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Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion

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Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion. / 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; Erhardt, Marc.

In: NAT COMMUN, Vol. 11, No. 1, 24.04.2020, p. 2013.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Horstmann, JA, Lunelli, M, Cazzola, H, Heidemann, J, Kühne, C, Steffen, P, Szefs, S, Rossi, C, Lokareddy, RK, Wang, C, Lemaire, L, Hughes, KT, Uetrecht, C, Schlüter, H, Grassl, GA, Stradal, TEB, Rossez, Y, Kolbe, M & Erhardt, M 2020, 'Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion', NAT COMMUN, vol. 11, no. 1, pp. 2013. https://doi.org/10.1038/s41467-020-15738-3

APA

Horstmann, J. A., Lunelli, M., Cazzola, H., Heidemann, J., Kühne, C., Steffen, P., Szefs, S., Rossi, C., Lokareddy, R. K., Wang, C., Lemaire, L., Hughes, K. T., Uetrecht, C., Schlüter, H., Grassl, G. A., Stradal, T. E. B., Rossez, Y., Kolbe, M., & Erhardt, M. (2020). Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion. NAT COMMUN, 11(1), 2013. https://doi.org/10.1038/s41467-020-15738-3

Vancouver

Horstmann JA, Lunelli M, Cazzola H, Heidemann J, Kühne C, Steffen P et al. Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion. NAT COMMUN. 2020 Apr 24;11(1):2013. https://doi.org/10.1038/s41467-020-15738-3

Bibtex

@article{c4ca1999ef08433c9fb6a1c065ad9a0c,
title = "Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion",
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.",
author = "Horstmann, {Julia A} and Michele Lunelli and H{\'e}l{\`e}ne Cazzola and Johannes Heidemann and Caroline K{\"u}hne and Pascal Steffen and Sandra Szefs and Claire Rossi and Lokareddy, {Ravi K} and Chu Wang and Laurine Lemaire and Hughes, {Kelly T} and Charlotte Uetrecht and Hartmut Schl{\"u}ter and Grassl, {Guntram A} and Stradal, {Theresia E B} and Yannick Rossez and Michael Kolbe and Marc Erhardt",
year = "2020",
month = apr,
day = "24",
doi = "10.1038/s41467-020-15738-3",
language = "English",
volume = "11",
pages = "2013",
journal = "NAT COMMUN",
issn = "2041-1723",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion

AU - Horstmann, Julia A

AU - Lunelli, Michele

AU - Cazzola, Hélène

AU - Heidemann, Johannes

AU - Kühne, Caroline

AU - Steffen, Pascal

AU - Szefs, Sandra

AU - Rossi, Claire

AU - Lokareddy, Ravi K

AU - Wang, Chu

AU - Lemaire, Laurine

AU - Hughes, Kelly T

AU - Uetrecht, Charlotte

AU - Schlüter, Hartmut

AU - Grassl, Guntram A

AU - Stradal, Theresia E B

AU - Rossez, Yannick

AU - Kolbe, Michael

AU - Erhardt, Marc

PY - 2020/4/24

Y1 - 2020/4/24

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-020-15738-3

DO - 10.1038/s41467-020-15738-3

M3 - SCORING: Journal article

C2 - 32332720

VL - 11

SP - 2013

JO - NAT COMMUN

JF - NAT COMMUN

SN - 2041-1723

IS - 1

ER -