New ribosome-inactivating proteins with polynucleotide:adenosine glycosidase and antiviral activities from Basella rubra L. and Bougainvillea spectabilis Willd. |
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Authors: | Andrea Bolognesi Letizia Polito Fabiola Olivieri Paola Valbonesi Luigi Barbieri M. Giulia Battelli M. Vittoria Carusi Eugenio Benvenuto Francesca Del Vecchio Blanco Antimo Di Maro Augusto Parente Mario Di Loreto Fiorenzo Stirpe |
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Affiliation: | (1) Dipartimento di Patologia Sperimentale dell'Università di Bologna, Via S. Giacomo 14, I-40126 Bologna, Italy, IT;(2) ENEA, Dipartimento Innovazione, Settore Biotecnologie e Agricoltura, Via Anguillarese 301, I-00060 S. Maria di Galeria RM, Italy, AI;(3) Dipartimento di Chimica Organica e Biologica, Università Federico II, Via Mezzocannone 16, I-80134 Napoli, Italy, IT;(4) Instituto di Biologia, II Università di Napoli, Via Arena 18, I-81100 Caserta, Italy, IT;(5) Dipartimento di Biotecnologie, Menarini Ricerche Sud, Via Tito Speri 10, I-00040 Pomezia RM, Italy, IT |
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Abstract: | New single-chain (type 1) ribosome-inactivating proteins (RIPs) were isolated from the seeds of Basella rubra L. (two proteins) and from the leaves of Bougainvillea spectabilis Willd. (one protein). These RIPs inhibit protein synthesis both in a cell-free system, with an IC50 (concentration causing 50% inhibition) in the 10−10 M range, and by various cell lines, with IC50s in the 10−8–10−6 M range. All three RIPs released adenine not only from rat liver ribosomes but also from Escherichia coli rRNA, polyadenylic acid, herring sperm DNA, and artichoke mottled crinkle virus (AMCV) genomic RNA, thus being polynucleotide:adenosine glycosidases. The proteins from Basella rubra had toxicity to mice similar to that of most type 1 RIPs (Barbieri et al., 1993, Biochim Biophys Acta 1154: 237–282) with an LD50 (concentration that is 50% lethal) ≤ 8 mg · kg−1 body weight, whilst the RIP from Bougainvillea spectabilis had an LD50 >32 mg · kg−1. The N-terminal sequence of the two RIPs from Basella rubra had 80–93% identity, whereas it differed from the sequence of the RIP from Bougainvillea spectabilis. When tested with antibodies against various RIPs, the RIPs from Basella gave some cross-reactivity with sera against dianthin 32, and weak cross-reactivity with momordin I and momorcochin-S, whilst the RIP from Bougainvillea did not cross-react with any antiserum tested. An RIP from Basella rubra and one from Bougainvillea spectabilis were tested for antiviral activity, and both inhibited infection of Nicotiana benthamiana by AMCV. Received: 5 March 1997 / Accepted: 27 May 1997 |
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Keywords: | : Antiviral protein Basella Bougainvillea Polynucleotide:adenosine glycosidase Ribosome-inactivating protein |
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