ArticleNature microbiology2016
Spirochaete flagella hook proteins self-catalyse a lysinoalanine covalent crosslink for motility.
Article in Nature microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- The bacterial swarming factor SwrD forms hexameric rings reminiscent of DNA-binding proteins.bioRxiv : the preprint server for biology · 2026Article
- An ELISA for discovering protein-protein interaction inhibitors: Blocking lysinoalanine crosslinking between subunits of the spirochete flagellar hook as a test case.SLAS discovery : advancing life sciences R & D · 2026Article
- Inhibitors of Lysinoalanine Cross-Linking in the Flagella Hook as Antimicrobials against Spirochetes.ACS chemical biology · 2025Article
- Lysinoalanine cross-linking is a conserved post-translational modification in the spirochete flagellar hook.PNAS nexus · 2023Article
- The Effect of Dietary Supplementation with Zinc Amino Acids on Immunity, Antioxidant Capacity, and Gut Microbiota Composition in Calves.Animals : an open access journal from MDPI · 2023Article
- An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023Review
- Role of the major determinant of polar flagellation FlhG in the endoflagella-containing spirochete Leptospira.Molecular microbiology · 2021Article
- Bandgap-Coupled Template Autocatalysis toward the Growth of High-Purity spAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Review
- Dehydroamino acid chemical biology: an example of functional group interconversion on proteins.RSC chemical biology · 2020Article
- Spirochete Flagella and Motility.Biomolecules · 2020Review
- An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete.eLife · 2020Article
- Structure and chemistry of lysinoalanine crosslinking in the spirochaete flagella hook.Nature chemical biology · 2019Article
- Architecture and Assembly of Periplasmic Flagellum.Microbiology spectrum · 2019Review
- Design, Validation, and Application of an Enzyme-Coupled Hydrogen Sulfide Detection Assay.Biochemistry · 2019Article
- A pleiotropic role of FlaG in regulating the cell morphogenesis and flagellar homeostasis at the cell poles of Treponema denticola.Cellular microbiology · 2019Article
- Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex.PLoS biology · 2018Article
- Small RNAs ofThe Yale journal of biology and medicine · 2017Review
- Periplasmic flagella in Borrelia burgdoferi function to maintain cellular integrity upon external stress.PloS one · 2017Article
- Bacterial physiology: The ties that bind.Nature microbiology · 2016Article
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
Abstract
Spirochaetes are bacteria responsible for several serious diseases, including Lyme disease (Borrelia burgdorferi), syphilis (Treponema pallidum) and leptospirosis (Leptospira interrogans), and contribute to periodontal diseases (Treponema denticola)(1). These spirochaetes employ an unusual form of flagella-based motility necessary for pathogenicity; indeed, spirochaete flagella (periplasmic flagella) reside and rotate within the periplasmic space(2-11). The universal joint or hook that links the rotary motor to the filament is composed of ∼120-130 FlgE proteins, which in spirochaetes form an unusually stable, high-molecular-weight complex(9,12-17). In other bacteria, the hook can be readily dissociated by treatments such as heat(18). In contrast, spirochaete hooks are resistant to these treatments, and several lines of evidence indicate that the high-molecular-weight complex is the consequence of covalent crosslinking(12,13,17). Here, we show that T. denticola FlgE self-catalyses an interpeptide crosslinking reaction between conserved lysine and cysteine, resulting in the formation of an unusual lysinoalanine adduct that polymerizes the hook subunits. Lysinoalanine crosslinks are not needed for flagellar assembly, but they are required for cell motility and hence infection. The self-catalytic nature of FlgE crosslinking has important implications for protein engineering, and its sensitivity to chemical inhibitors provides a new avenue for the development of antimicrobials targeting spirochaetes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.