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Akademický článek

Receptor Binding Domains of TcdB from Clostridioides difficile for Chondroitin Sulfate Proteoglycan-4 and Frizzled Proteins Are Functionally Independent and Additive

Autor: Daniel Henkel, Helma Tatge, Dennis Schöttelndreier, Liang Tao, Min Dong, Ralf Gerhard

Publikováno v: Toxins, Vol 12, Iss 12, p 736 (2020)

Toxin B (TcdB) produced by Clostridioides difficile is a main pathogenicity factor that affects a variety of different cell types within the colonic mucosa. TcdB is known to utilize frizzled-1,2,7 and chondroitin sulfate proteoglycan-4 (CSPG4) as pro

Externí odkaz: https://doaj.org/article/eb60eca2b4744670acd0ec51a41bb789

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Akademický článek

The Conserved Cys-2232 in Clostridioides difficile Toxin B Modulates Receptor Binding

Autor: Soo-Young Chung, Dennis Schöttelndreier, Helma Tatge, Viola Fühner, Michael Hust, Lara-Antonia Beer, Ralf Gerhard

Publikováno v: Frontiers in Microbiology, Vol 9 (2018)

Clostridioides difficile toxins TcdA and TcdB are large clostridial glucosyltransferases which are the main pathogenicity factors in C. difficile-associated diseases. Four highly conserved cysteines are present in all large clostridial glucosyltransf

Externí odkaz: https://doaj.org/article/0d2807aa83454b7c96dfa8b97a7a32ca

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Akademický článek

The Combined Repetitive Oligopeptides of Clostridium difficile Toxin A Counteract Premature Cleavage of the Glucosyl-Transferase Domain by Stabilizing Protein Conformation

Autor: Alexandra Olling, Corinna Hüls, Sebastian Goy, Mirco Müller, Simon Krooss, Isa Rudolf, Helma Tatge, Ralf Gerhard

Publikováno v: Toxins, Vol 6, Iss 7, Pp 2162-2176 (2014)

Toxin A (TcdA) and B (TcdB) from Clostridium difficile enter host cells by receptor-mediated endocytosis. A prerequisite for proper toxin action is the intracellular release of the glucosyltransferase domain by an inherent cysteine protease, which is

Externí odkaz: https://doaj.org/article/7d1a453efcda473a9fb37522bfbb3547

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Akademický článek

The Binary Toxin CDT of Clostridium difficile as a Tool for Intracellular Delivery of Bacterial Glucosyltransferase Domains

Autor: Lara-Antonia Beer, Helma Tatge, Carmen Schneider, Maximilian Ruschig, Michael Hust, Jessica Barton, Stefan Thiemann, Viola Fühner, Giulio Russo, Ralf Gerhard

Publikováno v: Toxins, Vol 10, Iss 6, p 225 (2018)

Binary toxins are produced by several pathogenic bacteria. Examples are the C2 toxin from Clostridium botulinum, the iota toxin from Clostridium perfringens, and the CDT from Clostridium difficile. All these binary toxins have ADP-ribosyltransferases

Externí odkaz: https://doaj.org/article/bb87663f836244c28147411cb7715fe8

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Akademický článek

Serine-71 phosphorylation of Rac1 modulates downstream signaling.

Autor: Janett Schwarz, Julia Proff, Anika Hävemeier, Markus Ladwein, Klemens Rottner, Britta Barlag, Andreas Pich, Helma Tatge, Ingo Just, Ralf Gerhard

Publikováno v: PLoS ONE, Vol 7, Iss 9, p e44358 (2012)

The Rho GTPases Rac1 and Cdc42 regulate a variety of cellular functions by signaling to different signal pathways. It is believed that the presence of a specific effector at the location of GTPase activation determines the route of downstream signali

Externí odkaz: https://doaj.org/article/5e44924797cc488a8fbeaeddd3ecf374

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Akademický článek

The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A.

Autor: Alexandra Olling, Sebastian Goy, Florian Hoffmann, Helma Tatge, Ingo Just, Ralf Gerhard

Publikováno v: PLoS ONE, Vol 6, Iss 3, p e17623 (2011)

The pathogenicity of Clostridium difficile is primarily linked to secretion of the intracellular acting toxins A (TcdA) and B (TcdB) which monoglucosylate and thereby inactivate Rho GTPases of host cells. Although the molecular mode of action of TcdA

Externí odkaz: https://doaj.org/article/65c59061c845439185b277ed449cb002

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Impairment of lysosomal function by Clostridioides difficile TcdB

Autor: Carmen Klepka, Moritz Sandmann, Helma Tatge, Matthew Mangan, Annabel Arens, Daniel Henkel, Ralf Gerhard

Publikováno v: Molecular microbiology 117(2), 493-507 (2022). doi:10.1111/mmi.14864

TcdB is a potent cytotoxin produced by pathogenic Clostridioides difficile that inhibits Rho GTPases by mono-glucosylation. TcdB enters cells via receptor-mediated endocytosis. The pathogenic glucosyltransferase domain (GTD) egresses endosomes by pH-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8af5bef71e9418fd4c0a2a3c1227bf30
https://pub.dzne.de/record/163585