title: New ribosome-inactivating proteins with polynucleotide:adenosine glycosidase and antiviral activities from Basella rubra L. and bougainvillea spectabilis Willd.
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) < or = 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.
authors.affiliation: Dipartimento di Patologia Sperimentale dell'Università di Bologna, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Bolognesi
authors.forename: L
authors.initials: L
authors.lastname: Polito
authors.forename: F
authors.initials: F
authors.lastname: Olivieri
authors.forename: P
authors.initials: P
authors.lastname: Valbonesi
authors.forename: L
authors.initials: L
authors.lastname: Barbieri
authors.forename: M G
authors.initials: MG
authors.lastname: Battelli
authors.forename: M V
authors.initials: MV
authors.lastname: Carusi
authors.forename: E
authors.initials: E
authors.lastname: Benvenuto
authors.forename: F
authors.initials: F
authors.lastname: Del Vecchio Blanco
authors.forename: A
authors.initials: A
authors.lastname: Di Maro
authors.forename: A
authors.initials: A
authors.lastname: Parente
authors.forename: M
authors.initials: M
authors.lastname: Di Loreto
authors.forename: F
authors.initials: F
authors.lastname: Stirpe
mesh_terms: D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D000998:Antiviral Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D004247:DNA / Q000378:metabolism; D005260:Female; D006367:HeLa Cells; D006801:Humans; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D010944:Plants / Q000201:enzymology*; D011061:Poly A / Q000378:metabolism; D011500:Protein Synthesis Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D012329:RNA, Bacterial / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D054788:Ribosome Inactivating Proteins; D012270:Ribosomes; D014407:Tumor Cells, Cultured
chemical_list: D000998:Antiviral Agents; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D012329:RNA, Bacterial; D012367:RNA, Viral; C470296:momordin I (protein); D011061:Poly A; D004247:DNA; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins