{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T07:07:25Z","timestamp":1792048045621,"version":"4.4.0"},"reference-count":44,"publisher":"American Chemical Society (ACS)","issue":"10","license":[{"start":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T00:00:00Z","timestamp":1790208000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T00:00:00Z","timestamp":1790208000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T00:00:00Z","timestamp":1790208000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","award":["GT12053"],"award-info":[{"award-number":["GT12053"]}],"id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-21-CE44-0027"],"award-info":[{"award-number":["ANR-21-CE44-0027"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002915","name":"Fondation pour la Recherche M?dicale","doi-asserted-by":"publisher","award":["EQU202103012588"],"award-info":[{"award-number":["EQU202103012588"]}],"id":[{"id":"10.13039\/501100002915","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006342","name":"Association Vaincre la Mucoviscidose","doi-asserted-by":"publisher","award":["RF20230503223"],"award-info":[{"award-number":["RF20230503223"]}],"id":[{"id":"10.13039\/501100006342","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100031478","name":"NextGenerationEU","doi-asserted-by":"publisher","award":["09I01-03-V03-00001"],"award-info":[{"award-number":["09I01-03-V03-00001"]}],"id":[{"id":"10.13039\/100031478","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM131729"],"award-info":[{"award-number":["GM131729"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,9]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Patients infected with mycobacteria, particularly Mycobacterium abscessus, frequently experience antibiotic treatment failure. Phage therapy, used under compassionate care, offers a promising alternative and has already demonstrated clinical efficacy. However, phage-bacteria interactions and their coevolution remain critical factors that can compromise therapeutic success. Trehalose polyphleates (TPPs), complex lipids of the outer membrane, play a key role in the adhesion of the therapeutic mycobacteriophage BPs\u039433HTH_HRM10, and loss of TPP synthesis confers bacterial resistance to the phage. Herein, we found that deletion of the mycolyltransferase-encoding gene MSMEG_6398, but not of its homologues MSMEG_6396 or MSMEG_6399, all of which encode members of the Ag85 complex, increased resistance to BPs\u039433HTH_HRM10 on solid and liquid media. Alterations in the mycomembrane, the first barrier encountered by phages, were revealed by lipid profiling, while adhesion assays and flow cytometry indicated a defect at the binding stage. This effect was related to the accumulation of trehalose dimycolate (TDM) in the MSMEG_6398 mutant. The role of TDM in susceptibility\/resistance to BPs\u039433HTH_HRM10 was then demonstrated with a knockdown mutant of the arabinosyltransferase AftB involved in a terminal step of cell wall arabinan biosynthesis associated with TDM accumulation and further validated using ethambutol, a drug that induces TDM accumulation. Collectively, these findings suggest that TPPs may be masked by excess trehalose-bound lipids, reducing phage adsorption and preventing subsequent phage infection.<\/jats:p>","DOI":"10.1021\/acsinfecdis.6c00626","type":"journal-article","created":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T16:01:56Z","timestamp":1790265716000},"page":"3530-3542","source":"Crossref","is-referenced-by-count":1,"title":["Ag85A-Dependent\nSurface Lipid Remodeling Impairs Adhesion\nand Infection of Therapeutic Mycobacteriophage"],"prefix":"10.1021","volume":"12","author":[{"given":"Morgane","family":"Illouz","sequence":"first","affiliation":[{"name":"Universite\u0301 de Montpellier , , 1919 Route de Mende , ,","place":["Montpellier, France, 34293"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valentin","family":"Wasselin","sequence":"additional","affiliation":[{"name":"Univ Toulouse , , ,","place":["Toulouse, France, 31077"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adria\u0301n","family":"Pa\u0301l","sequence":"additional","affiliation":[{"name":"Comenius University in Bratislava , , ,","place":["Bratislava, Slovakia, 842 15"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Colin","family":"Lewis","sequence":"additional","affiliation":[{"name":"University of Pittsburgh , , , ,","place":["Pittsburgh, Pennsylvania, United States, 15260"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mae\u0308lle","family":"Foubert","sequence":"additional","affiliation":[{"name":"Universite\u0301 de Montpellier , , 1919 Route de Mende , ,","place":["Montpellier, France, 34293"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aurore","family":"Briand","sequence":"additional","affiliation":[{"name":"Universite\u0301 de Montpellier , , 1919 Route de Mende , ,","place":["Montpellier, France, 34293"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silke","family":"Malmsheimer","sequence":"additional","affiliation":[{"name":"Universite\u0301 de Montpellier , , 1919 Route de Mende , ,","place":["Montpellier, France, 34293"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4849-1369","authenticated-orcid":true,"given":"Christian","family":"Chalut","sequence":"additional","affiliation":[{"name":"Univ Toulouse , , ,","place":["Toulouse, France, 31077"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jana","family":"Kordula\u0301kova\u0301","sequence":"additional","affiliation":[{"name":"Comenius University in Bratislava , , ,","place":["Bratislava, Slovakia, 842 15"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Graham","family":"Hatfull","sequence":"additional","affiliation":[{"name":"University of Pittsburgh , , , ,","place":["Pittsburgh, Pennsylvania, United States, 15260"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6604-4458","authenticated-orcid":true,"given":"Laurent","family":"Kremer","sequence":"additional","affiliation":[{"name":"Universite\u0301 de Montpellier , , 1919 Route de Mende , ,","place":["Montpellier, France, 34293"]},{"name":"INSERM, IRIM , ,","place":["Montpellier, France, 34293"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,24]]},"reference":[{"issue":"10","key":"2026100909103947100_cit1","doi-asserted-by":"publisher","first-page":"926","DOI":"10.3390\/antibiotics13100926","article-title":"Mycobacteriophages\nand Their Applications","volume":"13","author":"Bonacorsi","year":"2024","journal-title":"Antibiotics"},{"issue":"7","key":"2026100909103947100_cit2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1010602","article-title":"Mycobacteriophages:\nFrom Petri Dish to Patient","volume":"18","author":"Hatfull","year":"2022","journal-title":"PLoS Pathog."},{"issue":"5","key":"2026100909103947100_cit3","doi-asserted-by":"publisher","first-page":"730","DOI":"10.1038\/s41591-019-0437-z","article-title":"Engineered\nBacteriophages for Treatment of a Patient with a Disseminated Drug-Resistant Mycobacterium abscessus","volume":"25","author":"Dedrick","year":"2019","journal-title":"Nat. Med."},{"issue":"1","key":"2026100909103947100_cit4","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1093\/cid\/ciac453","article-title":"Phage Therapy of Mycobacterium Infections: Compassionate Use of Phages in 20 Patients With Drug-Resistant\nMycobacterial Disease","volume":"76","author":"Dedrick","year":"2023","journal-title":"Clin. Infect. Dis."},{"issue":"11","key":"2026100909103947100_cit5","doi-asserted-by":"publisher","first-page":"1860","DOI":"10.1016\/j.cell.2022.04.024","article-title":"Host and\nPathogen Response to Bacteriophage Engineered\nagainst Mycobacterium abscessus Lung Infection","volume":"185","author":"Nick","year":"2022","journal-title":"Cell"},{"issue":"1","key":"2026100909103947100_cit6","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1007\/s41030-022-00210-y","article-title":"Phage Therapy\nfor Nontuberculous Mycobacteria: Challenges and Opportunities","volume":"9","author":"Hatfull","year":"2023","journal-title":"Pulm. Ther."},{"issue":"11","key":"2026100909103947100_cit7","doi-asserted-by":"publisher","first-page":"2925","DOI":"10.1016\/j.cell.2025.03.027","article-title":"Structure and Infection\nDynamics of Mycobacteriophage Bxb1","volume":"188","author":"Freeman","year":"2025","journal-title":"Cell"},{"key":"2026100909103947100_cit8","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1146\/annurev.bi.64.070195.000333","article-title":"The Envelope of Mycobacteria","volume":"64","author":"Brennan","year":"1995","journal-title":"Annu. Rev. Biochem."},{"issue":"1","key":"2026100909103947100_cit9","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.chembiol.2013.11.011","article-title":"Mycolic Acids: Structures, Biosynthesis,\nand Beyond","volume":"21","author":"Marrakchi","year":"2014","journal-title":"Chem. Biol."},{"issue":"Suppl","key":"2026100909103947100_cit10","doi-asserted-by":"publisher","first-page":"S3","DOI":"10.1016\/S1472-9792(13)70003-9","article-title":"Trehalose\n6,6\u2019-Dimycolate\n- a Coat to Regulate Tuberculosis Immunopathogenesis","volume":"93","author":"Welsh","year":"2013","journal-title":"Tuberculosis"},{"issue":"2","key":"2026100909103947100_cit11","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1046\/j.1462-5822.2003.00351.x","article-title":"Mycobacterium tuberculosis Cell Envelope Lipids and the\nHost Immune Response","volume":"6","author":"Karakousis","year":"2004","journal-title":"Cell. Microbiol."},{"issue":"3","key":"2026100909103947100_cit12","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.03959-25","article-title":"The Lipid Language of Tuberculosis: Mycobacterium tuberculosis Surface Molecules in Host Interaction and Drug\nResistance","volume":"17","author":"Radhakrishnan","year":"2026","journal-title":"mBio"},{"issue":"5317","key":"2026100909103947100_cit13","doi-asserted-by":"publisher","first-page":"1420","DOI":"10.1126\/science.276.5317.1420","article-title":"Role of the Major\nAntigen of Mycobacterium tuberculosis in Cell Wall Biogenesis","volume":"276","author":"Belisle","year":"1997","journal-title":"Science"},{"issue":"5","key":"2026100909103947100_cit14","doi-asserted-by":"publisher","first-page":"1573","DOI":"10.1046\/j.1365-2958.1999.01310.x","article-title":"Inactivation\nof the Antigen 85C Gene Profoundly Affects the Mycolate\nContent and Alters the Permeability of the Mycobacterium tuberculosis Cell Envelope","volume":"31","author":"Jackson","year":"1999","journal-title":"Mol. Microbiol."},{"issue":"4","key":"2026100909103947100_cit15","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1046\/j.1472-765x.2002.01091.x","article-title":"The M. tuberculosis Antigen 85 Complex and Mycolyltransferase\nActivity","volume":"34","author":"Kremer","year":"2002","journal-title":"Lett. Appl. Microbiol."},{"issue":"2","key":"2026100909103947100_cit16","doi-asserted-by":"publisher","first-page":"278","DOI":"10.1016\/j.chembiol.2015.11.013","article-title":"Trehalose Polyphleates\nAre Produced\nby a Glycolipid Biosynthetic Pathway Conserved across Phylogenetically\nDistant Mycobacteria","volume":"23","author":"Burbaud","year":"2016","journal-title":"Cell Chem. Biol."},{"issue":"12","key":"2026100909103947100_cit17","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.02970-24","article-title":"Trehalose Polyphleates\nParticipate in Mycobacterium abscessus Fitness and\nPathogenesis","volume":"15","author":"Malmsheimer","year":"2024","journal-title":"mBio"},{"issue":"3","key":"2026100909103947100_cit18","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/j.tube.2011.01.002","article-title":"Recent Advances in\nDeciphering the Contribution of Mycobacterium tuberculosis Lipids to Pathogenesis","volume":"91","author":"Neyrolles","year":"2011","journal-title":"Tuberculosis"},{"key":"2026100909103947100_cit19","doi-asserted-by":"publisher","first-page":"1145","DOI":"10.3389\/fmicb.2018.01145","article-title":"Glycopeptidolipids,\na Double-Edged Sword of the Mycobacterium abscessus Complex","volume":"9","author":"Gutie\u0301rrez","year":"2018","journal-title":"Front. Microbiol."},{"issue":"Pt 12","key":"2026100909103947100_cit20","doi-asserted-by":"publisher","first-page":"4050","DOI":"10.1099\/mic.0.033209-0","article-title":"Defects in Glycopeptidolipid Biosynthesis\nConfer Phage I3 Resistance\nin Mycobacterium smegmatis","volume":"155","author":"Chen","year":"2009","journal-title":"Microbiology"},{"issue":"9","key":"2026100909103947100_cit21","doi-asserted-by":"publisher","first-page":"1717","DOI":"10.1038\/s41564-023-01451-6","article-title":"Therapeutically Useful\nMycobacteriophages BPs and Muddy Require Trehalose Polyphleates","volume":"8","author":"Wetzel","year":"2023","journal-title":"Nat. Microbiol."},{"issue":"32","key":"2026100909103947100_cit22","doi-asserted-by":"publisher","first-page":"11184","DOI":"10.1074\/jbc.RA120.013299","article-title":"The Final\nAssembly of Trehalose Polyphleates Takes Place within the Outer Layer\nof the Mycobacterial Cell Envelope","volume":"295","author":"Thouvenel","year":"2020","journal-title":"J. Biol.\nChem."},{"issue":"19","key":"2026100909103947100_cit23","doi-asserted-by":"publisher","first-page":"6603","DOI":"10.1128\/JB.187.19.6603-6611.2005","article-title":"FbpA-Dependent Biosynthesis\nof Trehalose\nDimycolate Is Required for the Intrinsic Multidrug Resistance, Cell\nWall Structure, and Colonial Morphology of Mycobacterium smegmatis","volume":"187","author":"Nguyen","year":"2005","journal-title":"J. Bacteriol."},{"issue":"1","key":"2026100909103947100_cit24","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1128\/AAC.01316-18","article-title":"Mutations in the MAB_2299c TetR Regulator\nConfer Cross-Resistance to Clofazimine and Bedaquiline in Mycobacterium abscessus","volume":"63","author":"Richard","year":"2019","journal-title":"Antimicrob.\nAgents Chemother."},{"issue":"11","key":"2026100909103947100_cit25","doi-asserted-by":"publisher","first-page":"4828","DOI":"10.1128\/iai.61.11.4828-4834.1993","article-title":"Mechanism of Interaction of the 85B\nSecreted Protein of Mycobacterium bovis with Fibronectin","volume":"61","author":"Peake","year":"1993","journal-title":"Infect. Immun."},{"issue":"4","key":"2026100909103947100_cit26","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1038\/s41564-023-01333-x","article-title":"Mycobacterial\nNucleoid-Associated Protein Lsr2 Is Required for Productive Mycobacteriophage\nInfection","volume":"8","author":"Dulberger","year":"2023","journal-title":"Nat. Microbiol."},{"issue":"20","key":"2026100909103947100_cit27","doi-asserted-by":"publisher","first-page":"14729","DOI":"10.1074\/jbc.M700271200","article-title":"Identification\nof a Novel Arabinofuranosyltransferase\nAftB Involved in a Terminal Step of Cell Wall Arabinan Biosynthesis\nin Corynebacterianeae, Such as Corynebacterium glutamicum and Mycobacterium tuberculosis","volume":"282","author":"Seidel","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"1","key":"2026100909103947100_cit28","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1021\/acschembio.6b00898","article-title":"Disruption\nof Mycobacterial AftB Results in Complete\nLoss of Terminal \u03b2(1 \u2192 2) Arabinofuranose Residues of\nLipoarabinomannan","volume":"12","author":"Jankute","year":"2017","journal-title":"ACS Chem. Biol."},{"key":"2026100909103947100_cit29","doi-asserted-by":"publisher","first-page":"16274","DOI":"10.1038\/nmicrobiol.2016.274","article-title":"Programmable Transcriptional\nRepression in Mycobacteria Using an Orthogonal CRISPR Interference\nPlatform","volume":"2","author":"Rock","year":"2017","journal-title":"Nat. Microbiol."},{"issue":"21","key":"2026100909103947100_cit30","doi-asserted-by":"publisher","first-page":"11919","DOI":"10.1073\/pnas.93.21.11919","article-title":"The embAB Genes of Mycobacterium avium Encode an Arabinosyl\nTransferase Involved in Cell Wall Arabinan Biosynthesis That Is the\nTarget for the Antimycobacterial Drug Ethambutol","volume":"93","author":"Belanger","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"issue":"6496","key":"2026100909103947100_cit31","doi-asserted-by":"publisher","first-page":"1211","DOI":"10.1126\/science.aba9102","article-title":"Structures\nof Cell Wall Arabinosyltransferases with the Anti-Tuberculosis Drug\nEthambutol","volume":"368","author":"Zhang","year":"2020","journal-title":"Science"},{"issue":"5","key":"2026100909103947100_cit32","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1038\/nm0597-567","article-title":"The emb Operon, a Gene Cluster of Mycobacterium tuberculosis Involved in Resistance to Ethambutol","volume":"3","author":"Telenti","year":"1997","journal-title":"Nat.\nMed."},{"issue":"11","key":"2026100909103947100_cit33","doi-asserted-by":"publisher","first-page":"2484","DOI":"10.1128\/AAC.39.11.2484","article-title":"Biogenesis of the\nMycobacterial Cell Wall and the Site of Action of Ethambutol","volume":"39","author":"Mikusova\u0301","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"2026100909103947100_cit34","doi-asserted-by":"publisher","DOI":"10.4014\/jmb.2509.09030","article-title":"Clinical and\nTranslational Perspectives\non Bacteriophage Therapy for Nontuberculous Mycobacterial Diseases","volume":"35","author":"Ash","year":"2025","journal-title":"J. Microbiol. Biotechnol."},{"key":"2026100909103947100_cit35","doi-asserted-by":"publisher","DOI":"10.1128\/jb.00375-25","article-title":"Steering the Course:\nTargeting and Exploiting Surface\nReceptors in Phage Therapy","volume":"208","author":"Tran","year":"2026","journal-title":"J. Bacteriol."},{"issue":"5","key":"2026100909103947100_cit36","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1021\/acsinfecdis.6b00179","article-title":"A Screen for Protein-Protein\nInteractions in Live Mycobacteria\nReveals a Functional Link between the Virulence-Associated Lipid Transporter\nLprG and the Mycolyltransferase Antigen 85A","volume":"3","author":"Touchette","year":"2017","journal-title":"ACS Infect. Dis."},{"key":"2026100909103947100_cit37","doi-asserted-by":"publisher","DOI":"10.1128\/jb.00240-26","article-title":"Ag85A Loss Promotes Free Mycolate\nAccumulation and Sensitizes Plasma Membrane Domain to Disruption","volume":"208","author":"Kado","year":"2026","journal-title":"J. Bacteriol."},{"issue":"36","key":"2026100909103947100_cit38","doi-asserted-by":"publisher","first-page":"25041","DOI":"10.1074\/jbc.M114.581579","article-title":"The Three Mycobacterium tuberculosis Antigen 85 Isoforms Have Unique\nSubstrates and Activities Determined by Non-Active Site Regions","volume":"289","author":"Backus","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2026100909103947100_cit39","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.79981","article-title":"Phage Resistance\nProfiling Identifies New Genes Required\nfor Biogenesis and Modification of the Corynebacterial Cell Envelope","volume":"11","author":"McKitterick","year":"2022","journal-title":"Elife"},{"issue":"29","key":"2026100909103947100_cit40","doi-asserted-by":"publisher","first-page":"21908","DOI":"10.1074\/jbc.C110.133033","article-title":"O-Mycoloylated Proteins from Corynebacterium: An Unprecedented Post-Translational Modification\nin Bacteria","volume":"285","author":"Huc","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"5","key":"2026100909103947100_cit41","doi-asserted-by":"publisher","first-page":"1612","DOI":"10.1128\/JB.187.5.1612-1620.2005","article-title":"An Unusual\nMutation Results in the Replacement of Diaminopimelate with Lanthionine\nin the Peptidoglycan of a Mutant Strain of Mycobacterium smegmatis","volume":"187","author":"Consaul","year":"2005","journal-title":"J. Bacteriol."},{"issue":"Pt 10","key":"2026100909103947100_cit42","doi-asserted-by":"publisher","first-page":"3145","DOI":"10.1099\/00221287-148-10-3145","article-title":"Temperature-Induced\nChanges in the Cell-Wall Components of Mycobacterium thermoresistibile","volume":"148","author":"Kremer","year":"2002","journal-title":"Microbiology"},{"issue":"15","key":"2026100909103947100_cit43","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gks596","article-title":"Primer3 - New Capabilities and Interfaces","volume":"40","author":"Untergasser","year":"2012","journal-title":"Nucleic Acids Res."},{"issue":"7","key":"2026100909103947100_cit44","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image\nto ImageJ: 25 Years of\nImage Analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"}],"container-title":["ACS Infectious\nDiseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acsinfecdis.6c00626","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article-pdf\/12\/10\/3530\/68640991\/acsinfecdis.6c00626.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article-pdf\/12\/10\/3530\/68640991\/acsinfecdis.6c00626.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T13:49:36Z","timestamp":1791553776000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article\/12\/10\/3530\/5437795\/Ag85A-Dependent-Surface-Lipid-Remodeling-Impairs"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,24]]},"references-count":44,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2026,9,24]]},"published-print":{"date-parts":[[2026,10,9]]}},"URL":"https:\/\/doi.org\/10.1021\/acsinfecdis.6c00626","relation":{},"ISSN":["2373-8227"],"issn-type":[{"value":"2373-8227","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,24]]}}}