<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Martin FS</submitter><funding>NIAID NIH HHS</funding><funding>NIGMS NIH HHS</funding><pubmed_abstract>Spirochete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike other bacterial flagella, are encased in a spirochete-specific multi-protein sheath and deform the cell body into motile waves. How these filaments achieve the mechanical properties needed for invasive motility has remained unclear. Here we determine complete atomic structures of the &lt;i>Leptospira&lt;/i> endoflagellar filament, revealing an elaborate sheath of 9 to 12 distinct asymmetrically arranged proteins. We show that the flagellin variant forming the filament core determines sheath composition, producing curvatures ranging from ∼3.5 µm &lt;sup>-1&lt;/sup> to ∼5 µm &lt;sup>-1&lt;/sup> . The lower-curvature</pubmed_abstract><journal>bioRxiv : the preprint server for biology</journal><pagination>2026.02.02.703089</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12889604</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Core-sheath coupling controls flagellar curvature and motility in &amp;lt;i&amp;gt;Leptospira&amp;lt;/i&amp;gt;.</pubmed_title><pmcid>PMC12889604</pmcid><funding_grant_id>T32 GM008283</funding_grant_id><funding_grant_id>R01 AI052473</funding_grant_id><funding_grant_id>P01 AI168148</funding_grant_id><funding_grant_id>R21 AI163663</funding_grant_id><funding_grant_id>R01 AI182354</funding_grant_id><pubmed_authors>Mondino S</pubmed_authors><pubmed_authors>Rey M</pubmed_authors><pubmed_authors>Sindelar CV</pubmed_authors><pubmed_authors>Fule L</pubmed_authors><pubmed_authors>Nouchikian L</pubmed_authors><pubmed_authors>Duran R</pubmed_authors><pubmed_authors>Chamot-Rooke J</pubmed_authors><pubmed_authors>Trajtenberg F</pubmed_authors><pubmed_authors>Martin FS</pubmed_authors><pubmed_authors>Brady MR</pubmed_authors><pubmed_authors>Rodriguez A</pubmed_authors><pubmed_authors>Picardeau M</pubmed_authors><pubmed_authors>Buschiazzo A</pubmed_authors><pubmed_authors>Ko AI</pubmed_authors><pubmed_authors>Larrieux N</pubmed_authors><pubmed_authors>Wunder EA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Core-sheath coupling controls flagellar curvature and motility in &amp;lt;i&amp;gt;Leptospira&amp;lt;/i&amp;gt;.</name><description>Spirochete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike other bacterial flagella, are encased in a spirochete-specific multi-protein sheath and deform the cell body into motile waves. How these filaments achieve the mechanical properties needed for invasive motility has remained unclear. Here we determine complete atomic structures of the &lt;i>Leptospira&lt;/i> endoflagellar filament, revealing an elaborate sheath of 9 to 12 distinct asymmetrically arranged proteins. We show that the flagellin variant forming the filament core determines sheath composition, producing curvatures ranging from ∼3.5 µm &lt;sup>-1&lt;/sup> to ∼5 µm &lt;sup>-1&lt;/sup> . The lower-curvature</description><dates><release>2026-01-01T00:00:00Z</release><publication>2026 Feb</publication><modification>2026-07-12T03:14:27.728Z</modification><creation>2026-07-12T03:09:13.113Z</creation></dates><accession>S-EPMC12889604</accession><cross_references><pubmed>41676522</pubmed><doi>10.64898/2026.02.02.703089</doi></cross_references></HashMap>