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New ribosome-inactivating proteins with polynucleotide:adenosine glycosidase and antiviral activities from Basella rubra L. and Bougainvillea spectabilis Willd

TitleNew ribosome-inactivating proteins with polynucleotide:adenosine glycosidase and antiviral activities from Basella rubra L. and Bougainvillea spectabilis Willd
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication1997
AuthorsBolognesi, A., Polito L., Olivieri F., Valbonesi P., Barbieri L., M. Bartelli Giulia, M. Carusi Vittoria, Benvenuto Eugenio, F. Blanco Del Vecchio, Di Maro A., Parente A., Di Loreto M., and Stirpe F.
Pagination422 - 429
Date Published1997
ISBN Number00320935 (ISSN)
Keywords3T3 Cells, Amino Acid Sequence, animal, Animals, Antiviral Agents, Antiviral protein, antivirus agent, article, Bacterial, bacterial RNA, Basella, Bougainvillea, cell culture, cell strain 3T3, chemistry, Cultured, DNA, enzymology, Female, glycosidase, HeLa cell, Hela Cells, human, Humans, isolation and purification, male, metabolism, Mice, molecular genetics, Molecular Sequence Data, momordin I (protein), mouse, N-Glycosyl Hydrolases, Plant, Plant Proteins, Plants, Poly A, polyadenylic acid, Polynucleotide:adenosine glycosidase, protein synthesis inhibitor, Protein Synthesis Inhibitors, rabbit, Rabbits, rat, Rats, ribosome, Ribosome-inactivating protein, Ribosomes, RNA, RNA N glycosidase, RNA N-glycosidase, Tumor Cells, vegetable protein, Viral, virus RNA

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 I 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.


Cited By :46Export Date: 16 July 2015CODEN: PLANACorrespondence Address: Stirpe, F.; Dipartimento di Patologia, Sperimentale dell’Univ. di Bologna, Via S. Giacomo 14, I-40126 Bologna, Italy; email: stirpef@alma.unibo.itChemicals/CAS: Antiviral Agents; DNA, 9007-49-2; momordin I (protein); N-Glycosyl Hydrolases, EC 3.2.2.-; Plant Proteins; Poly A, 24937-83-5; Protein Synthesis Inhibitors; RNA N-glycosidase, EC; RNA, Bacterial; RNA, ViralReferences: Anas, F.J., Rojo, M.A., Ferreras, J.M., Iglesias, R., Muǹoz, R., Rocher, A., Méndez, E., Girbés, T., Isolation and partial characterization of a new ribosome-inactivating protein from Petrocoptis glancifolia (Lag.) 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