{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T08:44:21Z","timestamp":1785833061749,"version":"3.56.0"},"reference-count":145,"publisher":"Public Library of Science (PLoS)","issue":"6","license":[{"start":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T00:00:00Z","timestamp":1782259200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 AI30100"],"award-info":[{"award-number":["R01 AI30100"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 AI054476"],"award-info":[{"award-number":["R01 AI054476"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Research Fund for Tick-Borne Diseases","award":["NRFTD-2011"],"award-info":[{"award-number":["NRFTD-2011"]}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    <jats:italic>Anaplasma phagocytophilum<\/jats:italic>\n                    is an obligatory intracellular bacterium that causes an emerging infectious disease, human granulocytic anaplasmosis. It undergoes a biphasic developmental cycle inside membrane-bound vacuoles within the host human neutrophils, maturing from a proliferating reticulate cell form to an infectious dense core (DC) form that is subsequently spontaneously released from host cells to initiate a new infection cycle. However, how\n                    <jats:italic>A. phagocytophilum<\/jats:italic>\n                    coordinates growth and release is unknown. Here, we found localized cortical F-actin disruption occurs where\n                    <jats:italic>Anaplasma-<\/jats:italic>\n                    containing vacuoles abut on the plasma membrane to release bacteria. Disruption of actin filaments by cytochalasin D and latrunculin B induced unrestrained release of almost all intracellular\n                    <jats:italic>A. phagocytophilum<\/jats:italic>\n                    from host cells, which were significantly less infectious than spontaneously released bacteria.\n                    <jats:italic>A. phagocytophilum<\/jats:italic>\n                    AnkA, a type IV secretion system (T4SS) effector, was found to localize in the cell periphery with cortical F-actin. By immunoprecipitation followed by mass spectrometry, AnkA was found to interact with actin, \u03b1-actinin 4 (Actn4) involved in actin cross-linking, and gelsolin for actin filament remodeling. shRNA-knockdown of Actn4 or gelsolin, enhanced release of premature\n                    <jats:italic>A. phagocytophilum<\/jats:italic>\n                    . Glutathione S-transferase (GST)-tagged C-terminus of AnkA (AnkA-C) interacted with actin and gelsolin, whereas the N-terminus (AnkA-N) interacted with Actn4.\n                    <jats:italic>In vitro<\/jats:italic>\n                    pyrene-actin polymerization assay showed that GST-AnkA-C has stronger actin polymerizing activity than GST-AnkA or GST-AnkA-N. Ectopically expressed GFP-AnkA-N localized to the plasma membrane and induced membrane ruffling, whereas GFP-AnkA-C colocalized with and enhanced stress fiber formation. These results demonstrate that AnkA is the first example of bacterial molecules interacting with gelsolin and Actn4. The result suggests that by colocalizing with cortical F-actin and controlling F-actin dynamics and cross-linking, AnkA regulates spatiotemporal release of\n                    <jats:italic>A. phagocytophilum<\/jats:italic>\n                    . The current study unravels a new paradigm of retention\/release mechanism of intracellular pathogen regulated by a T4SS effector.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1014350","type":"journal-article","created":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T17:28:49Z","timestamp":1782322129000},"page":"e1014350","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":1,"title":["Obligatory intracellular bacterium Anaplasma phagocytophilum AnkA regulates actin dynamics and spatiotemporal bacterial release"],"prefix":"10.1371","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9964-5460","authenticated-orcid":true,"given":"Mingqun","family":"Lin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nan","family":"Duan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuko","family":"Rikihisa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2026,6,24]]},"reference":[{"key":"ppat.1014350.ref001","doi-asserted-by":"crossref","first-page":"2145","DOI":"10.1099\/00207713-51-6-2145","article-title":"Reorganization of genera in the families Rickettsiaceae and Anaplasmataceae in the order Rickettsiales: unification of some species of Ehrlichia with Anaplasma, Cowdria with Ehrlichia and Ehrlichia with Neorickettsia, descriptions of six new species combinations and designation of Ehrlichia equi and \u201cHGE agent\u201d as subjective synonyms of Ehrlichia phagocytophila","volume":"51","author":"JS Dumler","year":"2001","journal-title":"Int J Syst Evol Microbiol"},{"key":"ppat.1014350.ref002","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.vetpar.2009.09.017","article-title":"Molecular events involved in cellular invasion by Ehrlichia chaffeensis and Anaplasma phagocytophilum","volume":"167","author":"Y Rikihisa","year":"2010","journal-title":"Vet Parasitol"},{"issue":"1","key":"ppat.1014350.ref003","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.cll.2009.10.004","article-title":"Human ehrlichiosis and anaplasmosis","volume":"30","author":"N Ismail","year":"2010","journal-title":"Clin Lab Med"},{"issue":"3","key":"ppat.1014350.ref004","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1128\/jcm.32.3.589-595.1994","article-title":"Identification of a granulocytotropic Ehrlichia species as the etiologic agent of human disease","volume":"32","author":"SM Chen","year":"1994","journal-title":"J Clin Microbiol"},{"issue":"3","key":"ppat.1014350.ref005","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1001\/jama.1994.03520030054028","article-title":"Human granulocytic ehrlichiosis in the upper Midwest United States. A new species emerging?","volume":"272","author":"JS Bakken","year":"1994","journal-title":"JAMA"},{"key":"ppat.1014350.ref006","article-title":"Ehrlichioses in humans: epidemiology, clinical presentation, diagnosis, and treatment","author":"JS Dumler","year":"2007","journal-title":"Clin Infect Dis"},{"issue":"4","key":"ppat.1014350.ref007","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1056\/NEJM199601253340401","article-title":"Direct cultivation of the causative agent of human granulocytic ehrlichiosis","volume":"334","author":"JL Goodman","year":"1996","journal-title":"N Engl J Med"},{"issue":"3","key":"ppat.1014350.ref008","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.idc.2008.03.011","article-title":"Human granulocytic anaplasmosis","volume":"22","author":"JS Bakken","year":"2008","journal-title":"Infect Dis Clin North Am"},{"issue":"2","key":"ppat.1014350.ref009","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.0020021","article-title":"Comparative genomics of emerging human ehrlichiosis agents","volume":"2","author":"JC Dunning Hotopp","year":"2006","journal-title":"PLoS Genet"},{"issue":"1","key":"ppat.1014350.ref010","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.mib.2005.12.003","article-title":"Ehrlichia subversion of host innate responses","volume":"9","author":"Y Rikihisa","year":"2006","journal-title":"Curr Opin Microbiol"},{"key":"ppat.1014350.ref011","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1111\/j.1749-6632.2003.tb07425.x","article-title":"Mechanisms to create a safe haven by members of the family Anaplasmataceae","volume":"990","author":"Y Rikihisa","year":"2003","journal-title":"Ann N Y Acad Sci"},{"issue":"5","key":"ppat.1014350.ref012","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1038\/nrmicro2318","article-title":"Anaplasma phagocytophilum and Ehrlichia chaffeensis: subversive manipulators of host cells","volume":"8","author":"Y Rikihisa","year":"2010","journal-title":"Nat Rev Microbiol"},{"issue":"3","key":"ppat.1014350.ref013","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1111\/j.1462-5822.2007.01068.x","article-title":"Subversion of cellular autophagy by Anaplasma phagocytophilum","volume":"10","author":"H Niu","year":"2008","journal-title":"Cell Microbiol"},{"issue":"3","key":"ppat.1014350.ref014","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1128\/CMR.00064-10","article-title":"Mechanisms of obligatory intracellular infection with Anaplasma phagocytophilum","volume":"24","author":"Y Rikihisa","year":"2011","journal-title":"Clin Microbiol Rev"},{"issue":"1","key":"ppat.1014350.ref015","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.vetmic.2004.02.011","article-title":"Infection of endothelial cells with Anaplasma marginale and A. phagocytophilum","volume":"101","author":"UG Munderloh","year":"2004","journal-title":"Vet Microbiol"},{"key":"ppat.1014350.ref016","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1196\/annals.1355.090","article-title":"The interactions of Anaplasma phagocytophilum, endothelial cells, and human neutrophils","volume":"1063","author":"MJ Herron","year":"2005","journal-title":"Ann N Y Acad Sci"},{"issue":"1","key":"ppat.1014350.ref017","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1111\/2049-632X.12111","article-title":"Comparison and characterization of granulocyte cell models for Anaplasma phagocytophilum infection","volume":"71","author":"KE Rennoll-Bankert","year":"2014","journal-title":"Pathog Dis"},{"issue":"9","key":"ppat.1014350.ref018","doi-asserted-by":"crossref","first-page":"4018","DOI":"10.1128\/IAI.00527-09","article-title":"Anaplasma phagocytophilum dense-cored organisms mediate cellular adherence through recognition of human P-selectin glycoprotein ligand 1","volume":"77","author":"MJ Troese","year":"2009","journal-title":"Infect Immun"},{"issue":"3","key":"ppat.1014350.ref019","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1111\/j.1462-5822.2005.00643.x","article-title":"Differential expression of VirB9 and VirB6 during the life cycle of Anaplasma phagocytophilum in human leucocytes is associated with differential binding and avoidance of lysosome pathway","volume":"8","author":"H Niu","year":"2006","journal-title":"Cell Microbiol"},{"issue":"6","key":"ppat.1014350.ref020","doi-asserted-by":"crossref","first-page":"719","DOI":"10.2217\/fmb.12.45","article-title":"Anaplasma phagocytophilum: deceptively simple or simply deceptive?","volume":"7","author":"MS Severo","year":"2012","journal-title":"Future microbiology"},{"issue":"10","key":"ppat.1014350.ref021","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.01972-25","article-title":"Distinct modes of cell division drive Anaplasma phagocytophilum morphotype development and the infection cycle","volume":"16","author":"TJ Chiarelli","year":"2025","journal-title":"mBio"},{"issue":"3","key":"ppat.1014350.ref022","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1128\/JB.01218-08","article-title":"The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection","volume":"191","author":"T-H Lai","year":"2009","journal-title":"J Bacteriol"},{"issue":"6","key":"ppat.1014350.ref023","article-title":"The obligate intracellular bacterial pathogen anaplasma phagocytophilum exploits host cell multivesicular body biogenesis for proliferation and dissemination","volume":"13","author":"CB Read","year":"2022","journal-title":"mBio"},{"key":"ppat.1014350.ref024","doi-asserted-by":"crossref","DOI":"10.1017\/CBO9780511608421","volume-title":"Biochemistry and physiology of the neutrophil","author":"SW Edwards","year":"1994"},{"issue":"3","key":"ppat.1014350.ref025","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/S0014-5793(00)02324-3","article-title":"Molecular control of neutrophil apoptosis","volume":"487","author":"C Akgul","year":"2001","journal-title":"FEBS Lett"},{"issue":"1","key":"ppat.1014350.ref026","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1111\/j.1462-5822.2004.00427.x","article-title":"Anaplasma phagocytophilum inhibits human neutrophil apoptosis via upregulation of bfl-1, maintenance of mitochondrial membrane potential and prevention of caspase 3 activation","volume":"7","author":"Y Ge","year":"2005","journal-title":"Cell Microbiol"},{"issue":"3","key":"ppat.1014350.ref027","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1128\/IAI.68.3.1125-1133.2000","article-title":"Intracellular infection by the human granulocytic ehrlichiosis agent inhibits human neutrophil apoptosis","volume":"68","author":"K Yoshiie","year":"2000","journal-title":"Infect Immun"},{"issue":"4","key":"ppat.1014350.ref028","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1128\/MMBR.00023-09","article-title":"Biological diversity of prokaryotic type IV secretion systems","volume":"73","author":"CE Alvarez-Martinez","year":"2009","journal-title":"Microbiol Mol Biol Rev"},{"issue":"6","key":"ppat.1014350.ref029","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1038\/nrmicro3456","article-title":"Secretion systems in Gram-negative bacteria: structural and mechanistic insights","volume":"13","author":"TRD Costa","year":"2015","journal-title":"Nat Rev Microbiol"},{"issue":"3","key":"ppat.1014350.ref030","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1038\/s41579-023-00974-3","article-title":"Structural and functional diversity of type IV secretion systems","volume":"22","author":"TRD Costa","year":"2024","journal-title":"Nat Rev Microbiol"},{"key":"ppat.1014350.ref031","first-page":"24","article-title":"Global proteomic analysis of two tick-borne emerging zoonotic agents: anaplasma phagocytophilum and ehrlichia chaffeensis","volume":"2","author":"M Lin","year":"2011","journal-title":"Front Microbiol"},{"key":"ppat.1014350.ref032","first-page":"297","article-title":"Role and function of the Type IV secretion system in Anaplasma and Ehrlichia Species","volume":"413","author":"Y Rikihisa","year":"2017","journal-title":"Curr Top Microbiol Immunol"},{"issue":"11","key":"ppat.1014350.ref033","doi-asserted-by":"crossref","first-page":"2644","DOI":"10.1111\/j.1462-5822.2007.00985.x","article-title":"Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection","volume":"9","author":"M Lin","year":"2007","journal-title":"Cell Microbiol"},{"issue":"2","key":"ppat.1014350.ref034","article-title":"Anaplasma phagocytophilum Ats-1 is imported into host cell mitochondria and interferes with apoptosis induction","volume":"6","author":"H Niu","year":"2010","journal-title":"PLoS Pathog"},{"issue":"51","key":"ppat.1014350.ref035","doi-asserted-by":"crossref","first-page":"20800","DOI":"10.1073\/pnas.1218674109","article-title":"Autophagosomes induced by a bacterial Beclin 1 binding protein facilitate obligatory intracellular infection","volume":"109","author":"H Niu","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"33","key":"ppat.1014350.ref036","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2405209121","article-title":"Anaplasma phagocytophilum effector EgeA facilitates infection by hijacking TANGO1 and SCFD1 from ER-Golgi exit sites to pathogen-occupied inclusions","volume":"121","author":"L Wang","year":"2024","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"ppat.1014350.ref037","article-title":"An Anaplasma phagocytophilum T4SS effector, AteA, is essential for tick infection","volume":"14","author":"JM Park","year":"2023","journal-title":"mBio"},{"issue":"2","key":"ppat.1014350.ref038","doi-asserted-by":"crossref","first-page":"302","DOI":"10.3390\/jpm13020302","article-title":"Enhancement of cell adhesion by Anaplasma phagocytophilum Nucleolin-Interacting Protein AFAP","volume":"13","author":"H Tang","year":"2023","journal-title":"J Pers Med"},{"key":"ppat.1014350.ref039","doi-asserted-by":"crossref","first-page":"1533640","DOI":"10.3389\/fmicb.2024.1533640","article-title":"Anaplasma phagocytophilum AFAP targets the host nucleolus and inhibits induced apoptosis","volume":"15","author":"D Zhang","year":"2025","journal-title":"Front Microbiol"},{"key":"ppat.1014350.ref040","first-page":"55","article-title":"Bioinformatic and mass spectrometry identification of Anaplasma phagocytophilum proteins translocated into host cell nuclei","volume":"6","author":"SHG Sinclair","year":"2015","journal-title":"Front Microbiol"},{"issue":"5","key":"ppat.1014350.ref041","doi-asserted-by":"crossref","first-page":"1284","DOI":"10.1111\/j.1462-5822.2006.00871.x","article-title":"Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection","volume":"9","author":"JW IJdo","year":"2007","journal-title":"Cell Microbiol"},{"issue":"9","key":"ppat.1014350.ref042","doi-asserted-by":"crossref","first-page":"5277","DOI":"10.1128\/IAI.68.9.5277-5283.2000","article-title":"ankA: an Ehrlichia phagocytophila group gene encoding a cytoplasmic protein antigen with ankyrin repeats","volume":"68","author":"P Caturegli","year":"2000","journal-title":"Infect Immun"},{"issue":"8","key":"ppat.1014350.ref043","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1111\/j.1462-5822.2004.00400.x","article-title":"Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins","volume":"6","author":"J Park","year":"2004","journal-title":"Cell Microbiol"},{"issue":"6","key":"ppat.1014350.ref044","doi-asserted-by":"crossref","first-page":"2385","DOI":"10.1128\/IAI.00023-09","article-title":"Silencing of host cell CYBB gene expression by the nuclear effector AnkA of the intracellular pathogen Anaplasma phagocytophilum","volume":"77","author":"JC Garcia-Garcia","year":"2009","journal-title":"Infect Immun"},{"key":"ppat.1014350.ref045","doi-asserted-by":"crossref","first-page":"97","DOI":"10.3389\/fcimb.2016.00097","article-title":"Genome-wide Anaplasma phagocytophilum AnkA-DNA interactions are enriched in intergenic regions and gene promoters and correlate with infection-induced differential gene expression","volume":"6","author":"JS Dumler","year":"2016","journal-title":"Front Cell Infect Microbiol"},{"key":"ppat.1014350.ref046","doi-asserted-by":"crossref","first-page":"828605","DOI":"10.3389\/fcimb.2022.828605","article-title":"Anaplasma phagocytophilum Ankyrin A Protein (AnkA) enters the nucleus using an importin-beta-, RanGTP-dependent mechanism","volume":"12","author":"Y Kim","year":"2022","journal-title":"Frontiers in Cellular and Infection Microbiology"},{"key":"ppat.1014350.ref047","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1242\/jcs.00622","article-title":"Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases","volume":"116","author":"PJ Woodring","year":"2003","journal-title":"J Cell Sci"},{"issue":"1","key":"ppat.1014350.ref048","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/nrm1280","article-title":"Regulation of the c-Abl and Bcr-Abl tyrosine kinases","volume":"5","author":"O Hantschel","year":"2004","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"139","key":"ppat.1014350.ref049","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.3139re6","article-title":"ABL tyrosine kinases: evolution of function, regulation, and specificity","volume":"3","author":"J Colicelli","year":"2010","journal-title":"Sci Signal"},{"issue":"3","key":"ppat.1014350.ref050","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/j.devcel.2009.08.012","article-title":"Actin dynamics at the leading edge: from simple machinery to complex networks","volume":"17","author":"RH Insall","year":"2009","journal-title":"Dev Cell"},{"issue":"5","key":"ppat.1014350.ref051","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1007\/BF01774064","article-title":"Fluorescent phallotoxins as probes for filamentous actin","volume":"9","author":"H Faulstich","year":"1988","journal-title":"J Muscle Res Cell Motil"},{"issue":"6","key":"ppat.1014350.ref052","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.tcb.2012.03.003","article-title":"Actin coats and rings promote regulated exocytosis","volume":"22","author":"TD Nightingale","year":"2012","journal-title":"Trends Cell Biol"},{"issue":"4","key":"ppat.1014350.ref053","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1083\/jcb.128.4.589","article-title":"Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells","volume":"128","author":"S Muallem","year":"1995","journal-title":"J Cell Biol"},{"issue":"5830","key":"ppat.1014350.ref054","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/293302a0","article-title":"Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change","volume":"293","author":"JF Casella","year":"1981","journal-title":"Nature"},{"issue":"3","key":"ppat.1014350.ref055","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/cm.970130302","article-title":"Latrunculins--novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D","volume":"13","author":"I Spector","year":"1989","journal-title":"Cell Motil Cytoskeleton"},{"key":"ppat.1014350.ref056","doi-asserted-by":"crossref","first-page":"5559","DOI":"10.2741\/3099","article-title":"Control of granule exocytosis in neutrophils","volume":"13","author":"P Lacy","year":"2008","journal-title":"Frontiers in Bioscience: A Journal and Virtual Library"},{"key":"ppat.1014350.ref057","doi-asserted-by":"crossref","first-page":"448","DOI":"10.3389\/fimmu.2014.00448","article-title":"Granule protein processing and regulated secretion in neutrophils","volume":"5","author":"A Sheshachalam","year":"2014","journal-title":"Front Immunol"},{"issue":"3","key":"ppat.1014350.ref058","first-page":"905","article-title":"The effects of methyl (5-(2-thienylcarbonyl)-1H-benzimidazol-2-yl) carbamate, (R 17934; NSC 238159), a new synthetic antitumoral drug interfering with microtubules, on mammalian cells cultured in vitro","volume":"36","author":"MJ De Brabander","year":"1976","journal-title":"Cancer Res"},{"issue":"7","key":"ppat.1014350.ref059","doi-asserted-by":"crossref","first-page":"3793","DOI":"10.1128\/IAI.70.7.3793-3803.2002","article-title":"Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells","volume":"70","author":"RA Carabeo","year":"2002","journal-title":"Infect Immun"},{"issue":"20","key":"ppat.1014350.ref060","article-title":"Membrane Ruffles: Composition, Function, Formation and Visualization","volume":"25","author":"G Yan","year":"2024","journal-title":"International Journal of Molecular Sciences"},{"issue":"6","key":"ppat.1014350.ref061","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1128\/JCM.36.6.1666-1673.1998","article-title":"Cloning and expression of the 44-kilodalton major outer membrane protein gene of the human granulocytic ehrlichiosis agent and application of the recombinant protein to serodiagnosis","volume":"36","author":"N Zhi","year":"1998","journal-title":"J Clin Microbiol"},{"issue":"11","key":"ppat.1014350.ref062","doi-asserted-by":"crossref","first-page":"3278","DOI":"10.1128\/JCM.36.11.3278-3284.1998","article-title":"Characterization of monoclonal antibodies to the 44-kilodalton major outer membrane protein of the human granulocytic ehrlichiosis agent","volume":"36","author":"HY Kim","year":"1998","journal-title":"J Clin Microbiol"},{"issue":"14","key":"ppat.1014350.ref063","doi-asserted-by":"crossref","first-page":"1038","DOI":"10.1056\/NEJM200104053441402","article-title":"Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome","volume":"344","author":"BJ Druker","year":"2001","journal-title":"N Engl J Med"},{"issue":"7","key":"ppat.1014350.ref064","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/nrd839","article-title":"Glivec (STI571, imatinib), a rationally developed, targeted anticancer drug","volume":"1","author":"R Capdeville","year":"2002","journal-title":"Nat Rev Drug Discov"},{"key":"ppat.1014350.ref065","article-title":"Pharmacology of imatinib (STI571)","author":"E Buchdunger","year":"2002","journal-title":"Eur J Cancer"},{"key":"ppat.1014350.ref066","doi-asserted-by":"crossref","first-page":"2614","DOI":"10.1007\/s00018-004-4225-6","article-title":"Gelsolin superfamily proteins: key regulators of cellular functions","volume":"61","author":"P Silacci","year":"2004","journal-title":"Cell Mol Life Sci"},{"issue":"17","key":"ppat.1014350.ref067","doi-asserted-by":"crossref","first-page":"2688","DOI":"10.1007\/s00018-008-8080-8","article-title":"Alpha-actinin structure and regulation","volume":"65","author":"B Sj\u00f6blom","year":"2008","journal-title":"Cell Mol Life Sci"},{"issue":"6","key":"ppat.1014350.ref068","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1083\/jcb.140.6.1383","article-title":"Actinin-4, a novel actin-bundling protein associated with cell motility and cancer invasion","volume":"140","author":"K Honda","year":"1998","journal-title":"J Cell Biol"},{"issue":"2","key":"ppat.1014350.ref069","doi-asserted-by":"crossref","first-page":"362","DOI":"10.18632\/oncotarget.901","article-title":"Actin-binding protein alpha-actinin 4 (ACTN4) is a transcriptional co-activator of RelA\/p65 sub-unit of NF-kB","volume":"4","author":"V Aksenova","year":"2013","journal-title":"Oncotarget"},{"issue":"47","key":"ppat.1014350.ref070","doi-asserted-by":"crossref","first-page":"33179","DOI":"10.1074\/jbc.274.47.33179","article-title":"Gelsolin, a multifunctional actin regulatory protein","volume":"274","author":"HQ Sun","year":"1999","journal-title":"J Biol Chem"},{"issue":"11","key":"ppat.1014350.ref071","doi-asserted-by":"crossref","first-page":"4045","DOI":"10.1091\/mbc.e02-05-0294","article-title":"Motility determinants in WASP family proteins","volume":"13","author":"D Yarar","year":"2002","journal-title":"Mol Biol Cell"},{"issue":"2","key":"ppat.1014350.ref072","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1046\/j.1365-2958.2003.t01-1-03456.x","article-title":"Salmonella effectors translocated across the vacuolar membrane interact with the actin cytoskeleton","volume":"48","author":"EA Miao","year":"2003","journal-title":"Mol Microbiol"},{"issue":"8016","key":"ppat.1014350.ref073","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"J Abramson","year":"2024","journal-title":"Nature"},{"issue":"11","key":"ppat.1014350.ref074","doi-asserted-by":"crossref","first-page":"2145","DOI":"10.1080\/15548627.2016.1217369","article-title":"Ehrlichia secretes Etf-1 to induce autophagy and capture nutrients for its growth through RAB5 and class III phosphatidylinositol 3-kinase","volume":"12","author":"M Lin","year":"2016","journal-title":"Autophagy"},{"issue":"1","key":"ppat.1014350.ref075","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1074\/jbc.M605024200","article-title":"Alpha-actinin-4 is required for normal podocyte adhesion","volume":"282","author":"SV Dandapani","year":"2007","journal-title":"J Biol Chem"},{"issue":"2","key":"ppat.1014350.ref076","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1002\/cm.20007","article-title":"Alpha-actinin revisited: a fresh look at an old player","volume":"58","author":"CA Otey","year":"2004","journal-title":"Cell Motil Cytoskeleton"},{"key":"ppat.1014350.ref077","doi-asserted-by":"crossref","first-page":"97","DOI":"10.3389\/fmicb.2011.00097","article-title":"Advances in genetic manipulation of obligate intracellular bacterial pathogens","volume":"2","author":"PA Beare","year":"2011","journal-title":"Front Microbiol"},{"issue":"9","key":"ppat.1014350.ref078","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1038\/nrmicro.2017.59","article-title":"Engineering of obligate intracellular bacteria: progress, challenges and paradigms","volume":"15","author":"EE McClure","year":"2017","journal-title":"Nat Rev Microbiol"},{"key":"ppat.1014350.ref079","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/1472-6750-6-42","article-title":"Transformation of Anaplasma phagocytophilum","volume":"6","author":"RF Felsheim","year":"2006","journal-title":"BMC Biotechnol"},{"issue":"1","key":"ppat.1014350.ref080","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/ncb2409","article-title":"Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways","volume":"14","author":"M Anitei","year":"2011","journal-title":"Nat Cell Biol"},{"issue":"1","key":"ppat.1014350.ref081","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/S0955-0674(97)80156-1","article-title":"Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton","volume":"9","author":"N Tapon","year":"1997","journal-title":"Curr Opin Cell Biol"},{"issue":"6","key":"ppat.1014350.ref082","article-title":"EtpE binding to DNase X induces ehrlichial entry via CD147 and hnRNP-K recruitment, followed by mobilization of N-WASP and actin","volume":"6","author":"D Mohan","year":"2015","journal-title":"mBio"},{"issue":"5350","key":"ppat.1014350.ref083","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1126\/science.279.5350.527","article-title":"Unconventional myosins in cell movement, membrane traffic, and signal transduction","volume":"279","author":"V Mermall","year":"1998","journal-title":"Science"},{"issue":"2","key":"ppat.1014350.ref084","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/j.bbrc.2018.03.103","article-title":"Mammalian nonmuscle myosin II comes in three flavors","volume":"506","author":"MS Shutova","year":"2018","journal-title":"Biochem Biophys Res Commun"},{"issue":"8","key":"ppat.1014350.ref085","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1038\/nsmb796","article-title":"Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation","volume":"11","author":"JR Peterson","year":"2004","journal-title":"Nat Struct Mol Biol"},{"key":"ppat.1014350.ref086","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/0076-6879(95)56023-8","article-title":"In vitro ADP-ribosylation of Rho by bacterial ADP-ribosyltransferases","volume":"256","author":"K Aktories","year":"1995","journal-title":"Methods Enzymol"},{"issue":"16","key":"ppat.1014350.ref087","doi-asserted-by":"crossref","first-page":"7796","DOI":"10.1016\/S0021-9258(18)47638-7","article-title":"Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase","volume":"262","author":"M Saitoh","year":"1987","journal-title":"J Biol Chem"},{"issue":"5613","key":"ppat.1014350.ref088","doi-asserted-by":"crossref","first-page":"1743","DOI":"10.1126\/science.1081412","article-title":"Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor","volume":"299","author":"AF Straight","year":"2003","journal-title":"Science"},{"key":"ppat.1014350.ref089","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1007\/s10974-004-6060-7","article-title":"Specificity of blebbistatin, an inhibitor of myosin II","volume":"25","author":"J Limouze","year":"2004","journal-title":"J Muscle Res Cell Motil"},{"issue":"9","key":"ppat.1014350.ref090","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1002\/j.1552-4604.1990.tb01873.x","article-title":"New natural products in cancer chemotherapy","volume":"30","author":"WJ Slichenmyer","year":"1990","journal-title":"J Clin Pharmacol"},{"issue":"8","key":"ppat.1014350.ref091","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1182\/blood.V85.8.2212.bloodjournal8582212","article-title":"Role of gelsolin in the formation and organization of triton-soluble F-actin during myeloid differentiation of HL-60 cells","volume":"85","author":"RG Watts","year":"1995","journal-title":"Blood"},{"issue":"5","key":"ppat.1014350.ref092","article-title":"The actin cytoskeleton regulates exocytosis of all neutrophil granule subsets","volume":"292","author":"NR Jog","year":"2007","journal-title":"Am J Physiol Cell Physiol"},{"issue":"3","key":"ppat.1014350.ref093","doi-asserted-by":"crossref","DOI":"10.1128\/microbiolspec.VMBF-0024-2015","article-title":"Mechanism and Function of Type IV Secretion During Infection of the Human Host","volume":"4","author":"C Gonzalez-Rivera","year":"2016","journal-title":"Microbiol Spectr"},{"issue":"9","key":"ppat.1014350.ref094","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1111\/j.1462-5822.2010.01500.x","article-title":"Type IV secretion in the obligatory intracellular bacterium Anaplasma phagocytophilum","volume":"12","author":"Y Rikihisa","year":"2010","journal-title":"Cell Microbiol"},{"issue":"1","key":"ppat.1014350.ref095","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1006\/excr.1999.4521","article-title":"A role for gelsolin in stress fiber-dependent cell contraction","volume":"250","author":"PD Arora","year":"1999","journal-title":"Exp Cell Res"},{"issue":"5","key":"ppat.1014350.ref096","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1002\/pmic.200800503","article-title":"Actin, gelsolin and filamin-A are dynamic actors in the cytoskeleton remodelling contributing to the blood brain barrier phenotype","volume":"9","author":"G Pottiez","year":"2009","journal-title":"Proteomics"},{"key":"ppat.1014350.ref097","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1186\/1742-4690-10-39","article-title":"Gelsolin activity controls efficient early HIV-1 infection","volume":"10","author":"L Garc\u00eda-Exp\u00f3sito","year":"2013","journal-title":"Retrovirology"},{"issue":"12","key":"ppat.1014350.ref098","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1007\/s00018-012-1156-5","article-title":"Multiple roles for the actin cytoskeleton during regulated exocytosis","volume":"70","author":"N Porat-Shliom","year":"2013","journal-title":"Cell Mol Life Sci"},{"issue":"4","key":"ppat.1014350.ref099","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/S0955-0674(02)00349-6","article-title":"Regulating the actin cytoskeleton during vesicular transport","volume":"14","author":"M Stamnes","year":"2002","journal-title":"Curr Opin Cell Biol"},{"key":"ppat.1014350.ref100","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1146\/annurev.cellbio.14.1.137","article-title":"Intracellular pathogens and the actin cytoskeleton","volume":"14","author":"S Dramsi","year":"1998","journal-title":"Annu Rev Cell Dev Biol"},{"issue":"2","key":"ppat.1014350.ref101","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1111\/cmi.12399","article-title":"Subversion of the cytoskeleton by intracellular bacteria: lessons from Listeria, Salmonella and Vibrio","volume":"17","author":"M de Souza Santos","year":"2015","journal-title":"Cell Microbiol"},{"key":"ppat.1014350.ref102","doi-asserted-by":"crossref","first-page":"107","DOI":"10.3389\/fcimb.2016.00107","article-title":"Hijacking host cell highways: manipulation of the host actin cytoskeleton by obligate intracellular bacterial pathogens","volume":"6","author":"PM Colonne","year":"2016","journal-title":"Frontiers in Cellular and Infection Microbiology"},{"key":"ppat.1014350.ref103","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.mib.2016.11.007","article-title":"Actin-based motility and cell-to-cell spread of bacterial pathogens","volume":"35","author":"RL Lamason","year":"2017","journal-title":"Curr Opin Microbiol"},{"issue":"2","key":"ppat.1014350.ref104","doi-asserted-by":"crossref","first-page":"38","DOI":"10.4161\/bioa.20422","article-title":"A pathogen\u2019s journey in the host cell: Bridges between actin and traffic","volume":"2","author":"IS Franco","year":"2012","journal-title":"Bioarchitecture"},{"issue":"1","key":"ppat.1014350.ref105","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1083\/jcb.201103148","article-title":"Pathogens and polymers: microbe-host interactions illuminate the cytoskeleton","volume":"195","author":"CM Haglund","year":"2011","journal-title":"J Cell Biol"},{"issue":"2","key":"ppat.1014350.ref106","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/nrmicro1320","article-title":"Actin-dependent movement of bacterial pathogens","volume":"4","author":"JM Stevens","year":"2006","journal-title":"Nat Rev Microbiol"},{"issue":"11","key":"ppat.1014350.ref107","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1038\/ncb2109","article-title":"Rickettsia Sca2 is a bacterial formin-like mediator of actin-based motility","volume":"12","author":"CM Haglund","year":"2010","journal-title":"Nat Cell Biol"},{"issue":"10","key":"ppat.1014350.ref108","doi-asserted-by":"crossref","first-page":"3867","DOI":"10.1073\/pnas.86.10.3867","article-title":"Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin","volume":"86","author":"ML Bernardini","year":"1989","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"14","key":"ppat.1014350.ref109","doi-asserted-by":"crossref","first-page":"6572","DOI":"10.1073\/pnas.92.14.6572","article-title":"Shigella flexneri surface protein IcsA is sufficient to direct actin-based motility","volume":"92","author":"MB Goldberg","year":"1995","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"ppat.1014350.ref110","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1083\/jcb.135.3.647","article-title":"The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin","volume":"135","author":"GA Smith","year":"1996","journal-title":"J Cell Biol"},{"issue":"8","key":"ppat.1014350.ref111","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1128\/JB.01455-10","article-title":"Identification of motifs of Burkholderia pseudomallei BimA required for intracellular motility, actin binding, and actin polymerization","volume":"193","author":"C Sitthidet","year":"2011","journal-title":"J Bacteriol"},{"issue":"19","key":"ppat.1014350.ref112","doi-asserted-by":"crossref","first-page":"5249","DOI":"10.1128\/JB.00608-10","article-title":"Actin-based motility of Burkholderia thailandensis requires a central acidic domain of BimA that recruits and activates the cellular Arp2\/3 complex","volume":"192","author":"C Sitthidet","year":"2010","journal-title":"J Bacteriol"},{"issue":"6973","key":"ppat.1014350.ref113","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/nature02318","article-title":"The RickA protein of Rickettsia conorii activates the Arp2\/3 complex","volume":"427","author":"E Gouin","year":"2004","journal-title":"Nature"},{"issue":"18","key":"ppat.1014350.ref114","doi-asserted-by":"crossref","first-page":"4926","DOI":"10.1093\/emboj\/18.18.4926","article-title":"Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella","volume":"18","author":"RD Hayward","year":"1999","journal-title":"EMBO J"},{"issue":"18","key":"ppat.1014350.ref115","doi-asserted-by":"crossref","first-page":"13357","DOI":"10.1074\/jbc.M109.094045","article-title":"The C terminus of SipC binds and bundles F-actin to promote Salmonella invasion","volume":"285","author":"SK Myeni","year":"2010","journal-title":"J Biol Chem"},{"issue":"27","key":"ppat.1014350.ref116","doi-asserted-by":"crossref","first-page":"10166","DOI":"10.1073\/pnas.0402829101","article-title":"A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin","volume":"101","author":"DR Clifton","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"42","key":"ppat.1014350.ref117","doi-asserted-by":"crossref","first-page":"15599","DOI":"10.1073\/pnas.0603044103","article-title":"Chlamydial TARP is a bacterial nucleator of actin","volume":"103","author":"TJ Jewett","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"ppat.1014350.ref118","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002546","article-title":"The Legionella pneumophila effector VipA is an actin nucleator that alters host cell organelle trafficking","volume":"8","author":"IS Franco","year":"2012","journal-title":"PLoS Pathog"},{"issue":"27","key":"ppat.1014350.ref119","doi-asserted-by":"crossref","first-page":"11430","DOI":"10.1073\/pnas.0703218104","article-title":"Mechanisms of host cell exit by the intracellular bacterium Chlamydia","volume":"104","author":"K Hybiske","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"10","key":"ppat.1014350.ref120","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0046949","article-title":"Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors","volume":"7","author":"E Chin","year":"2012","journal-title":"PLoS One"},{"issue":"2","key":"ppat.1014350.ref121","doi-asserted-by":"crossref","first-page":"241","DOI":"10.2217\/fmb.11.150","article-title":"Bacterial Type IV secretion systems: versatile virulence machines","volume":"7","author":"DE Voth","year":"2012","journal-title":"Future Microbiol"},{"issue":"6","key":"ppat.1014350.ref122","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1016\/j.celrep.2013.04.027","article-title":"Chlamydia trachomatis inclusion membrane protein CT228 recruits elements of the myosin phosphatase pathway to regulate release mechanisms","volume":"3","author":"EI Lutter","year":"2013","journal-title":"Cell Rep"},{"issue":"5","key":"ppat.1014350.ref123","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01802-14","article-title":"Septins arrange F-actin-containing fibers on the Chlamydia trachomatis inclusion and are required for normal release of the inclusion by extrusion","volume":"5","author":"L Volceanov","year":"2014","journal-title":"mBio"},{"issue":"12","key":"ppat.1014350.ref124","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0015775","article-title":"Exit mechanisms of the intracellular bacterium Ehrlichia","volume":"5","author":"S Thomas","year":"2010","journal-title":"PLoS One"},{"key":"ppat.1014350.ref125","doi-asserted-by":"crossref","DOI":"10.7717\/peerj.264","article-title":"Ankyrin domains across the Tree of Life","volume":"2","author":"KK Jernigan","year":"2014","journal-title":"PeerJ"},{"issue":"7","key":"ppat.1014350.ref126","doi-asserted-by":"crossref","first-page":"2847","DOI":"10.1128\/IAI.05097-11","article-title":"Expression of Anaplasma marginale ankyrin repeat-containing proteins during infection of the mammalian host and tick vector","volume":"79","author":"SS Ramabu","year":"2011","journal-title":"Infect Immun"},{"issue":"1","key":"ppat.1014350.ref127","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.mib.2009.12.008","article-title":"Anaplasma phagocytophilum and Ehrlichia chaffeensis type IV secretion and Ank proteins","volume":"13","author":"Y Rikihisa","year":"2010","journal-title":"Curr Opin Microbiol"},{"issue":"3","key":"ppat.1014350.ref128","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.tim.2009.11.004","article-title":"Functional diversity of ankyrin repeats in microbial proteins","volume":"18","author":"S Al-Khodor","year":"2010","journal-title":"Trends Microbiol"},{"issue":"44","key":"ppat.1014350.ref129","doi-asserted-by":"crossref","first-page":"18997","DOI":"10.1073\/pnas.1004380107","article-title":"Inhibition of pathogen-induced apoptosis by a Coxiella burnetii type IV effector protein","volume":"107","author":"A L\u00fchrmann","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"13","key":"ppat.1014350.ref130","doi-asserted-by":"crossref","first-page":"4232","DOI":"10.1128\/JB.01656-08","article-title":"The Coxiella burnetii ankyrin repeat domain-containing protein family is heterogeneous, with C-terminal truncations that influence Dot\/Icm-mediated secretion","volume":"191","author":"DE Voth","year":"2009","journal-title":"J Bacteriol"},{"issue":"5883","key":"ppat.1014350.ref131","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1126\/science.1158160","article-title":"Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors","volume":"320","author":"X Pan","year":"2008","journal-title":"Science"},{"issue":"6","key":"ppat.1014350.ref132","doi-asserted-by":"crossref","first-page":"1460","DOI":"10.1111\/j.1462-2920.2007.01560.x","article-title":"Role for the Ankyrin eukaryotic-like genes of Legionella pneumophila in parasitism of protozoan hosts and human macrophages","volume":"10","author":"F Habyarimana","year":"2008","journal-title":"Environ Microbiol"},{"key":"ppat.1014350.ref133","first-page":"186","article-title":"Orientia tsutsugamushi ankyrin repeat-containing protein family members are type 1 secretion system substrates that traffic to the host cell endoplasmic reticulum","volume":"4","author":"L VieBrock","year":"2014","journal-title":"Frontiers in Cellular and Infection Microbiology"},{"issue":"7","key":"ppat.1014350.ref134","doi-asserted-by":"crossref","DOI":"10.1111\/cmi.12727","article-title":"Orientia tsutsugamushi Ank9 is a multifunctional effector that utilizes a novel GRIP-like Golgi localization domain for Golgi-to-endoplasmic reticulum trafficking and interacts with host COPB2","volume":"19","author":"AR Beyer","year":"2017","journal-title":"Cell Microbiol"},{"issue":"10","key":"ppat.1014350.ref135","doi-asserted-by":"crossref","DOI":"10.1128\/iai.00059-24","article-title":"crANKing up the infection: ankyrin domains in Rickettsiales and their role in host manipulation","volume":"92","author":"WC Hamilton","year":"2024","journal-title":"Infect Immun"},{"issue":"8","key":"ppat.1014350.ref136","doi-asserted-by":"crossref","first-page":"1727","DOI":"10.1084\/jem.20100276","article-title":"Anaplasma phagocytophilum induces actin phosphorylation to selectively regulate gene transcription in Ixodes scapularis ticks","volume":"207","author":"H Sultana","year":"2010","journal-title":"J Exp Med"},{"issue":"1","key":"ppat.1014350.ref137","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1093\/infdis\/175.1.210","article-title":"Ultrastructural and antigenic characterization of a granulocytic ehrlichiosis agent directly isolated and stably cultivated from a patient in New York state","volume":"175","author":"Y Rikihisa","year":"1997","journal-title":"J Infect Dis"},{"issue":"7","key":"ppat.1014350.ref138","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1111\/j.1462-5822.2012.01775.x","article-title":"Ehrlichia type IV secretion effector ECH0825 is translocated to mitochondria and curbs ROS and apoptosis by upregulating host MnSOD","volume":"14","author":"H Liu","year":"2012","journal-title":"Cell Microbiol"},{"issue":"2","key":"ppat.1014350.ref139","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1128\/IAI.70.2.889-898.2002","article-title":"Rapid activation of protein tyrosine kinase and phospholipase C-gamma2 and increase in cytosolic free calcium are required by Ehrlichia chaffeensis for internalization and growth in THP-1 cells","volume":"70","author":"M Lin","year":"2002","journal-title":"Infect Immun"},{"issue":"8","key":"ppat.1014350.ref140","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1111\/j.1462-5822.2006.00704.x","article-title":"Intra-leukocyte expression of two-component systems in Ehrlichia chaffeensis and Anaplasma phagocytophilum and effects of the histidine kinase inhibitor closantel","volume":"8","author":"Z Cheng","year":"2006","journal-title":"Cell Microbiol"},{"issue":"9","key":"ppat.1014350.ref141","doi-asserted-by":"crossref","first-page":"5014","DOI":"10.1128\/IAI.00735-06","article-title":"Biochemical activities of three pairs of Ehrlichia chaffeensis two-component regulatory system proteins involved in inhibition of lysosomal fusion","volume":"74","author":"Y Kumagai","year":"2006","journal-title":"Infect Immun"},{"issue":"7","key":"ppat.1014350.ref142","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/ncb1433","article-title":"Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners","volume":"8","author":"X Wu","year":"2006","journal-title":"Nat Cell Biol"},{"issue":"7","key":"ppat.1014350.ref143","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","author":"J Schindelin","year":"2012","journal-title":"Nat Methods"},{"issue":"9","key":"ppat.1014350.ref144","doi-asserted-by":"crossref","first-page":"5324","DOI":"10.1128\/IAI.71.9.5324-5331.2003","article-title":"Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival","volume":"71","author":"M Lin","year":"2003","journal-title":"Infect Immun"},{"issue":"3","key":"ppat.1014350.ref145","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000329","article-title":"Cholesterol-dependent anaplasma phagocytophilum exploits the low-density lipoprotein uptake pathway","volume":"5","author":"Q Xiong","year":"2009","journal-title":"PLoS Pathog"}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1014350","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T17:29:08Z","timestamp":1782322148000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1014350"}},"subtitle":[],"editor":[{"given":"Stacey D.","family":"Gilk","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2026,6,24]]},"references-count":145,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2026,6,24]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1014350","relation":{},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,24]]}}}