David Gerlach
University of Tübingen
12 Papers
David Gerlach is an academic researcher from University of Tübingen. The author has contributed to research in topics: Staphylococcus aureus & Teichoic acid. The author has an hindex of 5, co-authored 8 publications.
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Papers
Methicillin-resistant Staphylococcus aureus alters cell wall glycosylation to evade immunity.
David Gerlach,Yinglan Guo,Cristina De Castro,Sun-Hwa Kim,Katja Schlatterer,Fei-Fei Xu,Claney L. Pereira,Peter H. Seeberger,Sara Ali,Jeroen D. C. Codée,Wanchat Sirisarn,Berit Schulte,Christiane Wolz,Jesper Larsen,Antonio Molinaro,Bok Luel Lee,Guoqing Xia,Thilo Stehle,Thilo Stehle,Andreas Peschel +19 more
TL;DR: This study reveals an immune evasion strategy of S. aureus based on averting the immunogenicity of its dominant glycoantigen WTA and may enable the development of TarP inhibitors as a new strategy for rendering MRSA susceptible to human host defences.
An accessory wall teichoic acid glycosyltransferase protects Staphylococcus aureus from the lytic activity of Podoviridae.
Xuehua Li,David Gerlach,Xin Du,Jesper Larsen,Marc Stegger,Marc Stegger,Petra Kühner,Andreas Peschel,Guoqing Xia,Guoqing Xia,Volker Winstel,Volker Winstel +11 more
TL;DR: A novel strategy of S. aureus is described, which protects against the lytic activity of Podoviridae, a unique family of staphylococcal lytic phages with short, non-contractile tails, indicating that a “glyco-switch” of WTA O-GlcNAcylation can prevent the infection by certain staphlyococcal phages.
Impact of Glycan Linkage to Staphylococcus aureus Wall Teichoic Acid on Langerin Recognition and Langerhans Cell Activation.
Astrid Hendriks,Astrid Hendriks,Rob van Dalen,Sara Ali,David Gerlach,Gijsbert A. van der Marel,Felix F. Fuchsberger,Piet C. Aerts,Carla J. C. de Haas,Andreas Peschel,Christoph Rademacher,Jos A. G. van Strijp,Jeroen D. C. Codée,Nina M. van Sorge +13 more
TL;DR: In this paper, the impact of β-GlcNAc linkage position on langerin binding and activation was investigated for staphylococcus aureus skin invasion.
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Structural and Enzymatic Analysis of TarM Glycosyltransferase from Staphylococcus aureus Reveals an Oligomeric Protein Specific for the Glycosylation of Wall Teichoic Acid
TL;DR: The structure-function analysis helps define the biosynthetic pathway leading to WTA glycosylation in S. aureus and identifies residues critical for enzyme activity, assign a putative role for the HUB in TarM function, and allow us to propose a likely reaction mechanism.
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Reply to: Do not discard Staphylococcus aureus WTA as a vaccine antigen.
TL;DR: It is shown that this alternative WTA epitope actually represents a highly dominant antigen in the reactive antibody pool against S. aureus in humans and should not be discarded as an antigen for vaccines that target S.Aureus.
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