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New Perspectives and Uses of Ribosome-Inactivating Toxins and Related Lectins of Plant Origin

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

Deadline for manuscript submissions: closed (30 June 2021) | Viewed by 2797

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Special Issue Editors

Special Issue Information

Dear Colleagues,

Plant ribosome-inactivating proteins (RIPs) belong to well-characterized EC 3.2.2.22 N glycosidases toxins, which irreversibly and specifically depurinate a single adenosine in the a-SRL of rRNA in eukaryotic cells. Apoptosis of affected cells has been also related to DNA damage. RIP-based drugs, immunotoxins, chimeric fusions, use of nucleic acids encoding the toxin domain (suicide gene therapy), engineered micro–nanoparticles, dendrimers, or targeted exosomes have been not only used against hematological and solid tumors but also as antiviral diseases, such as AIDS.

This Special Issue will cover all these strategies but focusing on the use of nanotechnology as a powerful strategy to increase the tumor penetration capability of RIPs as therapeutic agents or increase effectiveness of antiviral formulations.

Prof. Damian Cordoba-Diaz
Prof. Tomas Girbes
Guest Editors

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.

Keywords

nanoparticles
exosomes
vectorization
controlled release
RIPs
antiviral
cancer

Published Papers (1 paper)

Research

15 pages, 2397 KiB

Open AccessArticle

Ribosome-Inactivating Proteins of Bougainvillea glabra Uncovered Polymorphism and Active Site Divergence

by Yihua Lin, Liting Xu, Yanyan Li, Xiaobin Wu, Yijun Liu, Hongmei Zhu and Hantao Zhou

Toxins 2021, 13(5), 331; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13050331 - 04 May 2021

Cited by 2 | Viewed by 2372

Abstract

Ribosome-inactivating proteins (RIPs) are toxic proteins that can inhibit protein synthesis. RIPs purified from Bougainvillea have low nonspecific toxicity, showing promise for processing applications in the agricultural and medical fields. However, systematic research on the polymorphism of Bougainvillea RIPs is lacking, and it is worth exploring whether different isoforms differ in their active characteristics. The transcriptional and translational expression of type I RIPs in Bougainvillea glabra leaves was investigated in this study. Seven RIPs exhibited seasonal variation at both the mRNA and protein levels. The isoforms BI4 and BI6 showed the highest transcriptional expression in both the summer and autumn samples. Interestingly, BI6 was not detected in the protein level in any of the samples. However, the bioinformatics analysis showed that RIPs derived from the same species were gathered in a different cluster, and that the active sites changed among the isoforms during evolution. The significant discrepancy in Bougainvillea RIPs mainly locates at both termini of the amino acid sequence, particularly at the C terminus. Post-translational modifications may also exist in Bougainvillea RIPs. It is concluded that the reason for the polymorphism of Bougainvillea RIPs may be that these proteins are encoded by multiple genes due to genetic processes such as gene duplication and mutation. According to the results of sequence analysis, the possible functional differences of B. glabra RIP isoforms are discussed with regard to the observed discrepancy in both active sites and structures. Full article

(This article belongs to the Special Issue New Perspectives and Uses of Ribosome-Inactivating Toxins and Related Lectins of Plant Origin)

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