Proteomics

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Lysinoalanine crosslinking is a conserved post-translational modification in the spirochete flagellar hookLysinoalanine crosslinking is a conserved post-translational modification in the spirochete flagellar hook


ABSTRACT: In this project, we investigated whether diverse spirochete species contain lysinoalanine cross-linkages between conserved residues in their flagellar hook proteins (FlgE). We examined the following species: Treponema denticola¸ Borreliella burgdorferi, Treponema phagedenis, Treponema pallidum, Brachyspira hyodysenteriae, Leptospira interrogans. For each bacterial species, we examined a variety of different sample types, including recombinantly produced FlgE, polyhooks purified from flik knock-out strains, and wild-type periplasmic filaments. Overall, our data suggests that lysinoalanine crosslinking in a conserved FlgE post-translational modification in spirochetes and is required for the unique motility of these organisms. For more information, please see the following manuscript: https://doi.org/10.1101/2023.06.13.544825.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Borrelia Sp. Bc1

TISSUE(S): Cell Culture

SUBMITTER: Qin Fu  

LAB HEAD: Sheng Zhang

PROVIDER: PXD045997 | Pride | 2024-01-26

REPOSITORIES: Pride

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Lysinoalanine cross-linking is a conserved post-translational modification in the spirochete flagellar hook.

Lynch Michael J MJ   Deshpande Maithili M   Kurniyati Kurni K   Zhang Kai K   James Milinda M   Miller Michael M   Zhang Sheng S   Passalia Felipe J FJ   Wunder Elsio A EA   Charon Nyles W NW   Li Chunhao C   Crane Brian R BR  

PNAS nexus 20231026 12


Spirochetes cause Lyme disease, leptospirosis, syphilis, and several other human illnesses. Unlike other bacteria, spirochete flagella are enclosed within the periplasmic space where the filaments distort and push the cell body by the action of the flagellar motors. We previously demonstrated that the oral pathogen <i>Treponema denticola</i> (Td) and Lyme disease pathogen <i>Borreliella burgdorferi</i> (Bb) form covalent lysinoalanine (Lal) cross-links between conserved cysteine and lysine resid  ...[more]

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