{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Doran MH"],"funding":["NIAID NIH HHS","Wellcome Trust","NIGMS NIH HHS"],"pagination":["eadr5507"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7617938"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["387(6739)"],"pubmed_abstract":["The movement and pathogenicity of trypanosomatid species, the causative agents of trypanosomiasis and leishmaniasis, are dependent on a flagellum that contains an axoneme of dynein-bound doublet microtubules (DMTs). In this work, we present cryo-electron microscopy structures of DMTs from two trypanosomatid species, <i>Leishmania tarentolae</i> and <i>Crithidia fasciculata</i>, at resolutions up to 2.7 angstrom. The structures revealed 27 trypanosomatid-specific microtubule inner proteins, a specialized dynein-docking complex, and the presence of paralogous proteins that enable higher-order periodicities or proximal-distal patterning. Leveraging the genetic tractability of trypanosomatid species, we quantified the location and contribution of each structure-identified protein to swimming b"],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Evolutionary adaptations of doublet microtubules in trypanosomatid parasites."],"pmcid":["PMC7617938"],"funding_grant_id":["R01 AI179885","211075/Z/18/Z","R01 GM143183","R01 GM141109","R01 GM138854"],"pubmed_authors":["Brown A","Fochler S","Wheeler RJ","Zhang R","Smith J","Beneke T","Coscia A","Doran MH","Hoog JL","Niu Q","Lishko PV","Zeng J","Ren P","Gluenz E","Meleppattu S"],"additional_accession":[]},"is_claimable":false,"name":"Evolutionary adaptations of doublet microtubules in trypanosomatid parasites.","description":"The movement and pathogenicity of trypanosomatid species, the causative agents of trypanosomiasis and leishmaniasis, are dependent on a flagellum that contains an axoneme of dynein-bound doublet microtubules (DMTs). In this work, we present cryo-electron microscopy structures of DMTs from two trypanosomatid species, <i>Leishmania tarentolae</i> and <i>Crithidia fasciculata</i>, at resolutions up to 2.7 angstrom. The structures revealed 27 trypanosomatid-specific microtubule inner proteins, a specialized dynein-docking complex, and the presence of paralogous proteins that enable higher-order periodicities or proximal-distal patterning. Leveraging the genetic tractability of trypanosomatid species, we quantified the location and contribution of each structure-identified protein to swimming b","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-03-16T08:59:04.211Z","creation":"2025-08-17T03:06:13.482Z"},"accession":"S-EPMC7617938","cross_references":{"pubmed":["40080577"],"doi":["10.1126/science.adr5507"]}}