ADP-Ribosylation and Beyond

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: 31 July 2024 | Viewed by 1786

Special Issue Editor

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Guest Editor
Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan
Interests: ADP-ribosylating toxin; binary toxin; protein translocation; clostridium perfringens toxin; clostridioides difficile toxin; toxin-host interaction

Special Issue Information

Dear Colleagues,

ADP-ribosylation is a reversible post-translational modification defined by adding ADP-ribose moieties from NAD+ to the target. ADP-ribosylaton is widely used post-trans-modifications in all kingdoms of life. The system likely originated in bacteria, which functions in inter- and intra-species signalling, and stress response. At first, as bacterial toxins, it was found that cholera toxin ADP-ribosylates a specific arginine in the Gsa of heteromeric G-proteins, and the diphtheria toxin ADP-ribosdylates the eukaryotic elongation factor 2 (eEF2). Later, the ARTC and ARTD families were named because they are characterized by a catalytic domain fold related to cholera toxin or diphtheria toxin, respectively. For understanding mammalian ADP-ribosylation systems, these classifications were used. Later, other toxins such as C3 exoenzyme and C2 toxin were found to ADP-ribosylate RhoA and actin, respectively. These canonical bacterial toxins studies could give us basic knowledge of ADP-ribosylation.

On the other hand, recent studies opened the non-canonical ADP-ribosylation system. (1) DNA ADP-ribosylation: The target of ADP-ribosylation is not only protein but also nucleic acids, DNA. For example, pierisin found in cabbage butterflies was shown to modify DNA. Its related enzyme Streptomyces coelicolor ScARP ADP-ribosylates GDP. Following, reversible ADP-ribosylation of DNA on thymidine bases occurs through the DarT-DarG toxin-antitoxin system, which is found in a variety of bacteria, including such as Mycobacterium tuberculosis, enteropathogenic Escherichia coli and Pseudomonas aeruginosa. (2) Ubiquitination via ADP-ribosylations: Legionella pneumophila SidE effector ubiquitylates serine residues in substrate via an ADP-ribosylated ubiquitin intermediate without E1 and E2 enzymes. (3) ADP-riboxanation: The type III secretion system effector of Shigella flexneri, OspC3, ADP-ribosylates the caspase and then followed by non-enzymatic deamidation.

In addition to a basic understanding of canonical ADP-ribosylation, studies of non-canonical ADP-ribosylation would benefit an understanding of deep ADP ribosylation systems. Therefore, we are calling for the community to submit original research articles or reviews on elucidating the role of ADP-ribosylation, including both canonical and non-canonical ADP-ribosylation systems. The target includes not only bacterial enzymes but also plant, insect and virus enzymes.

Prof. Dr. Hideaki Tsuge
Guest Editor

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  • canonical ADP-ribosylation
  • non-canonical ADP-ribosylation
  • ubiquitination
  • DNA ADP-ribosylation
  • ADP-riboxanation

Published Papers (1 paper)

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11 pages, 670 KiB  
Cellular Uptake and Cytotoxicity of Clostridium perfringens Iota-Toxin
by Masahiro Nagahama, Masaya Takehara, Soshi Seike and Yoshihiko Sakaguchi
Toxins 2023, 15(12), 695; - 11 Dec 2023
Cited by 1 | Viewed by 1317
Clostridium perfringens iota-toxin is composed of two separate proteins: a binding protein (Ib) that recognizes a host cell receptor and promotes the cellular uptake of a catalytic protein and (Ia) possessing ADP-ribosyltransferase activity that induces actin cytoskeleton disorganization. Ib exhibits the overall structure [...] Read more.
Clostridium perfringens iota-toxin is composed of two separate proteins: a binding protein (Ib) that recognizes a host cell receptor and promotes the cellular uptake of a catalytic protein and (Ia) possessing ADP-ribosyltransferase activity that induces actin cytoskeleton disorganization. Ib exhibits the overall structure of bacterial pore-forming toxins (PFTs). Lipolysis-stimulated lipoprotein receptor (LSR) is defined as a host cell receptor for Ib. The binding of Ib to LSR causes an oligomer formation of Ib in lipid rafts of plasma membranes, mediating the entry of Ia into the cytoplasm. Ia induces actin cytoskeleton disruption via the ADP-ribosylation of G-actin and causes cell rounding and death. The binding protein alone disrupts the cell membrane and induces cytotoxicity in sensitive cells. Host cells permeabilized by the pore formation of Ib are repaired by a Ca2+-dependent plasma repair pathway. This review shows that the cellular uptake of iota-toxin utilizes a pathway of plasma membrane repair and that Ib alone induces cytotoxicity. Full article
(This article belongs to the Special Issue ADP-Ribosylation and Beyond)
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