ArticleNucleic acids research2010
A switch-on mechanism to activate maize ribosome-inactivating protein for targeting HIV-infected cells.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Plant Toxic Proteins: Their Biological Activities, Mechanism of Action and Removal Strategies.Toxins · 2023Review
- Isomorphic Fluorescent Nucleosides Facilitate Real-Time Monitoring of RNA Depurination by Ribosome Inactivating Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- A Sixty-Year Research and Development of Trichosanthin, a Ribosome-Inactivating Protein.Toxins · 2022Review
- Review
- Engineering of Ribosome-inactivating Proteins for Improving Pharmacological Properties.Toxins · 2020Review
- Development of latent Interferon alpha 2b as a safe therapeutic for treatment of Hepatitis C virus infection.Scientific reports · 2019Article
- Review
- Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins.Molecules (Basel, Switzerland) · 2016Review
- Improvement of the Pharmacological Properties of Maize RIP by Cysteine-Specific PEGylation.Toxins · 2016Article
- Article
- Protein engineering: a new frontier for biological therapeutics.Current drug metabolism · 2014Review
- Inhibition of HIV-1 replication by balsamin, a ribosome inactivating protein of Momordica balsamina.PloS one · 2013Article
- Article
- Article
- The N-end rule pathway and regulation by proteolysis.Protein science : a publication of the Protein Society · 2011Review
- Engineered toxins "zymoxins" are activated by the HCV NS3 protease by removal of an inhibitory protein domain.PloS one · 2011Article
- Toxin-based therapeutic approaches.Toxins · 2010Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maize ribosome-inactivating protein (RIP) is a plant toxin that inactivates eukaryotic ribosomes by depurinating a specific adenine residue at the α-sarcin/ricin loop of 28S rRNA. Maize RIP is first produced as a proenzyme with a 25-amino acid internal inactivation region on the protein surface. During germination, proteolytic removal of this internal inactivation region generates the active heterodimeric maize RIP with full N-glycosidase activity. This naturally occurring switch-on mechanism provides an opportunity for targeting the cytotoxin to pathogen-infected cells. Here, we report the addition of HIV-1 protease recognition sequences to the internal inactivation region and the activation of the maize RIP variants by HIV-1 protease in vitro and in HIV-infected cells. Among the variants generated, two were cleaved efficiently by HIV-1 protease. The HIV-1 protease-activated variants showed enhanced N-glycosidase activity in vivo as compared to their un-activated counterparts. They also possessed potent inhibitory effect on p24 antigen production in human T cells infected by two HIV-1 strains. This switch-on strategy for activating the enzymatic activity of maize RIP in target cells provides a platform for combating pathogens with a specific protease.
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