{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T01:25:22Z","timestamp":1794273922272,"version":"4.9.0"},"reference-count":54,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,7,6]],"date-time":"2026-07-06T00:00:00Z","timestamp":1783296000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["227774\/Z\/23\/Z"],"award-info":[{"award-number":["227774\/Z\/23\/Z"]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Structural Biology"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.sbi.2026.103336","type":"journal-article","created":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T16:04:51Z","timestamp":1784304291000},"page":"103336","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Structural dissection of apicomplexan gliding motility"],"prefix":"10.1016","volume":"100","author":[{"ORCID":"https:\/\/orcid.org\/0009-0009-8629-8306","authenticated-orcid":false,"given":"Pankti","family":"Vaishnav","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4411-6131","authenticated-orcid":false,"given":"Josie L.","family":"Ferreira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.sbi.2026.103336_bib1","doi-asserted-by":"crossref","DOI":"10.1038\/nrmicro.2017.86","article-title":"Gliding motility powers invasion and egress in Apicomplexa","volume":"15","author":"Fr\u00e9nal","year":"2017","journal-title":"Nat Rev Microbiol"},{"key":"10.1016\/j.sbi.2026.103336_bib2","doi-asserted-by":"crossref","DOI":"10.1128\/MMBR.66.1.21-38.2002","article-title":"Cytoskeleton of apicomplexan parasites","volume":"66","author":"Morrissette","year":"2002","journal-title":"Microbiol Mol Biol Rev"},{"key":"10.1016\/j.sbi.2026.103336_bib3","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.00194","article-title":"Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites","volume":"116","author":"Bergman","year":"2003","journal-title":"J Cell Sci"},{"key":"10.1016\/j.sbi.2026.103336_bib4","article-title":"Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii","volume":"165","author":"Gaskins","year":"2004","journal-title":"JCB (J Cell Biol)"},{"key":"10.1016\/j.sbi.2026.103336_bib5","doi-asserted-by":"crossref","DOI":"10.1016\/j.tcb.2004.08.002","article-title":"The glideosome: a molecular machine powering motility and host-cell invasion by Apicomplexa","volume":"14","author":"Keeley","year":"2004","journal-title":"Trends Cell Biol"},{"key":"10.1016\/j.sbi.2026.103336_bib6","doi-asserted-by":"crossref","DOI":"10.1016\/j.chom.2008.02.006","article-title":"A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion","volume":"3","author":"Baum","year":"2008","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.sbi.2026.103336_sref7","doi-asserted-by":"crossref","DOI":"10.15252\/embr.202357064","article-title":"Conformational change of Plasmodium TRAP is essential for sporozoite migration and transmission","volume":"24","author":"Braumann","year":"2023","journal-title":"EMBO Rep"},{"key":"10.1016\/j.sbi.2026.103336_bib8","doi-asserted-by":"crossref","DOI":"10.1186\/s12936-021-03960-3","article-title":"Limited Plasmodium sporozoite gliding motility in the absence of TRAP family adhesins","volume":"20","author":"Beyer","year":"2021","journal-title":"Malar J"},{"key":"10.1016\/j.sbi.2026.103336_bib9","doi-asserted-by":"crossref","DOI":"10.1093\/emboj\/cdg217","article-title":"Rapid invasion of host cells by toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex","volume":"22","author":"Huynh","year":"2003","journal-title":"EMBO J"},{"key":"10.1016\/j.sbi.2026.103336_bib10","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2005.03.056","article-title":"Malaria parasite actin filaments are very short","volume":"349","author":"Schmitz","year":"2005","journal-title":"J Mol Biol"},{"key":"10.1016\/j.sbi.2026.103336_bib11","doi-asserted-by":"crossref","DOI":"10.1091\/mbc.e05-06-0512","article-title":"Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii","volume":"17","author":"Sahoo","year":"2006","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.sbi.2026.103336_bib12","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002280","article-title":"Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites","volume":"7","author":"Skillman","year":"2011","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.sbi.2026.103336_bib13","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms3285","article-title":"The unusual dynamics of parasite actin result from isodesmic polymerization","volume":"4","author":"Skillman","year":"2013","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103336_bib14","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1906600116","article-title":"Unusual dynamics of the divergent malaria parasite PfAct1 actin filament","volume":"116","author":"Lu","year":"2019","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2026.103336_bib15","doi-asserted-by":"crossref","DOI":"10.1091\/mbc.e02-08-0458","article-title":"Actin filament polymerization regulates gliding motility by apicomplexan parasites","volume":"14","author":"Wetzel","year":"2003","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.sbi.2026.103336_bib16","doi-asserted-by":"crossref","DOI":"10.1186\/s12915-016-0343-5","article-title":"Surface attachment, promoted by the actomyosin system of Toxoplasma gondii is important for efficient gliding motility and invasion","volume":"15","author":"Whitelaw","year":"2017","journal-title":"BMC Biol"},{"key":"10.1016\/j.sbi.2026.103336_bib17","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1707506114","article-title":"Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability","volume":"114","author":"Pospich","year":"2017","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2026.103336_sref18","article-title":"Traction force generation in Plasmodium sporozoites is modulated by a surface adhesin","author":"Ripp","year":"2025","journal-title":"J Microsc"},{"key":"10.1016\/j.sbi.2026.103336_bib19","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010408","article-title":"High-resolution structures of malaria parasite actomyosin and actin filaments","volume":"18","author":"Vahokoski","year":"2022","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.sbi.2026.103336_bib20","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-11120-0","article-title":"Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism","volume":"10","author":"Robert-Paganin","year":"2019","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103336_bib21","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-021-22093-4","article-title":"The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity","volume":"12","author":"Robert-Paganin","year":"2021","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103336_bib22","doi-asserted-by":"crossref","DOI":"10.1007\/s00436-002-0666-8","article-title":"Effect of jasplakinolide on the growth, invasion, and actin cytoskeleton of Plasmodium falciparum","volume":"88","author":"Mizuno","year":"2002","journal-title":"Parasitol Res"},{"key":"10.1016\/j.sbi.2026.103336_bib23","article-title":"Evidence for cleft closure in actomyosin upon ADP release","volume":"7","author":"Volkmann","year":"2000","journal-title":"Nat Struct Biol"},{"key":"10.1016\/j.sbi.2026.103336_bib24","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.60581","article-title":"Full-length plasmodium falciparum myosin a and essential light chain pfelc structures provide new anti-malarial targets","volume":"9","author":"Moussaoui","year":"2020","journal-title":"eLife"},{"key":"10.1016\/j.sbi.2026.103336_sref25","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1011174","article-title":"Structure and function of Plasmodium actin II in the parasite mosquito stages","volume":"19","author":"Lopez","year":"2023","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.sbi.2026.103336_bib26","doi-asserted-by":"crossref","DOI":"10.1038\/347044a0","article-title":"Atomic model of the actin filament","volume":"347","author":"Holmes","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2026.103336_sref27","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-024-46111-3","article-title":"Toxoplasma gondii actin filaments are tuned for rapid disassembly and turnover","volume":"15","author":"Hvorecny","year":"2024","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103336_sref28","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.86049","article-title":"Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii","volume":"12","author":"Kumar","year":"2023","journal-title":"eLife"},{"key":"10.1016\/j.sbi.2026.103336_bib29","doi-asserted-by":"crossref","DOI":"10.1016\/j.chom.2016.10.020","article-title":"An apicomplexan actin-binding protein serves as a connector and lipid sensor to coordinate motility and invasion","volume":"20","author":"Jacot","year":"2016","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.sbi.2026.103336_bib30","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010779","article-title":"Divergent Plasmodium actin residues are essential for filament localization, mosquito salivary gland invasion and malaria transmission","volume":"18","author":"Yee","year":"2022","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.sbi.2026.103336_bib31","doi-asserted-by":"crossref","DOI":"10.15252\/embr.201948896","article-title":"Apicomplexan F-actin is required for efficient nuclear entry during host cell invasion","volume":"20","author":"Del Rosario","year":"2019","journal-title":"EMBO Rep"},{"key":"10.1016\/j.sbi.2026.103336_bib32","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.56635","article-title":"Essential function of the alveolin network in the subpellicular microtubules and conoid assembly in Toxoplasma gondii","volume":"9","author":"Tosetti","year":"2020","journal-title":"eLife"},{"key":"10.1016\/j.sbi.2026.103336_bib33","doi-asserted-by":"crossref","DOI":"10.1038\/s41564-022-01212-x","article-title":"Conoid extrusion regulates glideosome assembly to control motility and invasion in Apicomplexa","volume":"7","author":"Dos Santos Pacheco","year":"2022","journal-title":"Nat Microbiol"},{"key":"10.1016\/j.sbi.2026.103336_bib34","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.42669","article-title":"Three f-actin assembly centers regulate organelle inheritance, cell-cell communication and motility in Toxoplasma gondii","volume":"8","author":"Tosetti","year":"2019","journal-title":"eLife"},{"key":"10.1016\/j.sbi.2026.103336_sref35","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-023-40520-6","article-title":"Origin and arrangement of actin filaments for gliding motility in apicomplexan parasites revealed by cryo-electron tomography","volume":"14","author":"Martinez","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103336_sref36","article-title":"Atomic models of the toxoplasma cell invasion machinery","author":"Zeng","year":"2025","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.sbi.2026.103336_sref37","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2416602121","article-title":"Architecture of the Toxoplasma gondii apical polar ring and its role in gliding motility and invasion","volume":"121","author":"Ren","year":"2024","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2026.103336_bib38","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.73.9.5379-5387.2005","article-title":"Gliding motility leads to active cellular invasion by Cryptosporidium parvum sporozoites","volume":"73","author":"Wetzel","year":"2005","journal-title":"Infect Immun"},{"key":"10.1016\/j.sbi.2026.103336_bib39","doi-asserted-by":"crossref","DOI":"10.1016\/j.chom.2021.07.002","article-title":"Cryptosporidium rhoptry effector protein ROP1 injected during invasion targets the host cytoskeletal modulator LMO7","volume":"29","author":"Gu\u00e9rin","year":"2021","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.sbi.2026.103336_bib40","doi-asserted-by":"crossref","DOI":"10.1038\/nm1350","article-title":"Quantitative imaging of Plasmodium transmission from mosquito to mammal","volume":"12","author":"Amino","year":"2006","journal-title":"Nat Med"},{"key":"10.1016\/j.sbi.2026.103336_bib41","article-title":"Cellular hallmarks from volume electron microscopy reveal developmental progression of plasmodium ookinetes","author":"Darif","year":"2025","journal-title":"Adv Sci"},{"key":"10.1016\/j.sbi.2026.103336_sref42","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-023-36627-5","article-title":"Variable microtubule architecture in the malaria parasite","volume":"14","author":"Ferreira","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103336_bib43","article-title":"Expansion microscopy provides new insights into the cytoskeleton of malaria parasites including the conservation of a conoid","volume":"19","author":"Bertiaux","year":"2021","journal-title":"PLoS Biol"},{"key":"10.1016\/j.sbi.2026.103336_bib44","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3001081","article-title":"Molecular characterization of the conoid complex in toxoplasma reveals its conservation in all apicomplexans, including Plasmodium species","volume":"19","author":"Koreny","year":"2021","journal-title":"PLoS Biol"},{"key":"10.1016\/j.sbi.2026.103336_bib45","doi-asserted-by":"crossref","DOI":"10.1091\/mbc.10.11.3539","article-title":"Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion","volume":"10","author":"H\u00e5kansson","year":"1999","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.sbi.2026.103336_bib46","doi-asserted-by":"crossref","DOI":"10.1021\/acsnano.0c01893","article-title":"Coupling polar adhesion with traction, spring, and torque forces allows high-speed helical migration of the protozoan parasite toxoplasma","volume":"14","author":"Pavlou","year":"2020","journal-title":"ACS Nano"},{"key":"10.1016\/j.sbi.2026.103336_bib47","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2114442118","article-title":"Gliding motility of Plasmodium merozoites","volume":"118","author":"Yahata","year":"2021","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2026.103336_sref48","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.261270","article-title":"The cortical microtubules of Toxoplasma gondii underlie the helicity of parasite movement","volume":"136","author":"Tengganu","year":"2023","journal-title":"J Cell Sci"},{"key":"10.1016\/j.sbi.2026.103336_bib49","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2018100984","article-title":"Microtubule number and length determine cellular shape and function in Plasmodium","volume":"38","author":"Spreng","year":"2019","journal-title":"EMBO J"},{"key":"10.1016\/j.sbi.2026.103336_sref50","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1038\/s44319-025-00415-7","article-title":"Molecular architecture of glideosome and nuclear F-actin in Plasmodium falciparum","volume":"26","author":"Pra\u017e\u00e1k","year":"2025","journal-title":"EMBO Rep"},{"key":"10.1016\/j.sbi.2026.103336_bib51","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.2005345","article-title":"Inter-subunit interactions drive divergent dynamics in mammalian and Plasmodium actin filaments","volume":"16","author":"Douglas","year":"2018","journal-title":"PLoS Biol"},{"key":"10.1016\/j.sbi.2026.103336_bib52","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005710","article-title":"The actin filament-binding protein coronin regulates motility in plasmodium sporozoites","volume":"12","author":"Bane","year":"2016","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.sbi.2026.103336_bib53","doi-asserted-by":"crossref","DOI":"10.1186\/s12936-015-0801-5","article-title":"Plasmodium falciparum coronin organizes arrays of parallel actin filaments potentially guiding directional motility in invasive malaria parasites","volume":"14","author":"Olshina","year":"2015","journal-title":"Malar J"},{"key":"10.1016\/j.sbi.2026.103336_bib54","doi-asserted-by":"crossref","DOI":"10.1038\/s42003-020-01283-8","article-title":"Structural role of essential light chains in the apicomplexan glideosome","volume":"3","author":"Pazicky","year":"2020","journal-title":"Commun Biol"}],"container-title":["Current Opinion in Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X26001181?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X26001181?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T01:11:37Z","timestamp":1794273097000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959440X26001181"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":54,"alternative-id":["S0959440X26001181"],"URL":"https:\/\/doi.org\/10.1016\/j.sbi.2026.103336","relation":{},"ISSN":["0959-440X"],"issn-type":[{"value":"0959-440X","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural dissection of apicomplexan gliding motility","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Structural Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.sbi.2026.103336","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"103336"}}