ACS Infectious Diseases最新文献

{"title":"Activity Refinement and Property Assessment of Peptidomimetics with Potent Antimalarial Activity That Target Plasmepsin V","authors":"Gregory L. Adams,&nbsp;Madeline G. Dans,&nbsp;Qingmiao Zhou,&nbsp;Wenyin Su,&nbsp;Anna Ngo,&nbsp;Kate E. Jarman,&nbsp;Maria V. Fawaz,&nbsp;Michael J. Kelly, III,&nbsp;John A. McCauley,&nbsp;David B. Olsen,&nbsp;Justin A. Boddey,&nbsp;Alan F. Cowman,&nbsp;Brad E. Sleebs","doi":"10.1021/acsinfecdis.6c00314","DOIUrl":"10.1021/acsinfecdis.6c00314","url":null,"abstract":"<p>Plasmepsin V is an essential aspartyl protease that cleavesthe <em>Plasmodium</em> export element in proteins targetedfor exportfrom <em>Plasmodium</em> parasites into the host red bloodcell. Substrate-mimicking peptidomimetics have been developed thatpotently inhibit plasmepsin V but show modest parasite activity. Toadvance these inhibitors, we optimized their potency by introducinga 2-chloro aryl group at P₂ and an <em>N</em>-terminalsulfonamide that yielded WM960, which showed markedly improved plasmepsinV inhibition while retaining high selectivity over plasmepsin IX andX and human aspartyl proteases. WM960 also demonstrated enhanced activityagainst asexual blood-stage parasites and effectively suppressed proteinexport. However, WM960 displayed low metabolic stability and limitedsystemic exposure in mice, highlighting the need to improve pharmacokineticproperties in future development of peptidomimetic plasmepsin V targetedantimalarials.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3114–3126"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943840","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fatty Acid Biosynthesis Inhibitors─Fabimycin and Triclosan─Trigger Distinct Resistance Mutations in FabI and Potently Kill Gram-Negative Pathogens","authors":"Brett N. Cain,&nbsp;James E. Kent,&nbsp;Marinela Elane,&nbsp;John D. Williams,&nbsp;Myung Ryul Lee,&nbsp;Gee W. Lau,&nbsp;Paul J. Hergenrother,&nbsp;Andrei L. Osterman","doi":"10.1021/acsinfecdis.6c00339","DOIUrl":"10.1021/acsinfecdis.6c00339","url":null,"abstract":"<p>In an effort to developefficacious antibacterials thatengagetargets for which there is no preexisting resistance, inhibition ofthe enoyl-acyl carrier protein reductase FabI has shown promise, withtriclosan and fabimycin as representative members of the two majordrug classes that show activity against important bacterial pathogens.Here, we use a morbidostat and whole-genome sequencing approach tocomprehensively evaluate the resistance profiles that arise in pathogenicbacteria in response to these FabI inhibitors. When assessed against <em>E. coli</em>, fabimycin and triclosan were found to induceprimarily nonoverlapping resistance profiles, leading to minimal cross-resistancebetween the two compounds. Furthermore, <em>in vivo</em> evaluationof the prominent resistant mutants indicates poor fitness, with thefittest mutant still susceptible to fabimycin. Collectively, theseresults suggest the combination use of two antibiotics that engagedifferent positions on the same target as a means to kill pathogenicbacteria and limit resistance.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3159–3168"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943872","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fluorescent Farnesyl-Derived Probes Reveal Distinct Intracellular Localization Associated with Morphogenesis Suppression in Candida albicans","authors":"Ivan Voronov,&nbsp;Melissa Shbeta,&nbsp;Micha Fridman","doi":"10.1021/acsinfecdis.6c00671","DOIUrl":"10.1021/acsinfecdis.6c00671","url":null,"abstract":"<p>Farnesol is a quorum-sensing sesquiterpene produced by <em>Candida albicans</em> that inhibits filamentation, a morphogenetictransition underlying fungal invasion and virulence. Notably, severalfarnesyl-derived sesquiterpenes bearing functional groups other thanthe original alcohol of farnesol have also been reported to suppressfilamentation, indicating that this activity is not unique to farnesolitself but may instead reflect shared properties of the farnesyl scaffold.This observation prompted us to probe whether differences in the intracellulardistribution of farnesyl-derived molecules might accompany differencesin their morphogenesis-suppressing activity. To address this question,we synthesized two fluorescent farnesyl-derived probes, <strong>F-1</strong> and <strong>F-2</strong>, together with dodecyl-chain analogues as controls.Both probes preserve the native farnesyl isoprenoid scaffold but differin fluorophore identity, with <strong>F-1</strong> labeled with a tetramethylrhodamine(TAMRA) dye and <strong>F-2</strong> labeled with a 7-diethylaminocoumarindye. Counterintuitively, in live <em>C. albicans</em> cells, <strong>F-1</strong>, despite bearing the more sterically demandingTAMRA dye, inhibited filamentation and displayed broad cytosolic distributionwith enrichment along the tubular mitochondrial network. Inhibitionby <strong>F-1</strong> was reversed by exogenous dbcAMP, consistent witha mechanism like that of farnesol involving the Ras1-cAMP signalingpathway. In contrast, <strong>F-2</strong> showed no antifilamentationactivity and localized predominantly to cytosolic membranous compartmentswith irregular morphology. Notably, <strong>F-1</strong> retained mitochondrialenrichment and filamentation-inhibitory activity in drug-resistantstrains, and its intracellular accumulation at biologically activeconcentrations was not substantially diminished by enhanced efflux.Together, these findings demonstrate that chemical modification offarnesyl-derived sesquiterpenes, including incorporation of substituentswith substantial molecular weight and steric bulk, can preserve morphogenesis-inhibitoryactivity. These results support a model in which the pleiotropic morphogenesis-inhibitoryeffects of farnesyl-derived compounds involve not only plasma membrane-associatedsignaling but also access to intracellular compartments, includingmitochondria.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3265–3275"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943888","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Total Synthesis of Paenitracin B and Analogues with Enhanced Antibacterial Activity","authors":"Yunhao Duan,&nbsp;Lucas Jongman,&nbsp;Vladyslav Lysenko,&nbsp;Willem Jespers,&nbsp;Gilles P. van Wezel,&nbsp;Nataliia V. Machushynets,&nbsp;Nathaniel I. Martin","doi":"10.1021/acsinfecdis.6c00198","DOIUrl":"10.1021/acsinfecdis.6c00198","url":null,"abstract":"<p>The development of antibacterials with unique mechanismsof actionis key to addressing the threat posed by antibiotic resistance. Amongthe wide array of natural products that target bacterial cell wallbiosynthesis, bacitracin A is the preeminent example of an antibioticthat functions by selectively targeting and sequestering the key bacterialphospholipid undecaprenyl pyrophosphate (C₅₅PP). Historically,the bacitracins have been isolated from fermentations of <em>Bacillus</em> species. We recently discovered a series of structurally distinctbacitracin-like peptide antibiotics produced by members of the <em>Paenibacillus</em> genus, termed the paenitracins. Here, we reportthe total synthesis of paenitracin B (<strong>1</strong>), enabling definitivestereochemical validation of the previously proposed structure anddelivering quantities of material suitable for more extensive antibacterialtesting. The synthetic route developed was also applied to the preparationof paenitracin analogues, with some showing significantly enhancedantibacterial activity, particularly against VanA-type vancomycin-resistant <em>Enterococcus faecium</em> clinical isolates.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3002–3008"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943892","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tissue-Specific Parasite Persistence Following Chemotherapy in a Drug-Resistant Trypanosoma cruzi Preclinical Model","authors":"Valquíria Angelis Fernandes,&nbsp;Amanda Latércia Tranches Dias,&nbsp;Sérgio Caldas,&nbsp;Gilson Faria,&nbsp;Anna Luiza Leite Pereira,&nbsp;Gabriella Martiniano Pereira,&nbsp;Rodrigo Dian de Oliveira Aguiar Soares,&nbsp;Thais Lopes Valentim Di Paschoale Ostolin,&nbsp;Ivo Santana Caldas,&nbsp;Rômulo Dias Novaes,&nbsp;Lívia de Figueiredo Diniz","doi":"10.1021/acsinfecdis.6c00228","DOIUrl":"10.1021/acsinfecdis.6c00228","url":null,"abstract":"<p>Therapeutic failure in Chagas disease remains a majorunmet medicalchallenge, often associated with intrinsic variability in drug susceptibilityamong <em>Trypanosoma cruzi</em> strains. However, the biologicalbasis of incomplete parasite clearance after treatment remains poorlyunderstood. Here, we investigated the tissue distribution of an intrinsicallydrug-resistant <em>T. cruzi</em> strain in a murine modelof acute infection and evaluated the effects of short-term treatmentwith benznidazole or E1224 on parasite burden and host immune responses.Parasite loads were quantified by qPCR in multiple tissues beforeand after cyclophosphamide-induced immunosuppression, and plasma cytokineswere measured to assess systemic immune responses. The heart, skeletalmuscle, and white adipose tissue harbored the highest parasite burdens.Although both drugs significantly reduced parasite loads, incompleteclearance and tissue-specific recrudescence were observed followingimmunosuppression. Benznidazole-treated mice showed parasite reboundin the heart, adipose tissue, and large intestine, whereas E1224-treatedanimals exhibited recrudescence in the heart, skeletal muscle, andliver. Acute infection induced a robust pro-inflammatory response,and parasite reduction was accompanied by decreased Th1 cytokine levels.These findings demonstrate parasite persistence within defined tissuereservoirs despite chemotherapy, suggesting tissue-specific survivalas a potential biological basis for therapeutic failure.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3068–3079"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Allosteric Crosstalk between Inhibitor Binding Sites Drives Enhanced Islatravir Susceptibility in F227C HIV-1 Reverse Transcriptase","authors":"Corey W. Hecksel,&nbsp;Susanne N. Walker,&nbsp;Izzat Raheem,&nbsp;Ernest Asante-Appiah,&nbsp;Guillermo Calero,&nbsp;Tracy L. Diamond,&nbsp;Sandra B. Gabelli,&nbsp;Yacob Gomez-Llorente,&nbsp;Robert P. Hayes,&nbsp;Srivanya Tummala,&nbsp;Sandra Vergara,&nbsp;Daniel J. Klein","doi":"10.1021/acsinfecdis.6c00431","DOIUrl":"10.1021/acsinfecdis.6c00431","url":null,"abstract":"<p>Doravirine (DOR) and islatravir (ISL)are inhibitorsof human immunodeficiencyvirus type 1 (HIV-1) replication that block the viral reverse transcriptase(RT) by distinct mechanisms. The combination has demonstrated efficacyin Phase 3 clinical studies in both virologically suppressed and treatment-naïvepeople living with HIV-1 and has the potential to mitigate the emergenceof resistance-associated mutations through complementary virologicalprofiles. RT bearing a single point mutation, F227C, is associatedwith resistance to DOR, yet is hypersusceptible to ISL. Here, we reportcryoEM structures of islatravir triphosphate (ISL-TP) bound to wild-type(WT) RT and F227C RT. Comparison with the corresponding ISL-TP anddATP-bound WT RT structures reveals that the F227C mutation inducesan unexpected conformational change in a loop of the palm domain thatis positioned to gate substrate access, providing a structural basisfor ISL hypersusceptibility.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3179–3190"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943777","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antibiofilm Peptides Revisited: From Biofilm Models and Metrics to Mechanisms and Translation","authors":"Evan H. Frederick,&nbsp;Shilpa S. Nair,&nbsp;Sharmila Jayatilake,&nbsp;Samuel J. T. Wardell,&nbsp;Phil Bremer,&nbsp;Daniel Pletzer","doi":"10.1021/acsinfecdis.6c00266","DOIUrl":"10.1021/acsinfecdis.6c00266","url":null,"abstract":"<p>Biofilm-associatedinfections contribute substantially to the antimicrobialresistance-related burden by promoting persistent, difficult-to-treatinfections. Antibiotic failure often reflects biofilm recalcitrance(tolerance and persistence) and, in some contexts, the enhanced selectionand dissemination of resistance. To overcome this burden, antibiofilmpeptides (ABPs) are emerging as a versatile solution. ABPs can inhibitbiofilm development, weaken established biofilms, and synergize withexisting antimicrobials. This review highlights current biofilm modelsand susceptibility end points, emphasizing how experimental designand readout selection shape conclusions about ABP activity and comparabilityacross studies. We describe ABP discovery, the sequence–propertyfeatures that drive activity, and outline key modes of action. Theseinclude reprogramming biofilm-associated regulatory pathways, targetingconserved nucleotide signaling networks such as guanosine tetraphosphate(ppGpp) and cyclic di-GMP (c-di-GMP), matrix-directed effects, andbiofilm-specific tolerance and resistance mechanisms that may limitABP durability. Finally, we briefly discuss translational considerationsand selected clinical and industrial use cases for ABPs, emphasizingthe importance of improving and assessing their stability, delivery,and selectivity under physiological and industrially relevant conditions.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"2900–2921"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943823","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Harnessing Conventional and Nanotechnology-Enabled Combination Therapies to Combat Kinetoplastid Neglected Tropical Diseases","authors":"Eman Fathi Fadel,&nbsp;Maha M. Eissa","doi":"10.1021/acsinfecdis.6c00380","DOIUrl":"10.1021/acsinfecdis.6c00380","url":null,"abstract":"<p>The kinetoplastid neglected tropical diseases, Chagasdisease,African trypanosomiasis, and leishmaniasis, are vector-borne diseasesthat remain a persistent global health challenge. Progress has beenmade in combating human African trypanosomiasis, but efforts to containother kinetoplastid diseases have been slower. The current drugs usedfor treatment have limitations, such as drug resistance, toxicity,high cost, and limited access. To overcome these challenges, alternativetherapeutic strategies are being explored, including drug combinations,drug repurposing, and nanotechnology, which have shown promise inother diseases, like cancer. Combination therapies, both conventionaland nanobased, have the potential to enhance antiparasitic efficacy,reduce side effects, and prevent resistance development. This reviewfocuses on the efficacy and safety of drug combinations for kinetoplastidneglected tropical diseases, highlighting current conventional combinationtherapies and ongoing research on both conventional and nanobasedcombination therapies in various stages of development. The reviewaims to provide novel insights and promote future research for thedevelopment of innovative, safe, and effective drug combination therapies.This will help in accelerating progress toward the elimination ofKinetoplastid neglected tropical diseases, in line with SustainableDevelopment Goal 3.3 to ensure healthy lives and promote well-beingfor all, at every stage of life and to end the epidemics of neglectedtropical diseases by 2030.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"2922–2964"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943940","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insights into the Structure and Function of the OTU Protease Virulence Factors from Emerging Human Nairoviruses","authors":"David S. Gonzalez,&nbsp;Amritpal Jalf,&nbsp;Vanessa Moresco,&nbsp;Joseph Garcia,&nbsp;Lukasz Jaroszewski,&nbsp;David Matta,&nbsp;Jonathan Nguyen,&nbsp;Bryan Torres,&nbsp;Éric Bergeron,&nbsp;Adam Godzik,&nbsp;Scott D. Pegan","doi":"10.1021/acsinfecdis.6c00320","DOIUrl":"10.1021/acsinfecdis.6c00320","url":null,"abstract":"<p>Tick-borne negative-sense single-stranded RNA nairovirusesrepresenta significant global public-health threat. Over the past decade, discoveriesof new orthonairoviruses and norwaviruses have surged. Many of thesehave been observed to cause febrile illness in humans or have beenfound in vectors that carry other human diseases. All orthonairovirusesencode a viral homologue of the ovarian tumor protease (OTU) superfamily,which is part of the <span>l</span>-protein, and the OTU is conservedin the <em>Norwavirus</em> genus. OTUs exhibitvarying levels of deubiquitinating (DUB) and deISGylating activitiesthat facilitate viral immune evasion, establishing them as key virulencefactors. Here, these activities from emerging Songling, Yezo, Tachengtick virus 1, and Pacific Coast Tick orthonairoviruses, as well asthe Beiji norwavirus, were investigated. This analysis reveals a diverserange of DUB and human deISGylase enzymatic activities in the previouslyuncharacterized viral groups. This includes unexpected OTU human deISGylatingactivity and suggests that OTUs possess functions beyond their establishedDUB and deISGylating roles. Additionally, the molecular basis of theseactivities, or the absence thereof, is explored through X-ray crystallographicstructures of viral OTUs encoded by four orthonairoviruses and onenorwavirus. The biochemical and structural insights provide a pathforward for predicting OTU activity among current and emerging nairoviruses.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3127–3143"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148429365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"NIE Antigen Mapping for Serological Diagnostic of Strongyloidiasis","authors":"Maria Cambra-Pellejà,&nbsp;Ruth Aguilar,&nbsp;Marta Vidal,&nbsp;Alba Pejenaute,&nbsp;Alfons Jiménez,&nbsp;Pedro Fleitas,&nbsp;Claudia D. Simao,&nbsp;Luis Baptista-Pires,&nbsp;Daniel Camprubí-Ferrer,&nbsp;Jose Muñoz,&nbsp;Gabriel Ortega-Quintanilla,&nbsp;Carlota Dobaño,&nbsp;Claudio Parolo,&nbsp;Javier Gandasegui","doi":"10.1021/acsinfecdis.6c00271","DOIUrl":"10.1021/acsinfecdis.6c00271","url":null,"abstract":"<p>Strongyloidiasisis a neglected tropical disease forwhich scalableserological diagnostics are essential to support control programmes.The <em>Strongyloides stercoralis</em> NIE antigenis widely used for antibody detection, but its antigenic determinantsremain incompletely defined. Here, we performed epitope mapping ofthe NIE antigen using a panel of 23 overlapping 15-mer peptides and4 bioinformatically predicted peptides. Immunoreactivity was evaluatedby detecting IgG assay in sera from infected and noninfected individuals.Full-length NIE showed excellent diagnostic performance (AUC = 0.934),whereas four peptides (11, 12, 17, 18) demonstrated moderate discrimination(AUC = 0.59–0.64). Combining peptides improved performance(AUC &gt; 0.70), with peptides 12 and 18 consistently contributingtothe best models. Structural mapping revealed two solvent-exposed regionscorresponding to peptide pairs 11–12 and 17–18. Thesefindings identify key immunoreactive regions within NIE and providea structural basis for antigen engineering, while confirming the superiorperformance of the full-length antigen for serodiagnosis.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3104–3113"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943949","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}