Type I Ribosome-Inactivating Proteins from Saponaria officinalis

2010 ◽  
pp. 55-78 ◽  
Author(s):  
Alessio Lombardi ◽  
Richard S. Marshall ◽  
Carmelinda Savino ◽  
Maria Serena Fabbrini ◽  
Aldo Ceriotti
Keyword(s):  
Type I ◽  
Ribosome Inactivating Proteins ◽  
Saponaria Officinalis

scholarly journals The differential catalytic activity of ribosome-inactivating proteins saporin 5 and 6 is due to a single substitution at position 162

2006 ◽  
Vol 400 (1) ◽  
pp. 99-104 ◽  
Author(s):  
Paroma Ghosh ◽  
Janendra K. Batra
Keyword(s):  
Catalytic Activity ◽  
Amino Acid ◽  
Active Sites ◽  
Functional Characterization ◽  
Cytotoxic Activities ◽  
Type I ◽  
Ribosome Inactivating Protein ◽  
Aspartic Acid Residue ◽  
Ribosome Inactivating Proteins ◽  
Saponaria Officinalis

Saporin, a type I ribosome-inactivating protein produced by the soapwort plant Saponaria officinalis belongs to a multigene family that encodes its several isoforms. The saporin seed isoform 6 has significantly higher N-glycosidase and cytotoxic activities compared with the seed isoform 5, although the two have identical active sites. In the present study, we have investigated the contribution of non-conservative amino acid changes outside the active sites of these isoforms towards their differential catalytic activity. The saporin 6 residues Lys134, Leu147, Phe149, Asn162, Thr188 and Asp196 were replaced by the corresponding saporin 5 residues, Gln134, Ser147, Ser149, Asp162, Ile188 and Asn196, to generate six variants of saporin 6, K134Q, L147S, F149S, N162D, T188I and D196N. By functional characterization, we show that the change in amino acid Asn162 in saporin 6 to aspartic acid residue of saporin 5 contributes mainly to the lower catalytic activity of saporin 5 compared with saporin 6. The non-involvement of other non-conservative amino acids in the differential catalytic activity of these isoforms was confirmed with the help of the double mutations N162D/K134Q, N162D/L147S, N162D/F149S, N162D/T188I and N162D/D196N.

Studies on Ribosome-inactivating Proteins from Saponaria officinalis

2020 ◽  
pp. 193-212
Author(s):  
Marco R. Soria ◽  
Luca Benatti ◽  
Gianpaolo Nitti ◽  
Aldo Ceriotti ◽  
Michela Solinas ◽  
...  
Keyword(s):  
Ribosome Inactivating Proteins ◽  
Saponaria Officinalis

scholarly journals Polynucleotide: adenosine glycosidase activity of saporin-L1: effect on DNA, RNA and poly(A)

1996 ◽  
Vol 319 (2) ◽  
pp. 507-513 ◽  
Author(s):  
Luigi BARBIERI ◽  
Paola VALBONESI ◽  
Paola GORINI ◽  
Annalisa PESSION ◽  
Fiorenzo STIRPE
Keyword(s):  
Ionic Strength ◽  
Kinetic Parameters ◽  
Plant Protein ◽  
Ribosome Inactivating Proteins ◽  
Glycosidase Activity ◽  
Plant Enzymes ◽  
Low Ionic Strength ◽  
Different Sources ◽  
Saponaria Officinalis ◽  
Optimal Ph

The ribosome-inactivating proteins (RIPs) are a family of plant enzymes for which a unique activity has been determined: rRNA N-glycosidase, which removes adenine at a specific universally conserved position (A4324 in the case of rat ribosomes). Here we report that saporin-L1, a RIP from the leaves of Saponaria officinalis, recognizes other substrates, including RNAs from different sources, DNA and poly(A). Saporin-L1 depurinated DNA extensively and released adenine from all adenine-containing polynucleotides tested. Adenine was the only base released from DNA or artificial polynucleotides. The characteristics of the reactions catalysed by saporin-L1 have been determined: optimal pH and temperature, ionic requirements, and the kinetic parameters Km and kcat. The reaction proceeded without cofactors, at low ionic strength, in the absence of Mg2+ and K+. Saporin-L1 had no activity towards various adenine-containing non-polynucleotide compounds (cytokinins, cofactors, nucleotides). This plant protein may now be classified as a polynucleotide:adenosine glycosidase.

Cellular and subcellular distribution of saporins, type-1 ribosome-inactivating proteins, in soapwort (Saponaria officinalis L.)

Planta ◽  
1994 ◽  
Vol 194 (4) ◽  
pp. 461-470 ◽  
Author(s):  
Raffaella Carzaniga ◽  
Lesley Sinclair ◽  
Anthony P. Fordham-Skelton ◽  
Nick Harris ◽  
Ronald R. D. Croy
Keyword(s):  
Subcellular Distribution ◽  
Ribosome Inactivating Proteins ◽  
Saponaria Officinalis

scholarly journals Photochemical Internalization for Intracellular Drug Delivery. From Basic Mechanisms to Clinical Research

2020 ◽  
Vol 9 (2) ◽  
pp. 528 ◽  
Author(s):  
Waseem Jerjes ◽  
Theodossis A. Theodossiou ◽  
Henry Hirschberg ◽  
Anders Høgset ◽  
Anette Weyergang ◽  
...  
Keyword(s):  
Clinical Trial ◽  
Type I ◽  
Light Activation ◽  
Gene Encoding ◽  
Cytoplasmic Matrix ◽  
Cancer Vaccination ◽  
Ribosome Inactivating Proteins ◽  
Intracellular Drug Delivery ◽  
Photochemical Internalization ◽  
Endocytic Vesicles

Photochemical internalisation (PCI) is a unique intervention which involves the release of endocytosed macromolecules into the cytoplasmic matrix. PCI is based on the use of photosensitizers placed in endocytic vesicles that, following light activation, lead to rupture of the endocytic vesicles and the release of the macromolecules into the cytoplasmic matrix. This technology has been shown to improve the biological activity of a number of macromolecules that do not readily penetrate the plasma membrane, including type I ribosome-inactivating proteins (RIPs), gene-encoding plasmids, adenovirus and oligonucleotides and certain chemotherapeutics, such as bleomycin. This new intervention has also been found appealing for intracellular delivery of drugs incorporated into nanocarriers and for cancer vaccination. PCI is currently being evaluated in clinical trials. Data from the first-in-human phase I clinical trial as well as an update on the development of the PCI technology towards clinical practice is presented here.

scholarly journals The Streptomyces coelicolor genome encodes a type I ribosome-inactivating protein

Microbiology ◽  
2010 ◽  
Vol 156 (10) ◽  
pp. 3021-3030 ◽  
Author(s):  
Ana G. Reyes ◽  
Nick Geukens ◽  
Philip Gutschoven ◽  
Stijn De Graeve ◽  
René De Mot ◽  
...  
Keyword(s):  
Shiga Toxin ◽  
Streptomyces Coelicolor ◽  
Protein Translation ◽  
Type I ◽  
Free System ◽  
Ribosome Inactivating Proteins ◽  
E Coli ◽  
Genes Encoding ◽  
A Cell ◽  
A Subunit

Ribosome-inactivating proteins (RIPs) are cytotoxic N-glycosidases identified in numerous plants, but also constitute a subunit of the bacterial Shiga toxin. Classification of plant RIPs is based on the absence (type I) or presence (type II) of an additional lectin module. In Shiga toxin, sugar binding is mediated by a distinct RIP-associated homopentamer. In the genome of two actinomycetes, we identified RIP-like proteins that resemble plant type I RIPs rather than the RIP subunit (StxA) of Shiga toxin. Some representatives of β- and γ-proteobacteria also contain genes encoding RIP-like proteins, but these are homologous to StxA. Here, we describe the isolation and initial characterization of the RIP-like gene product SCO7092 (RIPsc) from the Gram-positive soil bacterium Streptomyces coelicolor. The ripsc gene was expressed in Escherichia coli as a recombinant protein of about 30 kDa, and displayed the characteristic N-glycosidase activity causing specific rRNA depurination. In Streptomyces lividans and E. coli, RIPsc overproduction resulted in a dramatic decrease in the growth rate. In addition, intracellular production was deleterious for Saccharomyces cerevisiae. However, when applied externally to microbial cells, purified RIPsc did not display antibacterial or antifungal activity, suggesting that it cannot enter these cells. In a cell-free system, however, purified S. coelicolor RIPsc protein displayed strong inhibitory activity towards protein translation.

Environmental factors and phytohormones enhancing expression of α-momorcharin gene in Momordica charantia

Biologia ◽  
2016 ◽  
Vol 71 (2) ◽  
Author(s):  
Shuzhen Wang ◽  
Hongyuan Zhang ◽  
Yinzhen Zheng ◽  
Zhiliang Li ◽  
Fu Xiang ◽  
...  
Keyword(s):  
Environmental Factors ◽  
Host Defense ◽  
Stress Resistance ◽  
Defense Mechanisms ◽  
Plant Stress ◽  
Momordica Charantia ◽  
Type I ◽  
Ribosome Inactivating Proteins ◽  
Typical Type

AbstractRibosome-inactivating proteins (RIPs), a type of defensive chemicals, play key roles in host defense mechanisms against foreign pathogenic invaders and plant stress resistance. Alpha-momorcharin, a member of typical type I RIPs isolated from

scholarly journals Ribosome-inactivating proteins from the seeds of Saponaria officinalis L. (soapwort), of Agrostemma githago L. (corn cockle) and of Asparagus officinalis L. (asparagus), and from the latex of Hura crepitans L. (sandbox tree)

1983 ◽  
Vol 216 (3) ◽  
pp. 617-625 ◽  
Author(s):  
F Stirpe ◽  
A Gasperi-Campani ◽  
L Barbieri ◽  
A Falasca ◽  
A Abbondanza ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Sugar Content ◽  
Asparagus Officinalis ◽  
Inhibit Protein Synthesis ◽  
Nicotiana Glutinosa ◽  
Ribosome Inactivating Proteins ◽  
Local Lesions ◽  
Hura Crepitans ◽  
Reticulocyte Lysate ◽  
Saponaria Officinalis

Ribosome-inactivating proteins, similar to those already known [Barbieri & Stirpe (1982) Cancer Surveys 1, 489-520] were purified from the seeds of Saponaria officinalis (two proteins), of Agrostemma githago (three proteins), and of Asparagus officinalis (three proteins), and from the latex of Hura crepitans (one protein). The yield ranged from 8 to 400 mg/100 g of starting material. All proteins have an Mr of approx. 30000 and an alkaline isoelectric point. Their sugar content varies from 0 (proteins from S. officinalis) to 40% (protein from H. crepitans). The ribosome-inactivating proteins inhibit protein synthesis by rabbit reticulocyte lysate, the ID50 (concentration giving 50% inhibition) ranging from 1 ng/ml (a protein from S. officinalis) to 18 ng/ml (a protein from A. githago). Those which were tested (the proteins from S. officinalis and from A. githago) also inhibit polymerization of phenylalanine by isolated ribosomes, acting in an apparently catalytic manner. The protein from H. crepitans inhibited protein synthesis by HeLa cells, with an ID50 of 4 micrograms/ml, whereas the proteins from S. officinalis and from A. githago had an ID50 of more than 50-100 micrograms/ml. The ribosome-inactivating proteins from S. officinalis and from A. githago reduced the number of local lesions by tobacco-mosaic virus in the leaves of Nicotiana glutinosa.

Ribosome-Inactivating Proteins from Saponaria Officinalis: Tools in the Design of Immunotoxins and Ligand Toxins

1992 ◽  
pp. 19-29 ◽  
Author(s):  
Marco R. Soria ◽  
Luca Benatti ◽  
Aldo Ceriotti ◽  
A. Vitale ◽  
Douglas A. Lappi
Keyword(s):  
Ribosome Inactivating Proteins ◽  
Saponaria Officinalis
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