Special Issue "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 253

Special Issue 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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


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

Published Papers

This special issue is now open for submission.
Back to TopTop