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https://www.readbyqxmd.com/read/26971856/biological-and-antipathogenic-activities-of-ribosome-inactivating-proteins-from-phytolacca-dioica-l
#1
Rosario Iglesias, Lucía Citores, Sara Ragucci, Rosita Russo, Antimo Di Maro, José M Ferreras
BACKGROUND: The species from the genus Phytolacca constitute one of the best sources of ribosome-inactivating proteins (RIPs) that have been used both in the therapy against virus and tumors and in the construction of transgenic plants resistant to virus, bacteria, fungi and insects. Here we investigate new activities of three representative RIPs from Phytolacca dioica (dioicin 2, PD-S2 and PD-L4). RESULTS: The three RIPs displayed, in addition to already reported activities, rRNA N-glycosylase activities against plant, bacterial and fungal ribosomes...
June 2016: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/25976013/antifungal-activity-of-the-ribosome-inactivating-protein-be27-from-sugar-beet-beta-vulgaris%C3%A2-l-against-the-green-mould-penicillium-digitatum
#2
Lucía Citores, Rosario Iglesias, Carolina Gay, José Miguel Ferreras
The ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) leaves is an apoplastic protein induced by signalling compounds, such as hydrogen peroxide and salicylic acid, which has been reported to be involved in defence against viruses. Here, we report that, at a concentration much lower than that present in the apoplast, BE27 displays antifungal activity against the green mould Penicillium digitatum, a necrotrophic fungus that colonizes wounds and grows in the inter- and intracellular spaces of the tissues of several edible plants...
February 2016: Molecular Plant Pathology
https://www.readbyqxmd.com/read/25326773/biological-activities-of-the-antiviral-protein-be27-from-sugar-beet-beta-vulgaris-l
#3
Rosario Iglesias, Lucía Citores, Antimo Di Maro, José M Ferreras
The ribosome inactivating protein BE27 displays several biological activities in vitro that could result in a broad action against several types of pathogens. Beetin 27 (BE27), a ribosome-inactivating protein (RIP) from sugar beet (Beta vulgaris L.) leaves, is an antiviral protein induced by virus and signaling compounds such as hydrogen peroxide and salicylic acid. Its role as a defense protein has been attributed to its RNA polynucleotide:adenosine glycosidase activity. Here we tested other putative activities of BE27 that could have a defensive role against pathogens finding that BE27 displays rRNA N-glycosidase activity against yeast and Agrobacterium tumefaciens ribosomes, DNA polynucleotide:adenosine glycosidase activity against herring sperm DNA, and magnesium-dependent endonuclease activity against the supercoiled plasmid PUC19 (nicking activity)...
February 2015: Planta
https://www.readbyqxmd.com/read/24880476/sequence-comparison-and-phylogenetic-analysis-by-the-maximum-likelihood-method-of-ribosome-inactivating-proteins-from-angiosperms
#4
COMPARATIVE STUDY
Antimo Di Maro, Lucía Citores, Rosita Russo, Rosario Iglesias, José Miguel Ferreras
Ribosome-inactivating proteins (RIPs) from angiosperms are rRNA N-glycosidases that have been proposed as defence proteins against virus and fungi. They have been classified as type 1 RIPs, consisting of single-chain proteins, and type 2 RIPs, consisting of an A chain with RIP properties covalently linked to a B chain with lectin properties. In this work we have carried out a broad search of RIP sequence data banks from angiosperms in order to study their main structural characteristics and phylogenetic evolution...
August 2014: Plant Molecular Biology
https://www.readbyqxmd.com/read/24186783/isolation-and-partial-characterization-of-a-new-ribosome-inactivating-protein-from-petrocoptis-glaucifolia-lag-boiss
#5
F J Arias, M A Rojo, J M Ferreras, R Iglesias, R Muñoz, A Rocher, E Mendez, L Barbieri, T Girbés
Petrocoptis glaucifolia, a paleoendemic member of the Caryophyllaceae from the North of Spain, was found to contain at least five proteins that inhibit protein synthesis in a rabbit reticulocyte lysate. One of them, for which the name petroglaucin is proposed, was purified to apparent electrophoretic homogeneity by chromatography through S-Sepharose Fast Flow, Sephadex G-75 and CM-Sepharose Fast Flow. The apparent Mr of the preparation was 27500. This protein does not contain appreciable glycan chains and displays 45...
March 1992: Planta
https://www.readbyqxmd.com/read/23076642/in-vitro-and-in-vivo-effects-of-an-anti-mouse-endoglin-cd105-immunotoxin-on-the-early-stages-of-mouse-b16mel4a5-melanoma-tumours
#6
Raquel Muñoz, Yolanda Arias, José Miguel Ferreras, Pilar Jiménez, Carmen Langa, María Angeles Rojo, Manuel José Gayoso, Damián Córdoba-Díaz, Carmelo Bernabéu, Tomás Girbés
TGF-beta superfamily co-receptors are emerging as targets for cancer therapy, acting both directly on cells and indirectly on the tumour neovasculature. Endoglin (CD105), an accessory component of the TGF-beta receptor complex, is expressed in certain melanoma cell lines and the endothelial cells of tumour neovessels. Targeting endoglin with immunotoxins is an attractive approach for actively suppressing the blood supply to tumours. Here, we report evidence indicating that endoglin is expressed in mouse melanoma B16MEL4A5 and mouse fibroblast L929 cell lines...
March 2013: Cancer Immunology, Immunotherapy: CII
https://www.readbyqxmd.com/read/22779758/transient-injury-dependent-up-regulation-of-cd105-and-its-specific-targeting-with-an-anti-vascular-anti-mouse-endoglin-nigrin-b-immunotoxin
#7
Raquel Muñoz, Yolanda Arias, José Miguel Ferreras, Pilar Jiménez, Maria Ángeles Rojo, Carmelo Bernabéu, Damián Córdoba-Díaz, Tomás Girbés
Endoglin (CD105), a cell-surface co-receptor for transforming growth factor-beta (TGF-β) superfamily members, is over-expressed in tumor neovasculature and can be targeted with anti-endoglin antibodies, thus becoming an important tool for anti-tumoral therapy. Injury of the mouse tail induced the transient expression of endoglin, this peaking at three days after injury and disappearing six days later. An immunotoxin containing the anti-mouse endoglin rat monoclonal antibody MJ7/18 and the non-toxic ribosome-inactivating protein nigrin b (Ngb) was found to be very active in targeting mouse endoglin in the L929 fibroblast cell line (IC(50) of 4 x 10(-11) M)...
November 2012: Medicinal Chemistry
https://www.readbyqxmd.com/read/22069717/use-of-ribosome-inactivating-proteins-from-sambucus-for-the-construction-of-immunotoxins-and-conjugates-for-cancer-therapy
#8
REVIEW
José M Ferreras, Lucía Citores, Rosario Iglesias, Pilar Jiménez, Tomás Girbés
The type 2 ribosome-inactivating proteins (RIPs) isolated from some species belonging to the Sambucus genus, have the characteristic that although being even more active than ricin inhibiting protein synthesis in cell-free extracts, they lack the high toxicity of ricin and related type 2 RIPs to intact cells and animals. This is due to the fact that after internalization, they follow a different intracellular pathway that does not allow them to reach the cytosolic ribosomes. The lack of toxicity of type 2 RIPs from Sambucus make them good candidates as toxic moieties in the construction of immunotoxins and conjugates directed against specific targets...
May 2011: Toxins
https://www.readbyqxmd.com/read/19799962/sialic-acid-binding-dwarf-elder-four-chain-lectin-displays-nucleic-acid-n-glycosidase-activity
#9
Rosario Iglesias, Lucía Citores, J Miguel Ferreras, Yolanda Pérez, Pilar Jiménez, Manuel J Gayoso, Sjur Olsnes, Rachele Tamburino, Antimo Di Maro, Augusto Parente, Tomás Girbés
Sialic acid-binding dwarf elder agglutinin (SEA) present only in rhizomes of the medicinal plant Sambucus ebulus L., was found to be a tetrameric glycoprotein consisting of two covalently-associated dimers of an enzymic A chain with rRNA N-glycosidase activity (EC 3.2.2.22) linked to a B chain with agglutinin properties. The lectin inhibited protein synthesis by a cell-free system and depurinated ribosomes. Cloning of the corresponding gene and molecular modeling of the deduced amino acid sequence demonstrated that SEA has a three-dimensional structure which resembles that reported for other two tetrameric type 2 RIPs from Sambucus (SNAI and SSA)...
January 2010: Biochimie
https://www.readbyqxmd.com/read/18343888/elicitor-dependent-expression-of-the-ribosome-inactivating-protein-beetin-is-developmentally-regulated
#10
Rosario Iglesias, Yolanda Pérez, Lucía Citores, José M Ferreras, Enrique Méndez, Tomás Girbés
BE27 and BE29 are two forms of beetin, a virus-inducible type 1 ribosome-inactivating protein isolated from leaves of Beta vulgaris L. Western blot analysis revealed the presence of beetin forms in adult plants but not in germ or young plants, indicating that the expression of these proteins is developmentally regulated. While beetins are expressed only in adult plants, their transcripts are present through all stages of development. In addition, the treatment of B. vulgaris leaves with mediators of plant-acquired resistance such as salicylic acid and hydrogen peroxide promoted the expression of beetin by induction of its transcript, but only in adult plants...
2008: Journal of Experimental Botany
https://www.readbyqxmd.com/read/18068741/transient-occurrence-of-an-ebulin-related-d-galactose-lectin-in-shoots-of-sambucus-ebulus-l
#11
Lucía Citores, María A Rojo, Pilar Jiménez, José M Ferreras, Rosario Iglesias, Isabel Aranguez, Tomás Girbés
Young shoots of Sambucus ebulus L. contain a monomeric d-galactose binding lectin (SELlm), which disappears upon shoot development, and was previously undetected since it co-purifies with the non-toxic type 2 ribosome-inactivating protein ebulin l and the dimeric lectin SELld. Molecular cloning of cDNA coding for SELlm and mass spectrometry analysis revealed a protein with a molecular mass of 34,239 Da, which displays 80%, 77% and 45% of amino acid sequence identity with the ebulin l-B chain, SELld and ricin-B chain, respectively...
February 2008: Phytochemistry
https://www.readbyqxmd.com/read/17637501/targeting-a-marker-of-the-tumour-neovasculature-using-a-novel-anti-human-cd105-immunotoxin-containing-the-non-toxic-type-2-ribosome-inactivating-protein-nigrin-b
#12
Raquel Muñoz, Yolanda Arias, José M Ferreras, María A Rojo, Manuel J Gayoso, Mercedes Nocito, Jorge Benitez, Pilar Jiménez, Carmelo Bernabéu, Tomas Girbés
Targeting tumour neovasculature using antibodies to the endothelial receptor CD105 (endoglin), is a potentially useful approach for anti-tumour therapy. We report on the preparation and the cytotoxicity of a novel immunotoxin consisting in the non-toxic type 2 ribosome-inactivating protein (RIP) nigrin b linked to the monoclonal anti-human CD105 (hCD105) antibody 44G4. The immunotoxin kills specifically mouse fibroblasts expressing the biomarker CD105 (L929-hCD105+ cells) with an IC(50) value of 6x10(-10)M while nigrin b does it at 2...
October 18, 2007: Cancer Letters
https://www.readbyqxmd.com/read/16789887/cytotoxicity-of-an-ebulin-l-anti-human-cd105-immunotoxin-on-mouse-fibroblasts-l929-and-rat-myoblasts-l6e9-cells-expressing-human-cd105
#13
Jorge Benítez, J Miguel Ferreras, Raquel Muñoz, Yolanda Arias, Rosario Iglesias, Manuel Córdoba-Díaz, Rosario del Villar, Tomás Girbés
Tumour growth is characterised by the formation of a fine vessel network or neovasculature which nourishes tumour cells. Two kinds of novel anti-angiogenic therapies are based on the prevention of vessels growth and on the destruction of those vessels already formed. We report here on the design and construction of a novel immunotoxin formed with the non-toxic type II ribosome-inactivating protein ebulin l and the mouse anti-human CD105 monoclonal antibody 44G4. The 44G4-ebulin immunotoxin was formed by covalent linking of both proteins with N-succinimidyl-3-(2-pyridyldithio)propionate (SPDP) and was purified by chromatography on Superdex 200 HiLoad...
January 2005: Medicinal Chemistry
https://www.readbyqxmd.com/read/16102565/specific-dose-dependent-damage-of-lieberk%C3%A3-hn-crypts-promoted-by-large-doses-of-type-2-ribosome-inactivating-protein-nigrin-b-intravenous-injection-to-mice
#14
M J Gayoso, R Muñoz, Y Arias, R Villar, M A Rojo, P Jiménez, J M Ferreras, I Aranguez, T Girbés
Nigrin b is a non-toxic type 2 ribosome-inactivating protein as active as ricin at ribosomal level but 10(5) and 5 x 10(3) times less toxic for animal cell cultures and mice, respectively, than ricin. The purpose of the present study was to analyze the effects of intravenous injection of large amounts of nigrin b to the mouse. Injection through the tail vein of 16 mg/kg body weight killed all mice studied before 2 days. Analysis of several major tissues by light microscopy did not reveal gross nigrin b-promoted changes, except in the intestines which appeared highly damaged...
September 1, 2005: Toxicology and Applied Pharmacology
https://www.readbyqxmd.com/read/15863448/molecular-characterization-and-systemic-induction-of-single-chain-ribosome-inactivating-proteins-rips-in-sugar-beet-beta-vulgaris-leaves
#15
Rosario Iglesias, Yolanda Pérez, Carlos de Torre, J Miguel Ferreras, Pilar Antolín, Pilar Jiménez, M Angeles Rojo, Enrique Méndez, Tomás Girbés
Sugar beet (Beta vulgaris L.) leaves contain virus-inducible type 1 (single chain) ribosome-inactivating proteins that have been named beetins. The structural and functional characterization, the cellular location, and the potential role of beetins as antiviral agents are reported here. Beetins are formed of a single polypeptide chain with a varying degree of glycosylation and strongly inhibited in vitro protein synthesis in rabbit reticulocyte lysates (IC50=1.15 ng ml(-1)) and a Vicia sativa L. cell-free system (IC50=68 ng ml(-1)) through the single depurination of the large rRNA...
June 2005: Journal of Experimental Botany
https://www.readbyqxmd.com/read/15180503/description-distribution-activity-and-phylogenetic-relationship-of-ribosome-inactivating-proteins-in-plants-fungi-and-bacteria
#16
REVIEW
Tomas Girbés, José Miguel Ferreras, Francisco Javier Arias, Fiorenzo Stirpe
Ribosome-Inactivating Proteins (RIPs) are enzymes that trigger the catalytic inactivation of ribosomes and other substrates. They are present in a large number of plants and have been found also in fungi, algae and bacteria. RIPs are currently classified as type 1, those formed by a single polypeptide chain with the enzymatic activity, and type 2, those formed by 2 types of chains, i.e. A chains equivalent to a type 1 RIPs and B chains with lectin activity. Type 2 RIPs usually contain the formulae A-B, (A-B)2 and less frequent (A-B)4 and polymeric forms of type 2 RIPs lectins...
June 2004: Mini Reviews in Medicinal Chemistry
https://www.readbyqxmd.com/read/14995076/evidence-for-distinct-cellular-internalization-pathways-of-ricin-and-nigrin-b
#17
L Citores, R Muñoz, M A Rojo, P Jiménez, J M Ferreras, T Girbés
Nigrin b and ricin are type 2 (two chain) ribosome-inactivating proteins that exhibited nearly the same strong inhibitory activity on cell-free protein synthesis. Incubation of HeLa cells for 6 hr with ricin at 37 degrees C promoted protein synthesis inhibition with an IC50 of 0.2 ng/ml. Incubation of the cells for 6 hr at 18 degrees C abolished completely the inhibition. Incubation of HeLa cells with nigrin b for 6 hr at 37 degrees C was nearly 10(5) times less inhibitory than ricin. In contrast to the effects observed with ricin, incubation of HeLa cells with nigrin b at 18 degrees C slightly increased the inhibitory action on protein synthesis as compared with incubation at 37 degrees C...
2003: Cellular and Molecular Biology
https://www.readbyqxmd.com/read/12899446/non-toxic-type-2-ribosome-inactivating-proteins-rips-from-sambucus-occurrence-cellular-and-molecular-activities-and-potential-uses
#18
REVIEW
T Girbes, J M Ferreras, F J Arias, R Muñoz, R Iglesias, P Jimenez, M A Rojo, Y Arias, Y Perez, J Benitez, D Sanchez, M J Gayoso
Ribosome-inactivating proteins (RIPs) are a family of enzymes that trigger the catalytic inactivation of ribosomes. The most known member of the family is the highly poisonous two-chain ricin isolated from Ricinus communis L. Sambucus species contain a number of two-chain RIPs structurally and enzymatically related to ricin which have the noteworthy feature that, having an enzymatic activity on ribosomes, leading to the inhibition of protein synthesis, higher than ricin, they are lacking of the tremendous unspecific toxicity of ricin...
June 2003: Cellular and Molecular Biology
https://www.readbyqxmd.com/read/12871149/isolation-and-characterization-of-a-new-d-galactose-binding-lectin-from-sambucus-racemosa-l
#19
COMPARATIVE STUDY
M Angeles Rojo, Lucía Citores, Pilar Jiménez, J Miguel Ferreras, F Javier Arias, Enrique Méndez, Tomás Girbés
A new acidic lectin from red elder (Sambucus racemosa L.) bark has been isolated by affinity chromatography and gel filtration. Noteworthy, and in contrast to other Sambucus species, red elder bark lacks acidic non-toxic type 2 ribosome-inactivating proteins but has basic ribosome-inactivating protein activities. The new lectin (SRLbm) shows specificity for N-Ac-Galactosamine/D-Galactose and has an apparent Mr of 30,000. The N-terminal amino acid sequence displays a close homology with other lectins and B chains of non-toxic type 2 ribosome-inactivating proteins nigrins and ebulins present in other Sambucus species...
June 2003: Protein and Peptide Letters
https://www.readbyqxmd.com/read/12672476/cdna-molecular-cloning-and-seasonal-accumulation-of-an-ebulin-l-related-dimeric-lectin-of-dwarf-elder-sambucus-ebulus-l-leaves
#20
COMPARATIVE STUDY
M Angeles Rojo, Lucía Citores, F Javier Arias, J Miguel Ferreras, Pilar Jimenez, Tomás Girbés
SELld is a dimeric D-galactose and mucin-binding lectin (apparent Mr 68000) which coexists with the non-toxic type 2 ribosome-inactivating protein (RIP) ebulin l in dwarf elder (Sambucus ebulus L.) leaves. To ascertain a potential structural correlation with ebulin l molecular cloning of a cDNA coding for SELld was performed. SELld shared a 76% of identity with the ebulin l-B chain. Notably, it was found that SELld has Tyr present in the high affinity 2gamma sugar-binding domain of ricin which is absent in ebulin l-B chain and which seems responsible of the low cell and in vivo toxicities of ebulin l...
July 2003: International Journal of Biochemistry & Cell Biology
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