Document Type
Article
Publication Date
4-24-2020
Abstract
The long external filament of bacterial flagella is composed of several thousand copies of a single protein, flagellin. Here, we explore the role played by lysine methylation of flagellin in Salmonella, which requires the methylase FliB. We show that both flagellins of Salmonella enterica serovar Typhimurium, FliC and FljB, are methylated at surface-exposed lysine residues by FliB. A Salmonella Typhimurium mutant deficient in flagellin methylation is outcompeted for gut colonization in a gastroenteritis mouse model, and methylation of flagellin promotes bacterial invasion of epithelial cells in vitro. Lysine methylation increases the surface hydrophobicity of flagellin, and enhances flagella-dependent adhesion of Salmonella to phosphatidylcholine vesicles and epithelial cells. Therefore, posttranslational methylation of flagellin facilitates adhesion of Salmonella Typhimurium to hydrophobic host cell surfaces, and contributes to efficient gut colonization and host infection.
Recommended Citation
Horstmann, Julia A; Lunelli, Michele; Cazzola, Hélène; Heidemann, Johannes; Kühne, Caroline; Steffen, Pascal; Szefs, Sandra; Rossi, Claire; Lokareddy, Ravi K; Wang, Chu; Lemaire, Laurine; Hughes, Kelly T; Uetrecht, Charlotte; Schlüter, Hartmut; Grassl, Guntram A; Stradal, Theresia E B; Rossez, Yannick; Kolbe, Michael; and Erhardt, Marc, "Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion." (2020). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 167.
https://jdc.jefferson.edu/bmpfp/167
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
PubMed ID
32332720
Language
English
Comments
This article is the final published version from Nature Communications, Volume 11, Issue 1, 2020, 2013
The published version of this article can be found at https://doi.org/10.1038/s41467-020-15738-3.
Copyright Horstmann et.al.