antibiotic, consistent with decreased cell wall integrity. The ΔmigC strain has reduced ability to colonize in a murine model of pneumonia highlighting the importance of the MigC-MurD interaction induced by A. baumannii infection. Together these data suggest that MigC impacts cell wall biogenesis, in part through interactions with MurD, emphasizing the importance of MigC and MurD to the survival and pathogenicity of A. baumannii while expanding the potential functions of the COG0523 family of enzymes.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013209"},"PeriodicalIF":5.5,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12208494/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144310670","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"IFN alpha inducible protein 27 (IFI27) acts as a positive regulator of PACT-dependent PKR activation after RNA virus infections.","authors":"Darío López-García, Vanessa Rivero, Laura Villamayor, Marta L DeDiego","doi":"10.1371/journal.ppat.1013246","DOIUrl":"10.1371/journal.ppat.1013246","url":null,"abstract":"<p><p>Protein kinase R (PKR) expression is induced by interferons. This protein is activated by double-stranded (ds) RNAs or RNAs containing duplex regions, produced after different stimuli, such as after viral infections, leading to the phosphorylation of the eukaryotic translation initiation factor 2α (eIF2α), and subsequently inhibiting cellular and viral protein translation. This function may lead to different effects such as to impairing the replication of RNA viruses by inhibiting viral protein translation, and to modulating the innate immune responses after viral infections by affecting the translation of effector proteins. In this work, we identify, for the first time, an interaction of IFN alpha inducible protein 27 (IFI27) with PKR-activating protein (PACT or PRKRA) and with PKR, showing that the interaction of IFI27 with PACT is likely mediated by dsRNAs or RNAs containing duplex regions, and that the interaction of IFI27 with PKR is PACT-dependent. Interestingly, using IFI27 knocked-down, knocked-out and overexpressing tumour-derived, established cells, we show that these interactions trigger a potentiation of the activity of PKR and, therefore, a decrease in protein translation. Moreover, we find that IFI27 increases PKR function in cells infected with different RNA viruses such as Severe Acute Respiratory virus 2 (SARS-CoV-2), and Vesicular Stomatitis virus (VSV), and in cells transfected with the dsRNA analog poly(I:C), suggesting a broad effect of IFI27 on PKR activation. Moreover, we show that IFI27 expression increases the formation of stress granules (SGs) at the cell cytoplasm, correlating with the increased PKR activation mediated by IFI27, as it has been shown that the translational arrest induced by activated PKR leads to the formation of SGs. Mechanistically, we describe that this ability of IFI27 to activate PKR is dependent on its interaction with PACT. Further understanding of the regulation of PKR activity will allow us to develop new antiviral drugs to modulate this signalling axis, which is crucial in RNA virus infections.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013246"},"PeriodicalIF":5.5,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12204625/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144310667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"APOE protects against severe infection with Mycobacterium tuberculosis by restraining production of neutrophil extracellular traps.","authors":"Dong Liu, Dat Mai, Ana N Jahn, Tara A Murray, John D Aitchison, Benjamin H Gern, Kevin B Urdahl, Alan Aderem, Alan H Diercks, Elizabeth S Gold","doi":"10.1371/journal.ppat.1013267","DOIUrl":"10.1371/journal.ppat.1013267","url":null,"abstract":"<p><p>Mice lacking apolipoprotein E (APOE, Apoe-/- mice) on a high cholesterol (HC) diet are highly susceptible to infection with Mycobacterium tuberculosis (Mtb) but the underlying immune dysregulation has been unclear. While neutrophils are often the predominant cell type in the lungs of humans with severe tuberculosis (TB), they are relatively scarce in the lungs of some strains of mice that are used to study the disease. The neutrophil levels in the lungs of Mtb-infected Apoe-/- HC mice are very high, and thus studies in this model offer the opportunity to examine the role of specific neutrophil functions in the pathology of severe TB. We determined that depleting neutrophils, depleting plasmacytoid dendritic cells (pDCs), or blocking type I interferon signaling improved the outcome of TB in Apoe-/- HC mice. We also demonstrated that blocking the activation of peptidylarginine deiminase 4 (PAD4), an enzyme critical to NET formation, leads to fewer NETs in the lungs and dramatically improves the outcome of TB in Apoe-/- HC mice without affecting the number of neutrophils in the lung. We found that the transcriptional profile of neutrophils in Mtb-infected Apoe-/- HC mice is biased towards a state that resembles the \"N2\" phenotype that has been defined in cancer models and has been implicated in matrix degradation and tissue destruction. Our observations strongly suggest that the state of the neutrophil when it encounters the Mtb-infected lung is one of the main drivers of severe disease and implies that targeted interventions that alter specific states or functions, such as the production of NETs, may improve outcome while preserving sufficient capacity for host-defense.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013267"},"PeriodicalIF":5.5,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12201663/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144310655","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Toxoplasma gondii infection of neurons alters the production and content of extracellular vesicles directing astrocyte phenotype and contributing to the loss of GLT-1 in the infected brain.","authors":"Emily Z Tabaie, Ziting Gao, Nala Kachour, Arzu Ulu, Stacey Gomez, Zoe A Figueroa, Kristina V Bergersen, Wenwan Zhong, Emma H Wilson","doi":"10.1371/journal.ppat.1012733","DOIUrl":"10.1371/journal.ppat.1012733","url":null,"abstract":"<p><p>Toxoplasma gondii (T. gondii), a prolific protozoan parasite, forms cysts within neurons of the central nervous system that maintain infection for the lifetime of the host. Astrocytes are fundamental to neuronal health by providing nutrients and structural support and help regulate neurotransmitters by continuous communication with neurons. It is not yet known how infection and the presence of intracellular cysts, disrupts the crucial relationship between these cells. Extracellular vesicles (EVs) function in intracellular communication and can contain proteins, lipids, DNA, miRNA, and other RNA subtypes. EVs are produced by all cells and play an important role in neuronal-astrocyte interactions, including the regulation of glutamate receptors on astrocytes. Previous work has demonstrated that Toxoplasma infection reduces astrocytic expression of the primary glutamate transporter, GLT-1. Here we tested if cyst infection of neurons alters the production and content of EVs. EVs were isolated from uninfected and infected primary murine cortical neurons and their size, concentration, and characterization were confirmed with nanoparticle tracking analysis (NTA), transmission electron microscopy (TEM), ELISA, western blot, liquid chromatography (LC)-mass spectrometry (MS)/MS, and microRNA sequencing. Analysis reveals that infection of neurons reduced neuronal production of EVs and altered their protein and miRNA content. In addition to changes in host protein content, EVs from infected neurons contained the Toxoplasma proteins GRA1, GRA2, GRA7, MAG1 and MAG2. Following incubation of neuronal EVs with primary astrocytes, GRA7 protein could be observed within intracellular EVs and the nuclei of GRA7 + EV-containing cells. EVs from infected neurons altered gene expression of astrocytes resulting in an increase in pro-inflammatory transcriptional signatures, along with a downregulation of GLT-1 protein expression with similar transcriptional changes found in astrocytes in vivo. These results demonstrate the ability of a parasitic infection in the brain to alter EV production and the fundamental communication between neurons and astrocytes.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1012733"},"PeriodicalIF":5.5,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12193631/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144310671","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Env from EIAV vaccine delicately regulates NLRP3 activation via attenuating NLRP3-NEK7 interaction.","authors":"Xing Guo, Cong Liu, Yuhong Wang, Hongxin Li, Saiwen Ma, Lei Na, Huiling Ren, Yuezhi Lin, Xiaojun Wang","doi":"10.1371/journal.ppat.1012772","DOIUrl":"10.1371/journal.ppat.1012772","url":null,"abstract":"<p><p>The current equine infectious anemia virus (EIAV) vaccine causes attenuation of the inflammatory response to an appropriate level, compared to that produced by virulent EIAV. However, how the EIAV vaccine finely regulates the inflammatory response remains unclear. Using a constructed NLRP3-IL-1β screening system, viral proteins from two EIAV strains (the attenuated vaccine and its virulent mother strain) were examined separately. Firstly, EIAV-Env was screened to direct binding P2X7 (R) with notable K+ efflux trans-cellularly. Secondly, EIAV-Env was found to bind NLRP3 and/or NEK7 to trigger aggregation of NLRP3-NEK7 to form NLRP3-NEK7 complex in cells. Comparison of the two strains, we observed a significant reduction on vaccine-Env-initiated NLRP3-NEK7 complex formation, with no difference in Env triggering P2X7 (R)-mediated ion fluxes. Thirdly, reciprocally mutation on four stable varied amino acids between two strains produced an anticipated outcome on NLRP3-IL-1β-axis activation. As the attenuated vaccine was shown evolved as a natural quasispecies of the virulent EIAV, its precise and adaptable regulation via spatial proximity-dependent intracellular activation might present a \"win-win\" virus-host adaption, offering an alternative strategy on envelop-based vaccines development.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1012772"},"PeriodicalIF":5.5,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12187018/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144310657","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Circovirus Rep evades immune restriction by disrupting cGAS oligomerization and phase separation.","authors":"Hongyan Yin, Zhenchao Zhao, Ye Yuan, Minjie Li, Lvye Chai, Weiyu Qu, Yan Ya, Haiwei Wang, Xin Li","doi":"10.1371/journal.ppat.1013244","DOIUrl":"10.1371/journal.ppat.1013244","url":null,"abstract":"<p><p>Cyclic GMP-AMP synthase (cGAS) is a key sensor of double-stranded DNA (dsDNA), initiating oligomerization and phase separation to drive immune responses against pathogens and endogenous damage. Porcine circovirus (PCV) induces immunosuppression, heightening susceptibility to secondary infections, but the underlying mechanisms remain unclear. Here, we report PCV type 2d (PCV2d) infection fails to induce type I interferons (IFN-I) and significantly suppresses IFN-I production upon poly (dA:dT) stimulation in a dose-dependent manner. Mechanistically, the replication-related protein (Rep) proteins of PCV2, PCV3 and PCV4 inhibit cGAS-mediated IFN-I induction by competitively binding dsDNA, thereby disrupting cGAS oligomerization and phase separation. Interestingly, Rep also suppresses mitochondria DNA-induced cGAS activation. We further identify Rep residues Q12 and R199-W202 as key regions facilitating dsDNA binding. Our findings reveal a previously unrecognized mechanism by which circovirus Rep antagonizes cGAS activation, providing new insights into PCV-induced immunosuppression.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013244"},"PeriodicalIF":5.5,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12201654/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144310656","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural exposure of different microtubule binding domains determines the propagation and toxicity of pathogenic tau conformers in Alzheimer's disease.","authors":"Lenka Hromadkova, Chae Kim, Tracy Haldiman, Mohammad Khursheed Siddiqi, Krystyna Surewicz, Kiley Urquhart, Dur-E-Nayab Sadruddin, Lihua Peng, Xiongwei Zhu, Witold K Surewicz, Mark L Cohen, Mark R Chance, Rohan de Silva, Janna Kiselar, Jiri G Safar","doi":"10.1371/journal.ppat.1012926","DOIUrl":"10.1371/journal.ppat.1012926","url":null,"abstract":"<p><p>Deposits of misfolded tau proteins are leading indicators of cognitive decline in Alzheimer's disease (AD), and our recent data implicate distinctly misfolded conformers of the tau protein with high seeding potency in rapid progression. We considered prion-like templated propagation of misfolding in neurons as an underlying mechanism and derived sensitive conformational assays to test this concept and identify critical structural drivers. Using novel photochemical hydroxylation monitored with a panel of Europium-labeled monoclonal antibodies, we investigated the structural organization of different microtubule binding domains (MTBDs) in brain-derived tau conformers in AD with different progression rates. We analyzed the impact of structural organization of different MTBDs on seeding potency in vitro and in primary neurons, and on the propagation rate of tau misfolding, compartmentalization, cytotoxicity, and calcium homeostasis in neuronally differentiated SH-SY5Y cells. Within the extensive inter-individual structural variability in all MTBDs and C-terminal tails, the most significant driver of seeding potency and propagation of tau protein misfolding in both in vitro seeding assays and in neuronal cultures was the structural exposure of the fourth MTBD (R4). In contrast, the major driver of calcium influx induced in neurons by the accumulation of misfolded tau was the structural exposure of the R1 domain. The data provide compelling evidence for a major diversity in the structural organization of MTBDs of misfolded AD brain-derived tau protein and implicate the structural exposure of distinct domains in different pathogenetic steps of AD - R4 tau domain in progression rate, and R1 domain in variable synaptic toxicity of misfolded tau, and thus in cognitive decline.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1012926"},"PeriodicalIF":5.5,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12187016/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144289703","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"White spot syndrome virus immediate-early protein (wsv100) antagonizes the NF-κB pathway to inhibit innate immune response in shrimp.","authors":"Bang Xiao, Fang Kang, Qianqian Li, Junming Pan, Yue Wang, Jianguo He, Chaozheng Li","doi":"10.1371/journal.ppat.1012828","DOIUrl":"10.1371/journal.ppat.1012828","url":null,"abstract":"<p><p>Viruses have evolved sophisticated strategies to evade host immune defenses, often targeting conserved signaling pathways. In shrimp, the NF-κB signaling pathway is crucial for antiviral immunity, yet its regulation during White Spot Syndrome Virus (WSSV) infection remains poorly understood. Here, we identify and characterize wsv100, an immediate-early (IE) protein of WSSV, as a key antagonist of the NF-κB pathway. wsv100 interacts directly with the transcription factor Dorsal, preventing Dorsal phosphorylation by Pelle kinase. This inhibition suppresses Dorsal's nuclear translocation and downstream expression of antimicrobial peptides (AMPs), essential for antiviral defense. Knockdown of wsv100 reduced WSSV replication, increased Dorsal phosphorylation, and enhanced AMP expression, leading to higher survival rates in infected shrimp. Conversely, wsv100 overexpression promoted WSSV replication and AMPs suppression. These findings reveal a novel immune evasion mechanism by which WSSV subverts the NF-κB pathway and highlight the evolutionary arms race between hosts and viruses. This study enhances our understanding of host-virus interactions and offers potential targets for antiviral strategies in shrimp aquaculture.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1012828"},"PeriodicalIF":5.5,"publicationDate":"2025-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12187017/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144286876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The rise of fungal G-protein coupled receptors in pathogenesis and symbiosis.","authors":"Max Heinen, Hanna Rovenich, Florian Altegoer","doi":"10.1371/journal.ppat.1013212","DOIUrl":"10.1371/journal.ppat.1013212","url":null,"abstract":"","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 6","pages":"e1013212"},"PeriodicalIF":5.5,"publicationDate":"2025-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12161586/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144286874","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}