ACS Infectious Diseases最新文献

{"title":"Human Milk Oligosaccharides Modulate Nitrogen Utilization in Lactobacillus crispatus in a Glucose-Dependent Manner","authors":"Julie A. Talbert,&nbsp;Thomas L. Kalmer,&nbsp;Allison S. Walker,&nbsp;Jennifer A. Gaddy,&nbsp;Steven D. Townsend","doi":"10.1021/acsinfecdis.6c00250","DOIUrl":"10.1021/acsinfecdis.6c00250","url":null,"abstract":"<p>The vaginal microbiome’s transition to a dysbioticstateincreases susceptibility to pathogens like group B Streptococcus.While human milk oligosaccharides are established prebiotics in theneonatal gut, their impact on the vaginal niche remains largely unexplored.This study investigated the effects of pooled human milk oligosaccharideson the growth and physiology of vaginal (<em>Lactobacillus crispatus</em>, <em>Lactobacillus gasseri</em>, <em>Lactobacillus iners</em>) and gut-derived(<em>Lactobacillus reuteri</em>, <em>Lactobacillus rhamnosus</em>) commensals. Growth analysesrevealed that human milk oligosaccharides significantly and selectivelystimulated growth across all vaginal strains tested, whereas gut commensalsexhibited variable or inhibited growth. Carbohydrate utilization assaysand comparative genomics against <em>Bifidobacterium infantis</em> showed that <em>Lactobacillus crispatus</em> and <em>Lactobacillus reuteri</em> lack thecanonical metabolic machinery to catabolize human milk oligosaccharides.Instead, nitrogen utilization assays identified a glucose-dependentpathway where human milk oligosaccharides are associated with thedepletion of primary amines and amino acids in <em>Lactobacillus crispatus</em> supernatants. These results suggest thathuman milk oligosaccharides act as noncatabolic modulators of vaginallactobacilli. Collectively, these in vitro findings may warrant investigationof human milk oligosaccharides as modulators of vaginal commensalphysiology in more complex experimental systems.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3080–3091"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943914","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":"Sip4p Regulates the Transcription of Enzymes for Gluconeogenesis in Nakaseomyces glabratus","authors":"Ryan J. Galloway,&nbsp;Alexandria J. Walgren,&nbsp;Yusra M. Naeem,&nbsp;Lana C. Geiger,&nbsp;Meghan E. Breen","doi":"10.1021/acsinfecdis.6c00455","DOIUrl":"10.1021/acsinfecdis.6c00455","url":null,"abstract":"<p>To survive in glucosepoor niches within the host, theopportunisticpathogen <em>Nakaseomyces glabratus</em> mustassimilate alternative carbon sources. In many yeasts, pathways foralternative carbon metabolism are regulated at the transcriptionallevel by Zn₂Cys₆ transcription factors, a classof proteins that are unique to fungi. Here, we investigated the transcriptionalregulation of alternative carbon metabolism pathways by the Zn₂Cys₆ transcription factors Cat8p, Sip4p, and Rds2pin the opportunistic pathogen <em>N. glabratus</em>. Phenotypic screens of transcription factor knockout strains grownon alternative carbon sources identified that deletion of <em>CAT8</em>, a transcription factor required for growth in theclosely related model organisms <em>Saccharomyces cerevisiae</em>, did not affect the growth of <em>N. glabratus</em>, but deletion of <em>SIP4</em> resulted in growth defects.We further probed the changes in gene expression that occur upon treatmentwith lactate or ethanol using RNA-seq. In the wild type strain, genesrelated to gluconeogenesis, the TCA cycle, and the glyoxylate cyclewere upregulated in the presence of alternative carbon sources, andtranscription of <em>PCK1</em>, encoding the gluconeogenesisenzyme phosphoenolpyruvate carboxykinase, was induced over 2000-fold.Deletion of <em>SIP4</em> resulted in a 4-fold decrease in <em>PCK1</em> gene expression in lactate and ethanol treated cells,and a 6-fold decrease in the cytosolic malate dehydrogenase <em>MDH2</em> in lactate treated cells. Taken together, our resultshave uncovered transcriptional rewiring and a role for Sip4p in theregulation of alternative carbon metabolism in <em>N. glabratus</em>.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3204–3216"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943915","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":"Inhibition of Fosfomycin Resistance Protein FosA from Pseudomonas aeruginosa","authors":"Vanessa Wiltsie,&nbsp;Tatum Smith,&nbsp;Nishad Thamban Chandrika,&nbsp;Nathaniel C. Gilbert,&nbsp;Sylvie Garneau-Tsodikova,&nbsp;Matthew K. Thompson","doi":"10.1021/acsinfecdis.6c00121","DOIUrl":"10.1021/acsinfecdis.6c00121","url":null,"abstract":"<p>Antimicrobialresistance is an urgent issue in modern-day medicine.One way to address this problem is to repurpose and restore the functionof older antibacterials through the specific targeting of antibiotic-modifyingenzymes produced by bacteria. Fosfomycin is an antibiotic that isattractive for repurposing because it has been previously approvedfor use in uncomplicated urinary tract infections (UTIs) and is widelyregarded as safe with no known off-target interactions. The primarylimitation to fosfomycin usage has been the emergence of fosfomycinresistance enzymes. FosA^<em>Pa</em> is the fosfomycinresistance enzyme from <em>Pseudomonas aeruginosa</em>. Weidentified and evaluated several potential inhibitors of FosA^<em>Pa</em> using high-throughput virtual screening(HTVS) and ³¹P-NMR. In addition, we obtained X-ray crystalstructures of FosA^<em>Pa</em> with the inhibitorsbound in the active site to gain insights into important protein–ligandinteractions necessary for the potential structure-based drug design.Preliminary cell-based assays were performed to evaluate the effectthat the inhibitors have on the minimum inhibitory concentration (MIC)of fosfomycin in <em>P. aeruginosa</em>. Our results providean initial scaffold for structure–activity relationships andfuture compound modifications for combating fosfomycin resistancein <em>P. aeruginosa</em> and other FosA-containing Gram-negativepathogens.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 9","pages":"3043–3052"},"PeriodicalIF":4.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943933","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":"Structural Insights into Pyrethroid Recognition by Anopheles Chemosensory Proteins.","authors":"Shibani Biswas, Yogavel Manickam, Choong Yeu Khai, Ritu Goswami, Sanskrita Sukla, Rosicler Barbosa, Sihyun Sung, Rini Chaturvedi, José Antonio Márquez, Aditya Chaki, Amit Sharma, Ram Das, J Sivaraman, Soumyananda Chakraborti","doi":"10.1021/acsinfecdis.6c00114","DOIUrl":"https://doi.org/10.1021/acsinfecdis.6c00114","url":null,"abstract":"<p><p>Mosquito-borne diseases, particularly malaria, remain a major global health challenge. Among different mosquitoes, Anopheles are solely responsible for malaria. Insecticide-based interventions such as insecticide-treated nets (ITNs) and indoor residual spraying (IRS) are central to mosquito control. However, the widespread emergence of insecticide resistance, especially to pyrethroids, the most commonly used insecticides for mosquito worldwide, threatens their effectiveness. While genetic and metabolic mechanisms of resistance are well characterized, behavioral and sequestration-based mechanisms, particularly those involving chemosensory proteins (CSPs), are less understood. CSPs and odorant-binding proteins (OBPs) are integral components of the mosquito olfactory system, mediating host-seeking and other behavioral processes by transporting odorant molecules to olfactory receptors. Recent evidence suggests that CSPs may also bind insecticides like pyrethroids, contributing to resistance through sequestration. In this study, we investigated the structural and functional roles of CSPs in Anopheles mosquitoes. We determined three high-resolution X-ray crystal structures (apo-form) of CSPs (<2 Å) from Anopheles culicifacies and Anopheles gambiae, representing the first crystal structures of CSPs from any Anopheles species reported to date. Using structural, biophysical and computational approaches, we assessed CSP-ligand recognition of various insecticides, specifically pyrethroids and identified key residues potentially involved in pyrethroid interaction through site-directed mutagenesis. The moderate micromolar binding affinities of deltamethrin and permethrin, compared to other insecticides, support the role of CSPs in pyrethroid sequestration. Our findings offer mechanistic insights into pyrethroid sequestration and provide a foundation for developing novel vector control strategies that target CSP-insecticide interactions to combat pyrethroid resistance.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148862585","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":"Nanotechnology to Break the Antimicrobial Resistance","authors":"Navjot Kaur,&nbsp;Pragnya Roy,&nbsp;Mrinmoy De","doi":"10.1021/acsinfecdis.6c00018","DOIUrl":"10.1021/acsinfecdis.6c00018","url":null,"abstract":"<p>The global rise in antibiotic resistance has become amajor publichealth concern, driving an urgent demand for new therapeutic strategiesto manage infections caused by multidrug-resistant (MDR) pathogens.Nanomaterials have therefore attracted significant interest as potentialalternatives or adjuvants to conventional antibiotics, owing to theirtunable physicochemical properties and their ability to act throughmechanisms distinct from those of classical drugs. In this review,we focus on surface-modified nanomaterials and metal–organiccages and examine how parameters such as size, charge, surface chemistry,and structural organization influence antibacterial and antibiofilmperformance. By integrating mechanistic insights with biological context,this review highlights the factors that govern efficacy in complexinfection environments and the translational challenges that mustbe addressed for practical application. Collectively, this articleprovides a framework for understanding how nanomaterial design canbe leveraged to develop more effective antimicrobial strategies.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2465–2484"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148395406","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":"Development of Fluorogenic Probes to Detect Glycan-Degrading Enzymes in Bacteria","authors":"Esteban Tarazona Guzman,&nbsp;Ankita Paul,&nbsp;Karen D. Moulton,&nbsp;Daniel E. Calles-Garcia,&nbsp;Maren Cooper,&nbsp;Lucas J. DiCerbo,&nbsp;Soumyakanta Maji,&nbsp;Elizabeth A. Stemmler,&nbsp;Suvarn S. Kulkarni,&nbsp;Danielle H. Dube","doi":"10.1021/acsinfecdis.6c00347","DOIUrl":"10.1021/acsinfecdis.6c00347","url":null,"abstract":"<p>Bacterial fitnessand survival depend on the biosynthesis and maintenanceof cell-envelope glycans. Bacterial glycans are composed of over 700monosaccharides, and their construction, tailoring, recycling, anddegradation require the choreographed action of myriad glycosyltransferasesand glycosidases. Because of the structural diversity and complexityof bacterial glycans, coupled to limited methods to profile bacterialglycosidase activity, the function and existence of glycosidases thatdegrade most bacterial glycans are unknown. Taking a cue from thesuccessful use of fluorogenic glycosides based on ubiquitous monosaccharidesto detect glycosidase activity in cells and tissues, we sought toexpand this approach to detect glycosidase activity in bacteria. Fluorogenicprobes based exclusively on bacterial amino and deoxy sugars <em>N</em>-acetyl-<span>d</span>-fucosamine and 2,4-diacetamido-2,4,6-trideoxy-<span>d</span>-galactose were developed, and their activation was directlycompared to a <span>d</span>-glucose-based fluorogenic probe in bacterialand mammalian cells. The species-selective utilization of these glycosidaseprobes, coupled to the difference in relative magnitude of glycosidaseactivity observed, provides important insights into these relativelyunexplored glycan-processing enzymes. The use of these fluorogenicprobes expands the toolkit for detecting glycan-degrading enzymesand offers an approach to enhancing a broader understanding of bacterialglycan metabolism and its diversity across different species.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2778–2787"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148519613","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":"Multipronged Cell Wall-Targeting Converts Ineffective Antibiotics into a Potent Regimen against Mycobacterium abscessus","authors":"Carmen J. E. Pee,&nbsp;May Delos Santos,&nbsp;Kevin Pethe","doi":"10.1021/acsinfecdis.6c00309","DOIUrl":"10.1021/acsinfecdis.6c00309","url":null,"abstract":"<p><em>Mycobacterium abscessus</em> is an intrinsicallydrug-resistant pathogen responsible for chronic lung infections thatare notoriously difficult to cure. Its complex, multilayered cellwall limits drug penetration and underlies the poor efficacy of mostantibiotics. Here, we show that targeting multiple components of cellwall biosynthesis simultaneously can convert otherwise inactive agentsinto potent, bactericidal combinations. Pairing glycopeptides withβ-lactams led to synergistic killing, while inclusion of ethambutolfurther enhances potency. Mechanistic studies indicated that the combinationsact through cumulative weakening of the cell envelope. Concomitantinhibition of peptidoglycan and arabinogalactan or lipoarabinomannansynthesis caused extensive ATP leakage and improved access of vancomycinto its targets, consistent with additive structural damage. This multilayereddisruption rendered the cell wall unable to maintain integrity. Thetriple combination of teicoplanin, cefoxitin and ethambutol also decreasedlung bacterial loads in mice infected with <em>M. abscessus</em>. These findings establish that intrinsic antibiotic resistance in <em>M. abscessus</em> can be overcome by coordinated interferencewith cell wall biogenesis using clinically available antibiotics.This strategy provides a mechanistic framework for rational repurposingof existing drugs to treat nontuberculous mycobacterial infectionsfor which new therapies are urgently needed.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2750–2762"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148546936","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":"Lyophilized LAMP Assay Combined with Lateral Flow Biosensor for Cold-Chain-Free Detection of Mycobacterium tuberculosis","authors":"Jutturong Ckumdee,&nbsp;Somchai Santiwatanakul,&nbsp;Nakarin Vutipow,&nbsp;Thongchai Kaewphinit","doi":"10.1021/acsinfecdis.6c00520","DOIUrl":"10.1021/acsinfecdis.6c00520","url":null,"abstract":"<p>To decentralize tuberculosis surveillancein resource-limited andtropical regions, a rapid, robust, and cold-chain-independent near-point-of-carebiosensor is urgently required to overcome the instability of conventionalliquid-formulation diagnostics. Herein, we developed a ready-to-uselyophilized reaction mix Loop-Mediated Isothermal Amplification (LAMP)matrix integrated with a Lateral Flow Biosensor (LFB) for the instrument-freevisual detection of <em>Mycobacterium tuberculosis</em> (<em>M. tuberculosis</em>). The freeze-driedreagents, stabilized with an optimized trehalose-BSA matrix, werehermetically packaged and systematically evaluated for long-term thermalstability across four regulated profiles (−20 °C, 4 °C,25 °C, and 37 °C) over a 12-month period. Diagnostic viabilitywas further validated in a double-blinded study using 191 clinicalsputum specimens against gold-standard culture and line probe assays.The stabilized platform demonstrated an analytical sensitivity downto 10² CFU/mL and maintained full functional activity forup to 12 months at −20 °C and 4 weeks at 4 °C, withrobust short-term resilience under tropical stress (25 °C) forup to 1 week. However, the formulation was unable to withstand prolongedexposure to harsh environmental conditions at 37 °C, resultingin a progressive decline in amplification performance following phase-transitioninstability. Crucially, clinical validation yielded an outstandingdiagnostic sensitivity of 98.92% and a positive predictive value (PPV)of 100.00%. These findings validate the lyophilized LAMP-LFB platformas a highly reliable, sustainable, and distributable molecular diagnostictool capable of overcoming the cold-chain bottleneck in field-basedtuberculosis detection. Although the developed platform shows strongpotential for near-point-of-care deployment, further optimizationof the lyophilization formulation and process will be necessary toenable prolonged storage and transportation under ambient-temperatureconditions.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2853–2862"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148560213","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":"Deadbolt Drug Discovery: Locking the Door to Class 1 Viral Entry by Small Molecules","authors":"John P. Sloan,&nbsp;Lijun Rong,&nbsp;Terry W. Moore","doi":"10.1021/acsinfecdis.6c00302","DOIUrl":"https://doi.org/10.1021/acsinfecdis.6c00302","url":null,"abstract":"<p>The continued emergence of viral pathogens underscoresthe needfor novel antiviral therapeutics with improved efficacy. Small-moleculeinhibitors of viral entry are attractive antiviral agents becausethey block the virus at its earliest step, preventing the virus fromentering host cells and causing downstream damage. Some of the virusesof greatest concern for human health, such as human immunodeficiencyvirus, respiratory syncytial virus, influenza virus, Ebola virus,severe acute respiratory syndrome coronavirus 2, and Lassa virus,encode Class 1 fusion proteins which mediate membrane fusion and viralentry. In this review, we highlight recent advances in the discoveryand development of small-molecule entry inhibitors reported over thepast five years that target viruses encoding Class 1 fusion proteins.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2485–2504"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729808","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":"A Divergent MBL-Fold Metallo-Hydrolase (Kmh-1) from Klebsiella pneumoniae Confers Aztreonam Degradation and Expands the β-Lactamase Landscape","authors":"Jyoti Barman,&nbsp;Partho Biswas,&nbsp;Partha Roy,&nbsp;Saugata Hazra","doi":"10.1021/acsinfecdis.5c01093","DOIUrl":"10.1021/acsinfecdis.5c01093","url":null,"abstract":"<p>The widespread use and misuse of β-lactam antibioticsexertselective pressure on bacteria, driving the continuous emergence ofnovel metallo-β-lactamases (MBLs). Characterizing newly evolvedMBLs is critical for elucidating the molecular basis of their antimicrobialresistance (AMR) and may contribute to designing novel inhibitors.In this study, we have done the functional characterization of anMBL-fold metallo-hydrolase from <em>Klebsiella pneumoniae</em> (designated Kmh-1), which shares low sequence similarity with B1MBLs. Unlike B1 enzymes, where zinc binding motifs are strictly conserved(H116–H118–H196 and D120–C221–H263), Kmh-1retains only Asp120 and His263, marking its clear divergence. Phylogeneticanalysis further establishes its divergence from the existing B1 MBLs.Kmh-1 has activity toward diverse β-lactams, and zinc is requiredfor enzymatic activity. This study also finds aztreonam hydrolyzingactivity in this enzyme. Kmh-1–aztreonam interaction is validatedthrough circular dichroism (CD) and fluorescence spectroscopy. AlphaFoldstructure prediction and docking studies confirm that Kmh-1 can accommodateaztreonam in the active site and disclose the probable aztreonam bindingresidues. Our results demonstrate a plausible explanation of effectiveaztreonam binding in Kmh-1, which is similar to that of clinicallyrelevant NDM-1. IC₅₀ values against different inhibitorsare determined for Kmh-1, and the IC₅₀ value against bicyclicboronate is observed in the nM range. Together, these findings establishKmh-1 as an MBL-fold metallo-hydrolase endowed with aztreonam bindingand hydrolysis, expanding the landscape of resistance and providinga framework for inhibitor design.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2614–2626"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147968502","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}