ACS Infectious Diseases最新文献

{"title":"Cytochrome bc1 Catalytic Subunit Rip1 Modulates Antifungal Tolerance in Candida auris.","authors":"Trinh Phan-Canh, Michaela Lackner, Manju Chauhan, Lisa-Maria Zenz, Neeraj Chauhan, Karl Kuchler","doi":"10.1021/acsinfecdis.5c01058","DOIUrl":"10.1021/acsinfecdis.5c01058","url":null,"abstract":"<p><p>Candida auris is an emerging fungal pathogen causing invasive infections in immunocompromised patients, with mortality rates reaching up to 60%. Pronounced drug resistance makes treatment failure common, and so does antifungal tolerance, a phenomenon enabling pathogen survival at supra-MIC concentrations without resistance mutations. Here, we uncover a mechanism of antifungal tolerance in C. auris engaging the mitochondrial cytochrome bc1 complex. Deletion of RIP1, a conserved catalytic complex subunit, does not significantly alter the susceptibility to caspofungin or voriconazole. However, rip1Δ mutants exhibit a marked reduction in antifungal tolerance across a wide range of supra-MIC concentrations. Transcriptomics reveals the dysregulation of multiple drug resistance and tolerance-related genes in the rip1Δ mutant, demonstrating a role for Rip1 in controlling antifungal susceptibility. Targeting cytochrome bc1 function with the fungal-specific inhibitor Inz-5 enhances antifungal action of both voriconazole and caspofungin. Additionally, ablation of RIP1 causes fitness defects, suggesting that cytochrome bc1 is a potential antifungal target against C. auris infections.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2026-07-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148617468","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":"Multiple Protein–Protein Interactions Drive the Assembly and Budding of the Chikungunya Virion","authors":"Miguel Angel Coronado-Ipiña,&nbsp;Shuyang Zhang,&nbsp;Siyu Li,&nbsp;Pedro Gerardo Hernández-Sánchez,&nbsp;Denisse Cadena-Lopez,&nbsp;Vanessa Labrada-Martagón,&nbsp;Ajay Gopinathan,&nbsp;Suchetana Mukhopadhyay,&nbsp;Roya Zandi* and Mauricio Comas-Garcia*,&nbsp;","doi":"10.1021/acsinfecdis.6c00369","DOIUrl":"10.1021/acsinfecdis.6c00369","url":null,"abstract":"<p >The assembly of enveloped viruses is a highly orchestrated process that depends on the coupling of multiple protein–protein interactions within a membrane environment. To gain mechanistic insight into this process, we use Chikungunya virus as a model system to study Alphavirus assembly, focusing on the interplay between core–spike and spike–spike interactions. We begin with coarse-grained molecular dynamics simulations to systematically explore how the symmetry of the nucleocapsid core, together with the relative strengths of spike–core and spike–spike interactions, influences budding efficiency and the emergence of icosahedral particle symmetry. Building on these computational results, we performed site-directed mutagenesis on Chikungunya virus 181/25 and examined the consequences for particle assembly and budding in cultured cells, as well as the impact of these mutations during <i>in-cellulo</i> assembly. Our results revealed that canonical core–spike interactions, while necessary, were not sufficient for successful assembly. Instead, lateral interactions among glycoproteins emerged as critical determinants of efficient budding, particle stability, and the maintenance of icosahedral symmetry. Together, these findings provided an integrated computational and experimental framework for understanding the molecular principles governing Alphavirus assembly.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2383–2395"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148209257","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":"Inhibiting Bacterioferritin Iron Release Induces Iron Starvation and Metabolic Downshift, Potentiating Aminoglycosides in P. aeruginosa Biofilms","authors":"Leo Fontenot,&nbsp;Huili Yao,&nbsp;Alexanndra M. Behm,&nbsp;Anabel Soldano,&nbsp;Fabrizio Donnarumma,&nbsp;Richard A. Bunce and Mario Rivera*,&nbsp;","doi":"10.1021/acsinfecdis.6c00329","DOIUrl":"10.1021/acsinfecdis.6c00329","url":null,"abstract":"<p >In <i>Pseudomonas aeruginosa</i>, bacterioferritin contributes to regulating cytosolic iron by oxidizing Fe²⁺ and storing Fe³⁺ within its internal cavity, and binding to its cognate ferredoxin to reduce stored Fe³⁺ and release Fe²⁺ to the cytosol. Small molecule derivatives of 4-aminoisoindoline-1,3-dione bind <i>P. aeruginosa</i> bacterioferritin at the cognate ferredoxin binding site, inhibit iron release from bacterioferritin, and exhibit bactericidal activity against mature <i>P. aeruginosa</i> biofilms. In this study we report that treatment of mature biofilms with the 4-aminoisoindoline-1,3-dione derivative KM-5-35 induced approximately 90% cell death. Proteomic analysis of surviving cells revealed iron limitation accompanied by disrupted central carbon metabolism, reduced fatty acid and amino acid biosynthesis, and alterations in ribosome protein composition. These metabolic downshifts likely resulted in unstable proton motive force, diminished efflux capacity and impaired ribosome turnover. In this compromised state, gentamicin and amikacin, but not tobramycin, efficiently exploit KM-5-35-induced translational stress, leading to profound synergistic killing of biofilm cells. These findings underscore the therapeutic potential of targeting bacterioferritin iron mobilization in biofilm-associated infections and suggest a promising strategy for combination antimicrobial therapy.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2358–2371"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acsinfecdis.6c00329","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148248050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Suilysin of Streptococcus suis Serotype 2 Drives Astrocyte Pyroptosis via Activation of the ROS/NLRP3/Caspase-1/GSDMD Pathway","authors":"Ruicheng Yang,&nbsp;Lang Tian,&nbsp;Jundan Wang,&nbsp;Wenquan Ouyang,&nbsp;Huanchun Chen and Xiangru Wang*,&nbsp;","doi":"10.1021/acsinfecdis.6c00307","DOIUrl":"10.1021/acsinfecdis.6c00307","url":null,"abstract":"<p >Emerging evidence indicates that pyroptosis contributes to neuroinflammation and central nervous system (CNS) injuries. However, its role in <i>Streptococcus suis</i> (<i>S. suis</i>)-induced brain damage remains unclear. Here, we demonstrate that <i>S. suis</i> strain P1/7 infection triggers pyroptosis in astrocytes, specifically characterized by activating NLRP3/caspase-1/GSDMD axis. Suilysin (SLY), a key virulence factor of <i>S. suis</i>, dose- and time-dependently induced pyroptosis in U251 cells. Notably, genetic ablation of NLRP3 or GSDMD significantly attenuated SLY-induced pyroptosis, and caspase-1 inhibition similarly suppressed this process. Furthermore, SLY promoted reactive oxygen species (ROS) production, and scavenging ROS inhibited NLRP3/caspase-1/GSDMD activation and pyroptosis. Consistently, in a murine infection model, <i>S. suis</i> P1/7 induced astrocyte pyroptosis in brain tissues, while its sly deleted mutant (P1/7-Δ<i>sly</i>) significantly reduced this effect. These findings reveal that SLY mediates pyroptosis in astrocytes via the ROS/NLRP3/caspase-1/GSDMD pathway, highlighting its critical role in <i>S. suis</i>-induced neuropathogenesis.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2345–2357"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148336923","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":"Antigen-Pulsed Dendritic Cell-Derived Dexosomes Induce a Robust Th1-Biased Antigen-Specific Humoral and Cellular Immunity in Mice against Latent Mycobacterium tuberculosis Antigen Rv2626c","authors":"Saima Naz*,&nbsp;Bandi Dharani,&nbsp;Farhan Ahmed,&nbsp;Suman Singh,&nbsp;Duvvada Srinivas,&nbsp;Manaswini Jagadeb,&nbsp;Kala Jyothi Kanaparthi,&nbsp;Shabbir Ahmad,&nbsp;Nooruddin Khan and Sharmistha Banerjee,&nbsp;","doi":"10.1021/acsinfecdis.5c01111","DOIUrl":"10.1021/acsinfecdis.5c01111","url":null,"abstract":"<p >Tuberculosis (TB) continues to be a leading health crisis globally, with latent tuberculosis infection (LTBI) affecting approximately 1.7 billion people worldwide. The current BCG vaccine does not provide consistent protection against pulmonary TB in adults, underscoring the need for innovative vaccine strategies that target both active and latent <i>Mycobacterium tuberculosis</i> (Mtb) infections. In this study, we introduced a vaccine engineering approach to enhance the immunogenicity of candidate vaccine antigens by utilizing exosomes derived from antigen-pulsed dendritic cells (dexosomes). We focused on a representative latency-associated Mtb protein, <i>Rv2626c</i>, which immunoinformatics studies predicted to contain epitopes capable of eliciting a cell-mediated response biased toward Th1 cells. <i>Rv2626c</i> was cloned, purified, and the recombinant form (<i>rRv2626c</i>) was used to generate antigen-pulsed dexosomes. <i>Rv2626c</i>-pulsed dexosomes were successfully isolated, characterized, and evaluated for their immunomodulatory properties. <i>In vitro</i> studies demonstrated that dendritic cells treated with Rv2626c-pulsed dexosomes exhibited enhanced antigen uptake, improved antigen presentation, and increased expression of costimulatory signals. When immunized with <i>Rv2626c</i>-pulsed dexosomes, mice displayed robust antigen-specific CD8⁺ and CD4⁺ T-cell responses, marked by elevated production of IL-2 and IFN-γ compared to those receiving <i>Rv2626c</i> alone. Additionally, significant antigen-specific antibody responses were observed, with increased IgG2a/IgG1 and IgG2b/IgG1 ratios, indicating a Th1-biased immune response. The sustained antibody response suggests potential for long-lasting protection against latent Mtb bacilli. These findings represent an initial report on the use of dexosomes pulsed with a latency-associated antigen to elicit potent antigen-specific immunological responses. By enhancing both cellular and humoral immune responses, <i>Rv2626c</i>-pulsed dexosomes present a promising platform for the development of next-generation efficacious TB vaccines aimed at targeting LTBI and preventing the reactivation of latent Mtb infections. This research paves the way for further exploration of exosome-based delivery systems as immunomodulatory vehicles for TB vaccine development.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2225–2238"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148325062","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":"Influenza Virus-Like Particles Displaying Leishmania donovani Promastigote Surface Antigen Induce Cross-Protective Immunity","authors":"Keon-Woong Yoon,&nbsp;Ki Back Chu,&nbsp;Gi-Deok Eom,&nbsp;Su In Heo,&nbsp;Hyeon-Woo Nam,&nbsp;Ji-Hyun Lee,&nbsp;Jie Mao,&nbsp;Manish Kumar Singh,&nbsp;Sung Soo Kim and Fu-Shi Quan*,&nbsp;","doi":"10.1021/acsinfecdis.6c00156","DOIUrl":"10.1021/acsinfecdis.6c00156","url":null,"abstract":"<p >Virus-like particles expressing the Promastigote surface antigen (PSA) of <i>Leishmania donovani</i> have shown great potential as a vaccine candidate against <i>L. donovani</i> infection. However, their potential as a cross-protective leishmaniasis vaccine candidate has remained unexplored. In this study, we generated the <i>L. donovani</i> PSA-expressing influenza virus-like particle vaccines and evaluated their cross-protective potential against <i>Leishmania amazonensis</i> infection in mice. Virus-like particles expressing the <i>L. donovani</i> PSA on influenza M1 protein (LdPSA-VLP) were self-assembled in insect cells using the baculovirus expression system. To evaluate the efficacy of our LdPSA-VLP vaccine, mice were subcutaneously immunized and then challenged with virulent <i>L. amazonensis</i>. LdPSA-VLP immunization elicited <i>L. amazonensis</i> antigen-specific IgG antibodies. Upon challenge infection with mCherry-expressing <i>L. amazonensis</i>, <i>L. amazonensis</i>-specific antibody-secreting cell responses, germinal center B cell, memory B cell, and CD4⁺/CD8⁺ T cell responses were markedly enhanced in immunized mice. Footpad inflammation was significantly inhibited, as indicated by decreased proinflammatory cytokine production. LdPSA-VLP provided cross-protection against <i>L. amazonensis</i> by reducing footpad swelling and parasite burden in the footpads. Our findings indicate that LdPSA-VLPs could serve as promising cross-protective vaccine candidates against cutaneous leishmaniasis.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2303–2311"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148336983","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 High-Sensitivity Colorimetric Dot-Blot Aptamer Assay Platform for SARS-CoV-2 Nucleocapsid Protein Detection in Resource-Limited Settings","authors":"Kauser Banu*,&nbsp;Bhairab Mondal*,&nbsp;S. Madhan Kumar,&nbsp;C. Sai Sudha and Raju H,&nbsp;","doi":"10.1021/acsinfecdis.5c01125","DOIUrl":"10.1021/acsinfecdis.5c01125","url":null,"abstract":"<p >We developed a colorimetric dot-blot aptamer assay to address the urgent need for accessible, high-performance SARS-CoV-2 diagnostics in resource-limited settings. Our in-house 96-well dot-blot platform featuring optimized PVDF membrane fluidics and standardized clamping combines nucleocapsid protein (N)-specific monoclonal antibody capture with biotinylated DNA aptamer detection, achieving high sensitivity (0.5 ng/mL limit of detection) and exceptional specificity (0/36 false positives) for the conserved nucleocapsid protein. The assay demonstrates 2-fold greater sensitivity than conventional ELISA (<i>p</i> &lt; 0.001). Clinical validation with 230 patient specimens showed 100% sensitivity (95% CI: 96.4–100%) and 100% specificity (95% CI: 96.4–100%), with results in 100 ± 5 min without specialized instrumentation. The assay enables semiquantitative classification of viral load (low, high) based on signal intensity without providing absolute quantitative measurements. The platform merges laboratory-grade performance with point-of-care practicality, supporting high-throughput processing, minimal infrastructure, low cost (&lt;$1 per test), and heat-inactivation compatibility.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2251–2261"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148161030","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":"Structure−Activity Relationships among Inhibitors of Acinetobacter baumannii and Klebsiella pneumoniae 1-Deoxy-d-xylulose 5-Phosphate Reductoisomerase (DXR/IspC) − A Promising Target for Antibiotic Development","authors":"Misgina Girma,&nbsp;Meagan Belcher Dufrisne,&nbsp;Archi Sehgal,&nbsp;Allyson Dailey,&nbsp;Kenneth Heidel,&nbsp;Darean Bague,&nbsp;Xu Wang,&nbsp;Logan Bartholomew,&nbsp;Richard Beck,&nbsp;Samuel Kirby,&nbsp;Haley Ball,&nbsp;Mosufa Zainab,&nbsp;Soo Hyeon Lee,&nbsp;Iswarduth Soojhawon,&nbsp;Schroeder M. Noble,&nbsp;Cynthia S. Dowd and Robin D. Couch*,&nbsp;","doi":"10.1021/acsinfecdis.5c00875","DOIUrl":"10.1021/acsinfecdis.5c00875","url":null,"abstract":"<p >Antimicrobial resistance (AMR) is a critical global health crisis, responsible for nearly 5 million deaths in 2019 and projected to impose up to $100 trillion in economic costs by 2050. To address this threat, we are developing new antibiotics targeting the methylerythritol phosphate (MEP) pathway in <i>Acinetobacter baumannii</i> and <i>Klebsiella pneumoniae</i>, major nosocomial pathogens. Our efforts focus on 1-deoxy-<span>d</span>-xylulose 5-phosphate reductoisomerase (IspC/DXR), the committed enzyme in MEP-mediated isoprenoid biosynthesis and absent in humans, making it an attractive therapeutic target. Natural products such as fosmidomycin (FOS) and FR900098 (FR) inhibit IspC but exhibit poor bioavailability. To improve drug-like properties, we synthesized FOS analogs and analyzed their structure−activity relationships (SARs) against recombinant Ab- and Kp-IspC, alongside in vitro susceptibility assays. The most potent analogs, α,β-unsaturated compounds <b>4b</b> and <b>16b</b>, inhibited Ab-IspC (AbIspC) with IC₅₀ values of 0.047 μM and 0.029 μM, and Kp-IspC (KpIspC) with 0.194 μM and 0.054 μM, respectively. These showed MICs of 64 μg/mL for <i>A. baumannii</i> and 512 μg/mL for <i>K. pneumoniae</i>. A prodrug series (<b>1d</b>−<b>8d</b>) demonstrated enhanced activity, with compound <b>3d</b> exhibiting MICs from 0.25 to 32 μg/mL against <i>A. baumannii</i>. X-ray crystallography of Ab-IspC with selected analogs (<b>2b</b>, <b>3b</b>, <b>4b</b>) at 2.0 Å resolution provides structural insights to guide future IspC inhibitor optimization.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2203–2215"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acsinfecdis.5c00875","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147429618","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Nanoconfined, Hydrogel-Partitioned LAMP Platform for Rapid, Extraction-Free Quantification of Mycoplasma pneumoniae","authors":"Xiaoyang Jin,&nbsp;Yuxuan Li,&nbsp;Yajun Guo,&nbsp;Xingyu Lin*,&nbsp;Wei Li* and Danli Xie*,&nbsp;","doi":"10.1021/acsinfecdis.6c00203","DOIUrl":"10.1021/acsinfecdis.6c00203","url":null,"abstract":"<p >Accurate quantification of <i>Mycoplasma pneumoniae</i> (<i>M. pneumoniae</i>) is important because pathogen load is associated with disease severity and treatment outcomes. However, quantitative polymerase chain reaction (qPCR) requires DNA extraction and standard-curve calibration, whereas digital polymerase chain reaction (dPCR) remains costly and less accessible. Here, we developed gLAMP-X, an extraction-free hydrogel-limited amplification (gLAMP) platform for rapid quantification of <i>M. pneumoniae</i> from clinical throat swabs. The “X” component denotes extraction-free lysis that disrupts the lipid bilayer of <i>M. pneumoniae</i> while preserving nucleic acid integrity. In gLAMP-X, a polyethylene glycol (PEG)-based nanoporous hydrogel partitions loop-mediated isothermal amplification (LAMP) into isolated nanoscopic microreactors, converting homogeneous amplification into a digital-like system in which each event forms a discrete fluorescent cluster for end point counting. Under optimized conditions, gLAMP-X achieved a limit of detection of 1.7 copies/μL within 20 min. In 90 pediatric throat swabs, gLAMP-X showed 100% sensitivity, 98.1% specificity, and strong quantitative agreement with qPCR.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2312–2323"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148222046","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":"Correction to “Mechanistic Insights into the Divergent Membrane Activities of a Viroporin from Chikungunya Virus and Its Transframe Variant”","authors":"Kirti Suhag,&nbsp;Subhomoi Borkotoky,&nbsp;Shumaila Iqbal Siddiqui,&nbsp;Jitender Kumar,&nbsp;Chandra Shekhar Kumar,&nbsp;Pushkar Tatiya,&nbsp;Subhendu Ghosh and Manidipa Banerjee*,&nbsp;","doi":"10.1021/acsinfecdis.6c00570","DOIUrl":"10.1021/acsinfecdis.6c00570","url":null,"abstract":"","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 7","pages":"2407–2408"},"PeriodicalIF":4.5,"publicationDate":"2026-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148300225","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}