Charakterisierung der bakteriellen Toxine YART und YGT aus Yersinia mollaretii

Abstract: At least 18 Yersinia species are known. Only three of them are recognized as human pathogenic species including Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis. Yersinia produce numerous types of protein toxins and effectors. Best known are Yersinia outer proteins (YOPs), which are translocated into target cells by the type-III-secretion system.
Here, we report on novel putative Yersinia toxins, which share the structure of large clostridial glucosylating toxins. The Yersinia toxins contains an N-terminal enzyme domain, which is followed by a cysteine protease domain. The C-terminal parts of the toxins exhibit significant sequence similarity with the delivery domains of large clostridial toxins. The enzyme domain of the Yersinia toxin, termed YGT, possesses glycohydrolase and glycosyltransferase activity. Surprisingly, the enzyme domain of the second Yersinia toxin, termed YART, harbors ADP-ribosyltransferase activity. Like the auto-protease domains of clostridial glycosylating toxins, the cysteine-protease domains of YART and YGT are activated by InsP6. This activation results in cleavage of the holotoxin and release of ADP-ribosyltransferase domain in the case of YART. However, activation of the cysteine domain of YGT results in cleavage of the holotoxin downstream of the cysteine domain, thereby releasing the glycosyltransferase domain linked to the cysteine protease domain.
The data indicate that typical toxin modules known from large clostridial glucosylating toxins are found in various Yersinia proteins. Targets and functions of the putative toxins are currently studied in the laboratory

Angaben zum Objekt

• Standort: Deutsche Nationalbibliothek Frankfurt am Main
• Umfang: Online-Ressource
• Sprache: Deutsch
• Anmerkungen: Universität Freiburg, Dissertation, 2019

Klassifikation und Themen

• Schlagwort: Clostridium difficile ; Yersinia ; Domäne ; Rab-Proteine ; Bakterien ; Clostridium difficile ; Glycosyltransferasen ; ADP-Ribosyltransferasen ; Rab-Proteine ; Intrazellulärer Transport ; Cysteinproteasen

Beteiligte, Orts- und Zeitangaben

• Ereignis: Veröffentlichung
• (wo): Freiburg
• (wer): Universität
• (wann): 2019
• Urheber: Ost, Gerhard Stefan
• Beteiligte Personen und Organisationen: Aktories, Klaus ; Albert-Ludwigs-Universität Freiburg. Fakultät für Biologie

Weitere Informationen

• DOI: 10.6094/UNIFR/150030
• URN: urn:nbn:de:bsz:25-freidok-1500308
• Rechteinformation: Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Letzte Aktualisierung: 25.03.2025, 13:58 MEZ