{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T02:24:28Z","timestamp":1780453468602,"version":"3.54.1"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009969","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,10,25]],"date-time":"2021-10-25T00:00:00Z","timestamp":1635120000000}}],"reference-count":67,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2021,10,6]],"date-time":"2021-10-06T00:00:00Z","timestamp":1633478400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["351262938"],"award-info":[{"award-number":["351262938"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["391524768"],"award-info":[{"award-number":["391524768"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["462625623"],"award-info":[{"award-number":["462625623"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>The pathology associated with malaria infection is largely due to the ability of infected human RBCs to adhere to a number of receptors on endothelial cells within tissues and organs. This phenomenon is driven by the export of parasite-encoded proteins to the host cell, the exact function of many of which is still unknown. Here we inactivate the function of one of these exported proteins, PFA66, a member of the J-domain protein family. Although parasites lacking this protein were still able to grow in cell culture, we observed severe defects in normal host cell modification, including aberrant morphology of surface knobs, disrupted presentation of the cytoadherence molecule PfEMP1, and a total lack of cytoadherence, despite the presence of the knob associated protein KAHRP. Complementation assays demonstrate that an intact J-domain is required for recovery to a wild-type phenotype and suggest that PFA66 functions in concert with a HSP70 to carry out host cell modification. Strikingly, this HSP70 is likely to be of host origin. ATPase assays on recombinant protein verify a functional interaction between PFA66 and residual host cell HSP70. Taken together, our data reveal a role for PFA66 in host cell modification, strongly implicate human HSP70s as being essential in this process and uncover a new KAHRP-independent molecular factor required for correct knob biogenesis.<\/jats:p>","DOI":"10.1371\/journal.ppat.1009969","type":"journal-article","created":{"date-parts":[[2021,10,7]],"date-time":"2021-10-07T08:43:30Z","timestamp":1633596210000},"page":"e1009969","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":21,"title":["Co-chaperone involvement in knob biogenesis implicates host-derived chaperones in malaria virulence"],"prefix":"10.1371","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7982-9764","authenticated-orcid":true,"given":"Mathias","family":"Diehl","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0018-7349","authenticated-orcid":true,"given":"Lena","family":"Roling","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1559-5097","authenticated-orcid":true,"given":"Lukas","family":"Rohland","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sebastian","family":"Weber","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marek","family":"Cyrklaff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3334-3726","authenticated-orcid":true,"given":"Cecilia P.","family":"Sanchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6027-0796","authenticated-orcid":true,"given":"Carlo A.","family":"Beretta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caroline S.","family":"Simon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8762-4259","authenticated-orcid":true,"given":"Julien","family":"Guizetti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julia","family":"Hahn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norma","family":"Schulz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7859-3112","authenticated-orcid":true,"given":"Matthias P.","family":"Mayer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3494-7767","authenticated-orcid":true,"given":"Jude M.","family":"Przyborski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,10,6]]},"reference":[{"key":"ppat.1009969.ref001","unstructured":"WHO World Malaria Report 2020."},{"key":"ppat.1009969.ref002","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/415673a","article-title":"The pathogenic basis of malaria","volume":"415","author":"LH Miller","year":"2002","journal-title":"Nature"},{"key":"ppat.1009969.ref003","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/0140-6736(91)91638-B","article-title":"Intracranial pressure in African children with cerebral malaria","volume":"337","author":"CR Newton","year":"1991","journal-title":"Lancet"},{"key":"ppat.1009969.ref004","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/0092-8674(95)90054-3","article-title":"Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes","volume":"82","author":"DI Baruch","year":"1995","journal-title":"Cell"},{"key":"ppat.1009969.ref005","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/0092-8674(95)90056-X","article-title":"Switches in expression of Plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes","volume":"82","author":"JD Smith","year":"1995","journal-title":"Cell"},{"key":"ppat.1009969.ref006","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0092-8674(95)90055-1","article-title":"The large diverse gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum-infected erythrocytes","volume":"82","author":"XZ Su","year":"1995","journal-title":"Cell"},{"key":"ppat.1009969.ref007","doi-asserted-by":"crossref","first-page":"1934","DOI":"10.1126\/science.1102737","article-title":"A host-targeting signal in virulence proteins reveals a secretome in malarial infection","volume":"306","author":"NL Hiller","year":"2004","journal-title":"Science"},{"key":"ppat.1009969.ref008","doi-asserted-by":"crossref","first-page":"1930","DOI":"10.1126\/science.1102452","article-title":"Targeting malaria virulence and remodeling proteins to the host erythrocyte","volume":"306","author":"M Marti","year":"2004","journal-title":"Science"},{"key":"ppat.1009969.ref009","doi-asserted-by":"crossref","first-page":"R12","DOI":"10.1186\/gb-2006-7-2-r12","article-title":"Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites","volume":"7","author":"TJ Sargeant","year":"2006","journal-title":"Genome Biol"},{"key":"ppat.1009969.ref010","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1083\/jcb.200508051","article-title":"Signal-mediated export of proteins from the malaria parasite to the host erythrocyte","volume":"171","author":"M Marti","year":"2005","journal-title":"J Cell Biol"},{"key":"ppat.1009969.ref011","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1038\/nrmicro.2016.79","article-title":"Plasmodium species: master renovators of their host cells","volume":"14","author":"TF de Koning-Ward","year":"2016","journal-title":"Nat Rev Microbiol"},{"key":"ppat.1009969.ref012","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.cell.2008.04.051","article-title":"Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes","volume":"134","author":"AG Maier","year":"2008","journal-title":"Cell"},{"key":"ppat.1009969.ref013","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/nrmicro2110","article-title":"Malaria parasite proteins that remodel the host erythrocyte","volume":"7","author":"AG Maier","year":"2009","journal-title":"Nat Rev Microbiol"},{"key":"ppat.1009969.ref014","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1016\/j.biocel.2007.02.011","article-title":"The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host","volume":"39","author":"M Botha","year":"2007","journal-title":"Int J Biochem Cell Biol"},{"key":"ppat.1009969.ref015","doi-asserted-by":"crossref","first-page":"2560","DOI":"10.1007\/s00018-006-6192-6","article-title":"The diversity of the DnaJ\/Hsp40 family, the crucial partners for Hsp70 chaperones","volume":"63","author":"XB Qiu","year":"2006","journal-title":"Cell Mol Life Sci"},{"key":"ppat.1009969.ref016","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1111\/j.1462-5822.2010.01477.x","article-title":"Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum-infected erythrocyte","volume":"12","author":"S K\u00fclzer","year":"2010","journal-title":"Cell Microbiol"},{"key":"ppat.1009969.ref017","doi-asserted-by":"crossref","first-page":"e44605","DOI":"10.1371\/journal.pone.0044605","article-title":"An exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytes","volume":"7","author":"P Acharya","year":"2012","journal-title":"PLoS One"},{"key":"ppat.1009969.ref018","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1111\/j.1462-5822.2012.01840.x","article-title":"Plasmodium falciparum-encoded exported hsp70\/hsp40 chaperone\/co-chaperone complexes within the host erythrocyte","volume":"14","author":"S K\u00fclzer","year":"2012","journal-title":"Cell Microbiol"},{"key":"ppat.1009969.ref019","doi-asserted-by":"crossref","first-page":"42188","DOI":"10.1038\/srep42188","article-title":"Proteomic analysis of exported chaperone\/co-chaperone complexes of P. falciparum reveals an array of complex protein-protein interactions","volume":"7","author":"Q Zhang","year":"2017","journal-title":"Sci Rep"},{"key":"ppat.1009969.ref020","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/nmeth.4223","article-title":"A genetic system to study Plasmodium falciparum protein function","volume":"14","author":"J Birnbaum","year":"2017","journal-title":"Nat Methods"},{"key":"ppat.1009969.ref021","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1086\/314899","article-title":"Plasmodium falciparum isolates from infected pregnant women and children are associated with distinct adhesive and antigenic properties","volume":"180","author":"JG Beeson","year":"1999","journal-title":"J Infect Dis"},{"key":"ppat.1009969.ref022","doi-asserted-by":"crossref","first-page":"5198","DOI":"10.1073\/pnas.96.9.5198","article-title":"The adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated by P. falciparum erythrocyte membrane protein 1","volume":"96","author":"JC Reeder","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1009969.ref023","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1186\/1475-2875-12-373","article-title":"An integrated strategy for efficient vector construction and multi-gene expression in Plasmodium falciparum","volume":"12","author":"JC Wagner","year":"2013","journal-title":"Malar J"},{"key":"ppat.1009969.ref024","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.ijpara.2016.03.005","article-title":"J-dot targeting of an exported HSP40 in Plasmodium falciparum-infected erythrocytes","volume":"46","author":"W Petersen","year":"2016","journal-title":"Int J Parasitol"},{"key":"ppat.1009969.ref025","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.1038\/s41598-019-39217-y","article-title":"Cholesterol bound Plasmodium falciparum co-chaperone \u2018PFA0660w\u2019 complexes with major virulence factor \u2018PfEMP1\u2019 via chaperone \u2018PfHsp70-x\u2019","volume":"9","author":"A Behl","year":"2019","journal-title":"Sci Rep"},{"key":"ppat.1009969.ref026","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1042\/BJ20061725","article-title":"Selective permeabilization of the host cell membrane of Plasmodium falciparum-infected red blood cells with streptolysin O and equinatoxin II","volume":"403","author":"KE Jackson","year":"2007","journal-title":"Biochem J"},{"key":"ppat.1009969.ref027","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/978-1-4939-2309-0_5","article-title":"Fractionation of Plasmodium-infected human red blood cells to study protein trafficking","volume":"1270","author":"S K\u00fclzer","year":"2015","journal-title":"Methods Mol Biol"},{"key":"ppat.1009969.ref028","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1111\/j.1365-2958.2006.05112.x","article-title":"Evidence for the involvement of Plasmodium falciparum proteins in the formation of new permeability pathways in the erythrocyte membrane","volume":"60","author":"S Baumeister","year":"2006","journal-title":"Mol Microbiol"},{"key":"ppat.1009969.ref029","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/0166-6851(83)90008-7","article-title":"New permeability pathways induced in membranes of Plasmodium falciparum infected erythrocytes","volume":"8","author":"H Ginsburg","year":"1983","journal-title":"Mol Biochem Parasitol"},{"key":"ppat.1009969.ref030","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0092-8674(00)80207-X","article-title":"Targeted gene disruption shows that knobs enable malaria-infected red cells to cytoadhere under physiological shear stress","volume":"89","author":"BS Crabb","year":"1997","journal-title":"Cell"},{"key":"ppat.1009969.ref031","doi-asserted-by":"crossref","first-page":"7139","DOI":"10.1073\/pnas.84.20.7139","article-title":"Primary structure and subcellular localization of the knob-associated histidine-rich protein of Plasmodium falciparum","volume":"84","author":"LG Pologe","year":"1987","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1009969.ref032","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1182\/blood-2005-11-4624","article-title":"The role of KAHRP domains in knob formation and cytoadherence of P falciparum-infected human erythrocytes","volume":"108","author":"M Rug","year":"2006","journal-title":"Blood"},{"key":"ppat.1009969.ref033","doi-asserted-by":"crossref","first-page":"1226","DOI":"10.1038\/s41592-019-0582-9","article-title":"ilastik: interactive machine learning for (bio)image analysis","volume":"16","author":"S Berg","year":"2019","journal-title":"Nat Methods"},{"key":"ppat.1009969.ref034","doi-asserted-by":"crossref","first-page":"8206","DOI":"10.1073\/pnas.97.15.8206","article-title":"Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission","volume":"97","author":"TA Klar","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1009969.ref035","doi-asserted-by":"crossref","first-page":"5644","DOI":"10.1364\/OE.19.005644","article-title":"Far-field optical nanoscopy with reduced number of state transition cycles","volume":"19","author":"T Staudt","year":"2011","journal-title":"Opt Express"},{"key":"ppat.1009969.ref036","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1242\/jcs.114454","article-title":"Membrane curvature at a glance","volume":"128","author":"HT McMahon","year":"2015","journal-title":"J Cell Sci"},{"key":"ppat.1009969.ref037","doi-asserted-by":"crossref","first-page":"5452","DOI":"10.1073\/pnas.96.10.5452","article-title":"Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones","volume":"96","author":"T Laufen","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1009969.ref038","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1006\/jmbi.1999.2844","article-title":"Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy","volume":"289","author":"MP Mayer","year":"1999","journal-title":"J Mol Biol"},{"key":"ppat.1009969.ref039","doi-asserted-by":"crossref","first-page":"e0148517","DOI":"10.1371\/journal.pone.0148517","article-title":"The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x","volume":"11","author":"MO Daniyan","year":"2016","journal-title":"PLoS One"},{"key":"ppat.1009969.ref040","doi-asserted-by":"crossref","first-page":"14611","DOI":"10.1096\/fj.201901741R","article-title":"The Plasmodium falciparum Hsp70-x chaperone assists the heat stress response of the malaria parasite","volume":"33","author":"J Day","year":"2019","journal-title":"FASEB J"},{"key":"ppat.1009969.ref041","doi-asserted-by":"crossref","first-page":"11236","DOI":"10.1074\/jbc.271.19.11236","article-title":"A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein","volume":"271","author":"AW Karzai","year":"1996","journal-title":"J Biol Chem"},{"key":"ppat.1009969.ref042","doi-asserted-by":"crossref","first-page":"4937","DOI":"10.1021\/bi027333o","article-title":"The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70","volume":"42","author":"P Wittung-Stafshede","year":"2003","journal-title":"Biochemistry"},{"key":"ppat.1009969.ref043","doi-asserted-by":"crossref","first-page":"e104096","DOI":"10.15252\/embj.2019104096","article-title":"Feedback regulation of heat shock factor 1 (Hsf1) activity by Hsp70-mediated trimer unzipping and dissociation from DNA","volume":"39","author":"SW Kmiecik","year":"2020","journal-title":"EMBO J"},{"key":"ppat.1009969.ref044","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.03320-19","article-title":"Role of Plasmodium falciparum Protein GEXP07 in Maurer\u2019s Cleft Morphology, Knob Architecture, and P. falciparum EMP1 Trafficking","volume":"11","author":"E McHugh","year":"2020","journal-title":"mBio"},{"key":"ppat.1009969.ref045","doi-asserted-by":"crossref","first-page":"e1008363","DOI":"10.1371\/journal.ppat.1008363","article-title":"Complex nutrient channel phenotypes despite Mendelian inheritance in a Plasmodium falciparum genetic cross","volume":"16","author":"A Gupta","year":"2020","journal-title":"PLoS Pathog"},{"key":"ppat.1009969.ref046","doi-asserted-by":"crossref","first-page":"e1007761","DOI":"10.1371\/journal.ppat.1007761","article-title":"The knob protein KAHRP assembles into a ring-shaped structure that underpins virulence complex assembly","volume":"15","author":"O Looker","year":"2019","journal-title":"PLoS Pathog"},{"key":"ppat.1009969.ref047","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1182\/blood-2015-10-674002","article-title":"A spiral scaffold underlies cytoadherent knobs in Plasmodium falciparum-infected erythrocytes","volume":"127","author":"JM Watermeyer","year":"2016","journal-title":"Blood"},{"key":"ppat.1009969.ref048","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1529\/biophysj.104.040634","article-title":"Cholesterol depletion increases membrane stiffness of aortic endothelial cells","volume":"87","author":"FJ Byfield","year":"2004","journal-title":"Biophys J"},{"key":"ppat.1009969.ref049","doi-asserted-by":"crossref","first-page":"13964","DOI":"10.1073\/pnas.2336102100","article-title":"Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin","volume":"100","author":"J Kwik","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1009969.ref050","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1379\/1466-1268(2003)008<0309:MFROHF>2.0.CO;2","article-title":"Mechanisms for regulation of Hsp70 function by Hsp40","volume":"8","author":"CY Fan","year":"2003","journal-title":"Cell Stress Chaperones"},{"key":"ppat.1009969.ref051","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1242\/jcs.02381","article-title":"PfEMP1 expression is reduced on the surface of knobless Plasmodium falciparum infected erythrocytes","volume":"118","author":"P Horrocks","year":"2005","journal-title":"J Cell Sci"},{"key":"ppat.1009969.ref052","doi-asserted-by":"crossref","first-page":"5636","DOI":"10.1093\/emboj\/20.20.5636","article-title":"Trafficking and assembly of the cytoadherence complex in Plasmodium falciparum-infected human erythrocytes","volume":"20","author":"ME Wickham","year":"2001","journal-title":"EMBO J"},{"key":"ppat.1009969.ref053","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1038\/s42003-019-0429-z","article-title":"Single-molecule imaging and quantification of the immune-variant adhesin VAR2CSA on knobs of Plasmodium falciparum-infected erythrocytes","volume":"2","author":"CP Sanchez","year":"2019","journal-title":"Commun Biol"},{"key":"ppat.1009969.ref054","doi-asserted-by":"crossref","first-page":"2752","DOI":"10.1021\/acs.jproteome.7b00025","article-title":"Quantitative Analysis of Human Red Blood Cell Proteome","volume":"16","author":"AH Bryk","year":"2017","journal-title":"J Proteome Res"},{"key":"ppat.1009969.ref055","doi-asserted-by":"crossref","first-page":"e0181656","DOI":"10.1371\/journal.pone.0181656","article-title":"The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites","volume":"12","author":"SC Charnaud","year":"2017","journal-title":"PLoS One"},{"key":"ppat.1009969.ref056","article-title":"The Exported Chaperone PfHsp70x Is Dispensable for the Plasmodium falciparum Intraerythrocytic Life Cycle","volume":"2","author":"DW Cobb","year":"2017","journal-title":"mSphere"},{"key":"ppat.1009969.ref057","doi-asserted-by":"crossref","first-page":"3902","DOI":"10.1074\/jbc.M110513200","article-title":"Host chaperones are recruited in membrane-bound complexes by Plasmodium falciparum","volume":"277","author":"G Banumathy","year":"2002","journal-title":"J Biol Chem"},{"key":"ppat.1009969.ref058","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1126\/science.781840","article-title":"Human malaria parasites in continuous culture","volume":"193","author":"W Trager","year":"1976","journal-title":"Science"},{"key":"ppat.1009969.ref059","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1073\/pnas.92.4.973","article-title":"Transfection of Plasmodium falciparum within human red blood cells","volume":"92","author":"Y Wu","year":"1995","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1009969.ref060","doi-asserted-by":"crossref","first-page":"418","DOI":"10.2307\/3280287","article-title":"Synchronization of Plasmodium falciparum erythrocytic stages in culture","volume":"65","author":"C Lambros","year":"1979","journal-title":"J Parasitol"},{"key":"ppat.1009969.ref061","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1080\/00034983.1994.11812859","article-title":"Purification of mature-stage Plasmodium falciparum by gelatine flotation","volume":"88","author":"ID Goodyer","year":"1994","journal-title":"Ann Trop Med Parasitol"},{"key":"ppat.1009969.ref062","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.molbiopara.2019.02.007","article-title":"Immunofluorescence staining protocol for STED nanoscopy of Plasmodium-infected red blood cells","volume":"229","author":"AK Mehnert","year":"2019","journal-title":"Mol Biochem Parasitol"},{"key":"ppat.1009969.ref063","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1083\/jcb.200406019","article-title":"What\u2019s in a picture? The temptation of image manipulation","volume":"166","author":"M Rossner","year":"2004","journal-title":"J Cell Biol"},{"key":"ppat.1009969.ref064","doi-asserted-by":"crossref","first-page":"e61170","DOI":"10.1371\/journal.pone.0061170","article-title":"Life cycle-dependent cytoskeletal modifications in Plasmodium falciparum infected erythrocytes","volume":"8","author":"H Shi","year":"2013","journal-title":"PLoS One"},{"key":"ppat.1009969.ref065","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1083\/jcb.97.3.795","article-title":"Scanning electron microscope-analysis of the protrusions (knobs) present on the surface of Plasmodium falciparum-infected erythrocytes","volume":"97","author":"J Gruenberg","year":"1983","journal-title":"J Cell Biol"},{"key":"ppat.1009969.ref066","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1083\/jcb.57.2.551","article-title":"A technique for ultracryotomy of cell suspensions and tissues","volume":"57","author":"KT Tokuyasu","year":"1973","journal-title":"J Cell Biol"},{"key":"ppat.1009969.ref067","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"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1009969","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,10,25]],"date-time":"2021-10-25T00:00:00Z","timestamp":1635120000000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1009969","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,25]],"date-time":"2021-10-25T13:39:32Z","timestamp":1635169172000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1009969"}},"subtitle":[],"editor":[{"given":"Kirk W.","family":"Deitsch","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2021,10,6]]},"references-count":67,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2021,10,6]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1009969","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2021.03.11.434953","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,10,6]]}}}