{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:43:13Z","timestamp":1791852193033,"version":"4.3.4"},"update-to":[{"DOI":"10.1371\/journal.ppat.1014043","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T00:00:00Z","timestamp":1773705600000}}],"reference-count":81,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T00:00:00Z","timestamp":1773187200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"crossref","award":["ANR-21-CE44-0002 ENIgMA"],"award-info":[{"award-number":["ANR-21-CE44-0002 ENIgMA"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Mycoplasmas are genome-reduced, parasitic bacteria colonizing a broad range of organisms, including most livestock species and humans. They are often pathogenic, and have evolved an arsenal of mechanisms to counter their host\u2019s immune response. Among these, the Mycoplasma Immunoglobulin Binding\/Protease (MIB-MIP) system appears to be particularly important, and is conserved in the majority of mycoplasma species. Through genomics analysis, we show that MIB-MIP systematically co-occurs with a cluster of 7 coding sequences corresponding to an atypical Type 3 F-ATPase termed \u201cF\n                    <jats:sub>1<\/jats:sub>\n                    -like X\n                    <jats:sub>0<\/jats:sub>\n                    \u201d. Working in the model organism\n                    <jats:italic>Mycoplasma mycoides<\/jats:italic>\n                    subsp.\n                    <jats:italic>capri<\/jats:italic>\n                    , we first performed a proteomics analysis to confirm that this ATPase is indeed expressed. We then generated two mutant strains in which the putative ATPase was either fully deleted, or rendered catalytically inactive through replacement of a conserved lysine residue in the Walker A motif of the ATPase \u03b2-like subunit. Functional assays in presence of immune serum showed that both mutants are unable to protect themselves from agglutination by immunoglobulins despite the MIB-MIP system still being present. We then attempted to affinity-purify the atypical F\n                    <jats:sub>1<\/jats:sub>\n                    -like X\n                    <jats:sub>0<\/jats:sub>\n                    ATPase from the membrane of its native host. Although the complex appears to be labile, under cross-linking conditions we were able to co-purify all its predicted components, as well as both MIB and MIP. These results allow us to attribute a function to Type 3 F-ATPase, namely to participate in the evasion from the humoral immune response in mycoplasmas, in conjunction with the MIB-MIP system through a currently unknown mechanism.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1014043","type":"journal-article","created":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T17:37:34Z","timestamp":1773250654000},"page":"e1014043","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":3,"title":["An atypical F-type ATPase is necessary for the function of the antibody cleavage system MIB-MIP in mycoplasmas"],"prefix":"10.1371","volume":"22","author":[{"given":"Julien","family":"Berlureau","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robin","family":"Anger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emilie","family":"Beaulieu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geraldine","family":"Gourgues","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laure","family":"Bataille","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jade","family":"Jaubert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carole","family":"Lartigue","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pascal","family":"Sirand-Pugnet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6064-7899","authenticated-orcid":true,"given":"Yonathan","family":"Arfi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2026,3,11]]},"reference":[{"issue":"10","key":"ppat.1014043.ref001","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1016\/j.resmic.2007.09.007","article-title":"Evolution of mollicutes: down a bumpy road with twists and turns","volume":"158","author":"P Sirand-Pugnet","year":"2007","journal-title":"Res Microbiol"},{"key":"ppat.1014043.ref002","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/msb.2013.6","article-title":"Dissecting the energy metabolism in Mycoplasma pneumoniae through genome-scale metabolic modeling","volume":"9","author":"JAH Wodke","year":"2013","journal-title":"Mol Syst Biol"},{"issue":"9","key":"ppat.1014043.ref003","doi-asserted-by":"crossref","first-page":"107722","DOI":"10.1016\/j.celrep.2020.107722","article-title":"Inferring Active Metabolic Pathways from Proteomics and Essentiality Data","volume":"31","author":"A Montero-Blay","year":"2020","journal-title":"Cell Rep"},{"issue":"1","key":"ppat.1014043.ref004","doi-asserted-by":"crossref","first-page":"9679","DOI":"10.1038\/s41467-024-53975-y","article-title":"A tuneable minimal cell membrane reveals that two lipid species suffice for life","volume":"15","author":"I Justice","year":"2024","journal-title":"Nat Commun"},{"issue":"2","key":"ppat.1014043.ref005","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1056\/NEJM198101083040204","article-title":"Mycoplasmas as agents of human disease","volume":"304","author":"GH Cassell","year":"1981","journal-title":"N Engl J Med"},{"issue":"4","key":"ppat.1014043.ref006","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.tim.2013.01.003","article-title":"Mycoplasmas and their host: emerging and re-emerging minimal pathogens","volume":"21","author":"C Citti","year":"2013","journal-title":"Trends Microbiol"},{"issue":"4","key":"ppat.1014043.ref007","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1128\/MMBR.62.4.1094-1156.1998","article-title":"Molecular biology and pathogenicity of mycoplasmas","volume":"62","author":"S Razin","year":"1998","journal-title":"Microbiol Mol Biol Rev"},{"key":"ppat.1014043.ref008","doi-asserted-by":"crossref","DOI":"10.2741\/minion","article-title":"Molecular pathogenesis of mycoplasma animal respiratory pathogens","volume":"7","author":"FC Minion","year":"2002","journal-title":"Front Biosci"},{"issue":"4","key":"ppat.1014043.ref009","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1128\/CMR.17.4.697-728.2004","article-title":"Mycoplasma pneumoniae and its role as a human pathogen","volume":"17","author":"KB Waites","year":"2004","journal-title":"Clin Microbiol Rev"},{"key":"ppat.1014043.ref010","first-page":"578","article-title":"Genital mycoplasma infections","volume":"109","author":"D Taylor-Robinson","year":"1997","journal-title":"Wien Klin Wochenschr"},{"key":"ppat.1014043.ref011","article-title":"Interactions of mycoplasmas with B cells: antibody production and nonspecific effects","author":"JW Simecka","year":"1993","journal-title":"Clin Infect Dis"},{"key":"ppat.1014043.ref012","doi-asserted-by":"crossref","first-page":"108541","DOI":"10.1016\/j.vetmic.2019.108541","article-title":"Differential innate immune responses induced by Mycoplasma hyopneumoniae and Mycoplasma hyorhinis in various types of antigen presenting cells","volume":"240","author":"BS Trueeb","year":"2020","journal-title":"Vet Microbiol"},{"key":"ppat.1014043.ref013","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3389\/fmicb.2016.00039","article-title":"Antibody response to Mycoplasma pneumoniae: protection of host and influence on outbreaks?","volume":"7","author":"R Dumke","year":"2016","journal-title":"Front Microbiol"},{"key":"ppat.1014043.ref014","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0139678","article-title":"Whole blood transcriptome analysis of Mycoplasma Mycoides subsp. Mycoides-infected cattle confirms immunosuppression but does not reflect local inflammation","volume":"10","author":"V Rodrigues","year":"2015","journal-title":"PLoS One"},{"issue":"6","key":"ppat.1014043.ref015","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01974-21","article-title":"Beware of Mycoplasma Anti-immunoglobulin Strategies","volume":"12","author":"Y Arfi","year":"2021","journal-title":"mBio"},{"key":"ppat.1014043.ref016","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1099\/mic.0.045641-0","article-title":"Mycoplasma gallisepticum and Mycoplasma synoviae express a cysteine protease CysP, which can cleave chicken IgG into Fab and Fc","volume":"157","author":"I Cizelj","year":"2011","journal-title":"Microbiology (Reading)"},{"issue":"6","key":"ppat.1014043.ref017","doi-asserted-by":"crossref","first-page":"2544","DOI":"10.1128\/iai.60.6.2544-2546.1992","article-title":"Characterization of the immunoglobulin A protease of Ureaplasma urealyticum","volume":"60","author":"RK Spooner","year":"1992","journal-title":"Infect Immun"},{"key":"ppat.1014043.ref018","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.vetmic.2018.03.002","article-title":"The major membrane nuclease MnuA degrades neutrophil extracellular traps induced by Mycoplasma bovis","volume":"218","author":"F Mitiku","year":"2018","journal-title":"Vet Microbiol"},{"issue":"6171","key":"ppat.1014043.ref019","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1126\/science.1246135","article-title":"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union","volume":"343","author":"RK Grover","year":"2014","journal-title":"Science"},{"key":"ppat.1014043.ref020","doi-asserted-by":"crossref","first-page":"685","DOI":"10.3389\/fmicb.2020.00685","article-title":"Characterization of an Immunoglobulin Binding Protein (IbpM) From Mycoplasma pneumoniae","volume":"11","author":"C Bl\u00f6tz","year":"2020","journal-title":"Front Microbiol"},{"key":"ppat.1014043.ref021","article-title":"The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction","author":"P Nottelet","year":"2021","journal-title":"Sci Adv"},{"issue":"19","key":"ppat.1014043.ref022","doi-asserted-by":"crossref","first-page":"5406","DOI":"10.1073\/pnas.1600546113","article-title":"MIB-MIP is a mycoplasma system that captures and cleaves immunoglobulin G","volume":"113","author":"Y Arfi","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"ppat.1014043.ref023","doi-asserted-by":"crossref","DOI":"10.1128\/spectrum.01873-23","article-title":"Improved transformation efficiency in Mycoplasma hominis enables disruption of the MIB-MIP system targeting human immunoglobulins","volume":"11","author":"J Guiraud","year":"2023","journal-title":"Microbiol 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Microbiol"},{"issue":"6","key":"ppat.1014043.ref027","doi-asserted-by":"crossref","first-page":"16054","DOI":"10.1038\/nmicrobiol.2016.54","article-title":"Microbially cleaved immunoglobulins are sensed by the innate immune receptor LILRA2","volume":"1","author":"K Hirayasu","year":"2016","journal-title":"Nat Microbiol"},{"issue":"6","key":"ppat.1014043.ref028","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0038793","article-title":"Specific evolution of F1-like ATPases in mycoplasmas","volume":"7","author":"L B\u00e9ven","year":"2012","journal-title":"PLoS One"},{"issue":"4","key":"ppat.1014043.ref029","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01414-21","article-title":"Chained Structure of Dimeric F1-like ATPase in Mycoplasma mobile Gliding Machinery","volume":"12","author":"T Toyonaga","year":"2021","journal-title":"mBio"},{"issue":"6","key":"ppat.1014043.ref030","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.02846-19","article-title":"Refined Mechanism of Mycoplasma mobile Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery","volume":"10","author":"MS Nishikawa","year":"2019","journal-title":"mBio"},{"key":"ppat.1014043.ref031","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.bbabio.2006.01.001","article-title":"The peripheral stalk of the mitochondrial ATP synthase","volume":"1757","author":"JE Walker","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"ppat.1014043.ref032","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.bbamem.2004.04.011","article-title":"Membrane proteins, lipids and detergents: not just a soap opera","volume":"1666","author":"AM Seddon","year":"2004","journal-title":"Biochim Biophys Acta"},{"issue":"5948","key":"ppat.1014043.ref033","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1126\/science.1173759","article-title":"Creating bacterial strains from genomes that have been cloned and engineered in yeast","volume":"325","author":"C Lartigue","year":"2009","journal-title":"Science"},{"issue":"1","key":"ppat.1014043.ref034","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1021\/acssynbio.5b00196","article-title":"In-Yeast Engineering of a Bacterial Genome Using CRISPR\/Cas9","volume":"5","author":"I Tsarmpopoulos","year":"2016","journal-title":"ACS Synth Biol"},{"issue":"8","key":"ppat.1014043.ref035","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1002\/j.1460-2075.1982.tb01276.x","article-title":"Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold","volume":"1","author":"JE Walker","year":"1982","journal-title":"EMBO J"},{"issue":"13","key":"ppat.1014043.ref036","doi-asserted-by":"crossref","first-page":"2709","DOI":"10.1016\/j.jmb.2016.04.029","article-title":"Walker-A Motif Acts to Coordinate ATP Hydrolysis with Motor Output in Viral DNA Packaging","volume":"428","author":"D delToro","year":"2016","journal-title":"J Mol Biol"},{"key":"ppat.1014043.ref037","article-title":"Evolution et caract\u00e9risation fonctionnelle d\u2019une ATPase de type F1-like X0 sp\u00e9cifique des mycoplasmes","author":"C Charenton","year":"2012"},{"issue":"1","key":"ppat.1014043.ref038","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.jcpa.2010.06.004","article-title":"Comparison of isolates of Mycoplasma mycoides subspecies capri from asymptomatic and septicaemic goats","volume":"144","author":"F Tardy","year":"2011","journal-title":"J Comp Pathol"},{"issue":"1","key":"ppat.1014043.ref039","doi-asserted-by":"crossref","first-page":"4403","DOI":"10.1038\/s41467-019-12301-7","article-title":"The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications","volume":"10","author":"H G\u00f6tzke","year":"2019","journal-title":"Nat Commun"},{"issue":"6","key":"ppat.1014043.ref040","doi-asserted-by":"crossref","first-page":"1760","DOI":"10.1073\/pnas.0813167106","article-title":"Detergent binding explains anomalous SDS-PAGE migration of membrane proteins","volume":"106","author":"A Rath","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"15","key":"ppat.1014043.ref041","doi-asserted-by":"crossref","DOI":"10.21769\/BioProtoc.4478","article-title":"DSP-crosslinking and Immunoprecipitation to Isolate Weak Protein Complex","volume":"12","author":"K Akaki","year":"2022","journal-title":"Bio Protoc"},{"key":"ppat.1014043.ref042","doi-asserted-by":"crossref","first-page":"19518","DOI":"10.1073\/pnas.0704280104","article-title":"Cytoskeletal \u201cjellyfish\u201d structure of Mycoplasma mobile","volume":"104","author":"D Nakane","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"9","key":"ppat.1014043.ref043","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adr9319","article-title":"Dimeric assembly of F1-like ATPase for the gliding motility of Mycoplasma","volume":"11","author":"T Toyonaga","year":"2025","journal-title":"Sci Adv"},{"issue":"10","key":"ppat.1014043.ref044","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1128\/JB.01418-13","article-title":"Localization of P42 and F(1)-ATPase \u03b1-subunit homolog of the gliding machinery in Mycoplasma mobile revealed by newly developed gene manipulation and fluorescent protein tagging","volume":"196","author":"I Tulum","year":"2014","journal-title":"J Bacteriol"},{"issue":"1","key":"ppat.1014043.ref045","doi-asserted-by":"crossref","first-page":"3792","DOI":"10.1038\/s41598-020-60535-z","article-title":"Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile","volume":"10","author":"I Tulum","year":"2020","journal-title":"Sci Rep"},{"key":"ppat.1014043.ref046","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.mib.2015.08.010","article-title":"Prospects for the gliding mechanism of Mycoplasma mobile","volume":"29","author":"M Miyata","year":"2016","journal-title":"Curr Opin Microbiol"},{"issue":"8","key":"ppat.1014043.ref047","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1101\/gr.2674004","article-title":"The complete genome and proteome of Mycoplasma mobile","volume":"14","author":"JD Jaffe","year":"2004","journal-title":"Genome Res"},{"key":"ppat.1014043.ref048","article-title":"Imaging minimal bacteria at the nanoscale: a reliable and versatile process to perform Single Molecule Localization Microscopy in mycoplasmas","author":"F Rideau","year":"2022","journal-title":"bioRxiv"},{"key":"ppat.1014043.ref049","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1007\/978-1-4939-9869-2_5","article-title":"ATP synthase: Expression, purification, and function","author":"M Sobti","year":"2020","journal-title":"Methods Mol Biol"},{"key":"ppat.1014043.ref050","article-title":"Structure of a bacterial ATP synthase","volume":"8","author":"H Guo","year":"2019","journal-title":"Elife"},{"issue":"7","key":"ppat.1014043.ref051","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abl5966","article-title":"Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii","volume":"8","author":"JK Demmer","year":"2022","journal-title":"Sci Adv"},{"issue":"11","key":"ppat.1014043.ref052","doi-asserted-by":"crossref","first-page":"3746","DOI":"10.1128\/jb.179.11.3746-3755.1997","article-title":"Composition and primary structure of the F1F0 ATP synthase from the obligately anaerobic bacterium Clostridium thermoaceticum","volume":"179","author":"A Das","year":"1997","journal-title":"J Bacteriol"},{"issue":"4","key":"ppat.1014043.ref053","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1038\/s41594-024-01219-4","article-title":"Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F1-Fo coupling","volume":"31","author":"S Sharma","year":"2024","journal-title":"Nat Struct Mol Biol"},{"key":"ppat.1014043.ref054","doi-asserted-by":"crossref","DOI":"10.1126\/science.aat4318","article-title":"Structure, mechanism, and regulation of the chloroplast ATP synthase","volume":"360","author":"A Hahn","year":"2018","journal-title":"Science"},{"issue":"8","key":"ppat.1014043.ref055","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2021012118","article-title":"Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes","volume":"118","author":"TE Spikes","year":"2021","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"12","key":"ppat.1014043.ref056","doi-asserted-by":"crossref","first-page":"183341","DOI":"10.1016\/j.bbamem.2020.183341","article-title":"Regulation and function of V-ATPases in physiology and disease","volume":"1862","author":"MP Collins","year":"2020","journal-title":"Biochim Biophys Acta Biomembr"},{"issue":"1","key":"ppat.1014043.ref057","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/1574-6968.12026","article-title":"Analysis of energy sources for Mycoplasma penetrans gliding motility","volume":"338","author":"DA Jurkovic","year":"2013","journal-title":"FEMS Microbiol Lett"},{"issue":"3","key":"ppat.1014043.ref058","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1128\/jb.92.3.714-722.1966","article-title":"Adenosine triphosphatase activity of mycoplasma membranes","volume":"92","author":"S Rottem","year":"1966","journal-title":"J Bacteriol"},{"issue":"3","key":"ppat.1014043.ref059","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1128\/jb.145.3.1299-1304.1981","article-title":"Proton motive force across the membrane of Mycoplasma gallisepticum and its possible role in cell volume regulation","volume":"145","author":"S Rottem","year":"1981","journal-title":"J Bacteriol"},{"issue":"1","key":"ppat.1014043.ref060","first-page":"61","article-title":"Immunoglobulin A1 protease activity in strains of Ureaplasma urealyticum","volume":"92","author":"M Kilian","year":"1984","journal-title":"Acta Pathol Microbiol Immunol Scand B"},{"issue":"1","key":"ppat.1014043.ref061","doi-asserted-by":"crossref","first-page":"7801","DOI":"10.1038\/s41467-022-35340-z","article-title":"Extensive substrate recognition by the streptococcal antibody-degrading enzymes IdeS and EndoS","volume":"13","author":"ASL Sudol","year":"2022","journal-title":"Nat Commun"},{"key":"ppat.1014043.ref062","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1134\/S0006297911030023","article-title":"IgG-binding proteins of bacteria","volume":"76","author":"EV Sidorin","year":"2011","journal-title":"Biochemistry (Mosc)"},{"issue":"1","key":"ppat.1014043.ref063","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.vetmic.2013.10.025","article-title":"Characterization of the in vitro core surface proteome of Mycoplasma mycoides subsp. mycoides, the causative agent of contagious bovine pleuropneumonia","volume":"168","author":"I Krasteva","year":"2014","journal-title":"Vet Microbiol"},{"key":"ppat.1014043.ref064","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.jprot.2015.10.016","article-title":"Proteomic characterization of pleural effusion, a specific host niche of Mycoplasma mycoides subsp. mycoides from cattle with contagious bovine pleuropneumonia (CBPP)","volume":"131","author":"YB Weldearegay","year":"2016","journal-title":"J Proteomics"},{"issue":"2","key":"ppat.1014043.ref065","doi-asserted-by":"crossref","first-page":"150210","DOI":"10.1098\/rsob.150210","article-title":"Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae","volume":"6","author":"JL Tacchi","year":"2016","journal-title":"Open Biol"},{"key":"ppat.1014043.ref066","doi-asserted-by":"crossref","first-page":"106034","DOI":"10.1016\/j.dib.2020.106034","article-title":"Data on proteome of Mycoplasma hominis cultivated with arginine or thymidine as a carbon source","volume":"31","author":"TA Semashko","year":"2020","journal-title":"Data Brief"},{"key":"ppat.1014043.ref067","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1186\/1471-2180-10-225","article-title":"The liposoluble proteome of Mycoplasma agalactiae: an insight into the minimal protein complement of a bacterial membrane","volume":"10","author":"C Cacciotto","year":"2010","journal-title":"BMC Microbiol"},{"issue":"6","key":"ppat.1014043.ref068","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01974-21","article-title":"Beware of Mycoplasma Anti-immunoglobulin Strategies","volume":"12","author":"Y Arfi","year":"2021","journal-title":"mBio"},{"key":"ppat.1014043.ref069","doi-asserted-by":"crossref","DOI":"10.1128\/microbiolspec.ARBA-0030-2018","article-title":"Antimicrobial Resistance in Mycoplasma spp","volume":"6","author":"AV Gautier-Bouchardon","year":"2018","journal-title":"Microbiol Spectr"},{"issue":"5707","key":"ppat.1014043.ref070","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1126\/science.1106753","article-title":"A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis","volume":"307","author":"K Andries","year":"2005","journal-title":"Science"},{"issue":"7","key":"ppat.1014043.ref071","doi-asserted-by":"crossref","first-page":"1292","DOI":"10.1016\/j.bmc.2019.02.026","article-title":"3,5-Dialkoxypyridine analogues of bedaquiline are potent antituberculosis agents with minimal inhibition of the hERG channel","volume":"27","author":"HS Sutherland","year":"2019","journal-title":"Bioorg Med 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