{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/peptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/proteinGroups.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/20210223_Q1_MD_ColQ1-106_Picardeau_FlaB1_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/20210223_Q1_MD_ColQ1-106_Picardeau_FlaB1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/20210223_Q1_MD_ColQ1-106_Picardeau_FlaB1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/20210223_Q1_MD_ColQ1-106_Picardeau_FlaB1_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/20210223_Q1_MD_ColQ1-106_Picardeau_FlaB1_3.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD077813/214675_5_Linterrogans_serovar_Manilae_PATRIC.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["julia.chamot-rooke@pasteur.fr"],"submitter":["Martial Rey"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Lc-ms/ms","Bottom up","Flagella","Cryoem","Leptospira"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077813"],"sample_protocol":["Protein digestion Sample were diluted in 8 M urea, 100 mM Tris HCl pH 8.5 to obtain a final urea concentration up to 6 M. Proteins were reduced using 5mM TCEP for 30 min at room temperature. Alkylation of the reduced disulfide bridges was performed using 10mM iodoacetamide for 30 min at room temperature in the dark. Proteins were then digested in two steps, first with 1 µg r-LysC Mass Spec Grade (Promega) for 4 h at 30°C and then samples were diluted below 2 M urea with 100 mM Tris HCl pH 8.5 and 1 µg Sequencing Grade Modified Trypsin was added for the second digestion overnight at 37°C. Proteolysis was stopped by adding formic acid (FA) at a final concentration of 5%. The resulting peptides were desalted and concentrated on Sep-Pak C18 SPE cartridge (Waters, Milford, MA, USA) according to manufacturer’s instructions. Peptides were eluted using 50 % acetonitrile (ACN), 0.1 % formic acid (FA). Peptides were concentrated to dryness and resuspended in 2 % acetonitrile (ACN)/0.1 % FA just prior to LC-MS injection. LC-MS/MS analysis LC-MS/MS analysis was performed on a Q Exactive™ Plus Mass Spectrometer (Thermo Fisher Scientific) coupled with a Proxeon EASY-nLC 1200 (Thermo Fisher Scientific). One µg of peptides was injected onto a home-made 40 cm C18 column (1.9 μm particles, 100 Å pore size, ReproSil-Pur Basic C18, Dr. Maisch GmbH, Ammerbuch-Entringen, Germany). Column equilibration and peptide loading were done at 900 bars in buffer A (0.1 % FA). Peptides were separated with a multi-step gradient from 3 to 22 % buffer B (80 % ACN, 0.1 % FA) in 110 min, 22 to 38 % buffer B in 35 min, 38 to 56 % buffer B in 15 min and finally 56 to 75% buffer B in 5 min at a flow rate of 250 nL/min. Column temperature was set to 60°C. MS data were acquired using Xcalibur software using a data-dependent method. MS scans were acquired at a resolution of 70,000 and MS/MS scans (fixed first mass 100 m/z) at a resolution of 17,500. The AGC target and maximum injection time for the survey scans and the MS/MS scans were set to 3E6, 20ms and 1E6, 60ms respectively. An automatic selection of the 10 most intense precursor ions was activated (Top 10) with a 45 s dynamic exclusion. The isolation window was set to 1.6 m/z and normalized collision energy fixed to 28 for HCD fragmentation. We used an underfill ratio of 1.0 % corresponding to an intensity threshold of 1.7E5. Unassigned precursor ion charge states as well as 1, 7, 8 and >8 charged states were rejected and peptide match was disable."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Protein identification and quantification Acquired Raw data were analyzed using MaxQuant software version 2.8.0.0 using the Andromeda search engine. The MS/MS spectra were searched against the Leptospira interrogans serovar Manilae database (https://www.patricbrc.org/view/Genome/214675.5) (4,561 entries). All searches were performed with oxidation of methionine and protein N-terminal acetylation as variable modifications and cysteine carbamidomethylation as fixed modification. Trypsin was selected as protease allowing for up to two missed cleavages. The minimum peptide length was set to 7 amino acids and the peptide mass was limited to a maximum of 4,600 Da. One unique peptide to the protein group was required for the protein identification. The main search peptide tolerance was set to 4.5 ppm and to 20 ppm for the MS/MS match tolerance. Second peptides was enabled to identify co-fragmentation events and match between runs option was selected with a match time window of 0.4 min over an alignment time window of 20 min."],"omics_type":["Proteomics"],"labhead":["Julia Chamot-Rooke"],"instrument_platform":[""],"labhead_affiliation":["Institut Pasteur, Université Paris Cité, CNRS UAR 2024, Mass Spectrometry for Biology Unit, Paris, France"],"submission_type":["PARTIAL"],"species":["Leptospira Interrogans Serovar Manilae"],"submitter_mail":["martial.rey@pasteur.fr"],"publication":["Not available"],"submitter_affiliation":["CNRS, Pasteur"],"submitter_country":["France"],"additional_accession":[]},"is_claimable":false,"name":"Core–sheath coupling controls flagellar curvature and motility in Leptospira","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 Leptospira 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-1 to ~5 µm-1. The lower-curvature architecture, employed by pathogenic Leptospira interrogans, proves essential for motility in viscous environments and during infection. Thus, Leptospira achieves environment-specific motility through modular core–sheath coupling, linking atomic scale strstructural plasticity to large-scale changes in swimming behaviour. Conservation of key sheath components suggests this mechanism may extend across 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