Special Issue "Ribosome inactivating proteins (RIPs)"

A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: closed (31 July 2019) | Viewed by 3400

Special Issue Editor

PD Dr. Alexander Weng
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Guest Editor
Institut für Pharmazie, Freie Universität Berlin

Special Issue Information

Dear Colleagues,

Ribosome-inactivating proteins (RIPs) are natural products that are synthesized by plants, as well as by microorganisms. They exhibit N-glycosidase (EC 3.2.2.22) activity and remove an essential purine base from the ribosomal RNA, thus inhibiting protein synthesis. In general, RIPs exhibit high turnover frequencies and inhibit protein synthesis in the pico- and nanomolar range. Despite their high enzymatic activity, a high number of RIPs are less toxic. This is often due to the incapability of RIPs to escape from intracellular compartments into the cytosol. However, once delivered into the cytosol of eukaryotic cells RIPs induce cell death by irreversible inactivation of protein synthesis. For this reason, RIPs are used as toxin moieties for targeted anti-tumour toxins.

The range of this Special Issue is broad, and authors are encouraged to submit their manuscripts. This Special Issue will include studies dealing with the isolation and characterization of RIPs, generating RIP-based anti-tumours agents and describing technologies that enhance the cytotoxicity of RIPs and related anti-tumor toxins.

PD Dr. Alexander Weng
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 2400 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.

Keywords

  • RIP
  • isolation
  • characterization
  • targeted toxins
  • technologies enhancing cytotoxicity

Published Papers (2 papers)

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Research

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Article
Structure and Activity of a Cytosolic Ribosome-Inactivating Protein from Rice
Toxins 2019, 11(6), 325; https://doi.org/10.3390/toxins11060325 - 06 Jun 2019
Cited by 5 | Viewed by 1611
Abstract
Ribosome-inactivating proteins (RIPs) are cytotoxic enzymes that inhibit protein translation by depurinating ribosomal RNA. Although most plant RIPs are synthesized with leader sequences that sequester them away from the host ribosomes, several RIPs from cereals lack these signal peptides and therefore probably reside [...] Read more.
Ribosome-inactivating proteins (RIPs) are cytotoxic enzymes that inhibit protein translation by depurinating ribosomal RNA. Although most plant RIPs are synthesized with leader sequences that sequester them away from the host ribosomes, several RIPs from cereals lack these signal peptides and therefore probably reside in the cytosol near the plant ribosomes. More than 30 RIP genes have been identified in the rice (Oryza sativa spp. japonica) genome, many of them lacking a signal peptide. This paper focuses on a presumed cytosolic type-1 RIP from rice, referred to as OsRIP1. Using 3D modeling it is shown that OsRIP1 structurally resembles other cereal RIPs and has an active site that meets the requirements for activity. Furthermore, localization studies indicate that OsRIP1-eGFP fusion proteins reside in the nucleocytoplasmic space when expressed in epidermal cells of Nicotiana benthamiana or Arabidopsis thaliana suspension cells. Finally, OsRIP1 was recombinantly produced in Escherichia coli and was demonstrated to possess catalytic activity. Interestingly, this recombinant RIP inactivates wheat ribosomes far less efficiently than rabbit ribosomes in an in vitro system. These findings raise some interesting questions concerning the mode of action and physiological role of OsRIP1. This is the first time a RIP from rice is investigated at protein level and is shown to possess biological activity. Full article
(This article belongs to the Special Issue Ribosome inactivating proteins (RIPs))
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Review

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Review
Dianthin and Its Potential in Targeted Tumor Therapies
Toxins 2019, 11(10), 592; https://doi.org/10.3390/toxins11100592 - 11 Oct 2019
Cited by 7 | Viewed by 1543
Abstract
Dianthin enzymes belong to ribosome-inactivating proteins (RIPs) of type 1, i.e., they only consist of a catalytic domain and do not have a cell binding moiety. Dianthin-30 is very similar to saporin-S3 and saporin-S6, two RIPs often used to design targeted toxins for [...] Read more.
Dianthin enzymes belong to ribosome-inactivating proteins (RIPs) of type 1, i.e., they only consist of a catalytic domain and do not have a cell binding moiety. Dianthin-30 is very similar to saporin-S3 and saporin-S6, two RIPs often used to design targeted toxins for tumor therapy and already tested in some clinical trials. Nevertheless, dianthin enzymes also exhibit differences to saporin with regard to structure, efficacy, toxicity, immunogenicity and production by heterologous expression. Some of the distinctions might make dianthin more suitable for targeted tumor therapies than other RIPs. The present review provides an overview of the history of dianthin discovery and illuminates its structure, function and role in targeted toxins. It further discusses the option to increase the efficacy of dianthin by endosomal escape enhancers. Full article
(This article belongs to the Special Issue Ribosome inactivating proteins (RIPs))
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