Investigation of the effect of posttranslational modification of lipoproteins in TLR2-mediated recognition of Staphylococcus aureus
Investigation of the effect of posttranslational modification of lipoproteins in TLR2-mediated recognition of Staphylococcus aureus
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DissertationPrüfungsdatum
21.08.2025Datum der Veröffentlichung
03.09.2025Erstgutachter
Bekeredjian-Ding, Isabelle BéatriceZweitgutachter
Bierbaum, GabrieleMetadaten
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Inhalt
S. aureus has been postulated to change its lipoprotein acylation patterns under varying environmental conditions. Whether lipoproteins are posttranslationally di- or tri-acylated results in differences in recognition by human Toll-like receptors. In 2012, Kurokawa et al. observed a shift from tri- to di-acylated S. aureus lipoproteins by growth in a decreased pH environment in the stationary phase of growth. The underlying mechanisms, especially the genes involved in tri-acylation of S. aureus lipoproteins, were unknown at that time. Eight years later, Gardiner et al. discovered that two genes lnsA and lnsB encoded enzymes responsible for tri-acylation. LnsA and LnsB activity decreased bacterial recognition by TLR2 and shifted its dimerization partner from TLR6 to TLR1.
Based on these findings, the aim of this study was to investigate whether S. aureus-mediated posttranslational lipoprotein modification under stress conditions is conserved across the S. aureus species. In particular, we hypothesized that regulation of lnsA and lnsB expression under stress conditions results in altered TLR2 recognition and immunogenicity, which could account for host adaptation of S. aureus to colonization and infection.
Based on these findings, the aim of this study was to investigate whether S. aureus-mediated posttranslational lipoprotein modification under stress conditions is conserved across the S. aureus species. In particular, we hypothesized that regulation of lnsA and lnsB expression under stress conditions results in altered TLR2 recognition and immunogenicity, which could account for host adaptation of S. aureus to colonization and infection.
Klassifikation (DDC)
610 Medizin, GesundheitMann, Justus: Investigation of the effect of posttranslational modification of lipoproteins in TLR2-mediated recognition of Staphylococcus aureus. - Bonn, 2025. - Dissertation, Rheinische Friedrich-Wilhelms-Universität Bonn.
Online-Ausgabe in bonndoc: https://nbn-resolving.org/urn:nbn:de:hbz:5-84690
Online-Ausgabe in bonndoc: https://nbn-resolving.org/urn:nbn:de:hbz:5-84690
@phdthesis{handle:20.500.11811/13407,
urn: https://nbn-resolving.org/urn:nbn:de:hbz:5-84690,
doi: https://doi.org/10.48565/bonndoc-642,
author = {{Justus Mann}},
title = {Investigation of the effect of posttranslational modification of lipoproteins in TLR2-mediated recognition of Staphylococcus aureus},
school = {Rheinische Friedrich-Wilhelms-Universität Bonn},
year = 2025,
month = sep,
note = {S. aureus has been postulated to change its lipoprotein acylation patterns under varying environmental conditions. Whether lipoproteins are posttranslationally di- or tri-acylated results in differences in recognition by human Toll-like receptors. In 2012, Kurokawa et al. observed a shift from tri- to di-acylated S. aureus lipoproteins by growth in a decreased pH environment in the stationary phase of growth. The underlying mechanisms, especially the genes involved in tri-acylation of S. aureus lipoproteins, were unknown at that time. Eight years later, Gardiner et al. discovered that two genes lnsA and lnsB encoded enzymes responsible for tri-acylation. LnsA and LnsB activity decreased bacterial recognition by TLR2 and shifted its dimerization partner from TLR6 to TLR1.
Based on these findings, the aim of this study was to investigate whether S. aureus-mediated posttranslational lipoprotein modification under stress conditions is conserved across the S. aureus species. In particular, we hypothesized that regulation of lnsA and lnsB expression under stress conditions results in altered TLR2 recognition and immunogenicity, which could account for host adaptation of S. aureus to colonization and infection.},
url = {https://hdl.handle.net/20.500.11811/13407}
}
urn: https://nbn-resolving.org/urn:nbn:de:hbz:5-84690,
doi: https://doi.org/10.48565/bonndoc-642,
author = {{Justus Mann}},
title = {Investigation of the effect of posttranslational modification of lipoproteins in TLR2-mediated recognition of Staphylococcus aureus},
school = {Rheinische Friedrich-Wilhelms-Universität Bonn},
year = 2025,
month = sep,
note = {S. aureus has been postulated to change its lipoprotein acylation patterns under varying environmental conditions. Whether lipoproteins are posttranslationally di- or tri-acylated results in differences in recognition by human Toll-like receptors. In 2012, Kurokawa et al. observed a shift from tri- to di-acylated S. aureus lipoproteins by growth in a decreased pH environment in the stationary phase of growth. The underlying mechanisms, especially the genes involved in tri-acylation of S. aureus lipoproteins, were unknown at that time. Eight years later, Gardiner et al. discovered that two genes lnsA and lnsB encoded enzymes responsible for tri-acylation. LnsA and LnsB activity decreased bacterial recognition by TLR2 and shifted its dimerization partner from TLR6 to TLR1.
Based on these findings, the aim of this study was to investigate whether S. aureus-mediated posttranslational lipoprotein modification under stress conditions is conserved across the S. aureus species. In particular, we hypothesized that regulation of lnsA and lnsB expression under stress conditions results in altered TLR2 recognition and immunogenicity, which could account for host adaptation of S. aureus to colonization and infection.},
url = {https://hdl.handle.net/20.500.11811/13407}
}
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