title: Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection.
abstract: The rRNA depurination activities of five ribosome-inactivating proteins (RIPs) were compared in vitro using yeast and tobacco leaf ribosomes as substrates. All of the RIPs (pokeweed antiviral protein (PAP), dianthin 32, tritin, barley RIP and ricin A-chain) were active on yeast ribosomes. PAP and dianthin 32 were highly active and ricin A-chain weakly active on tobacco ribosomes, whereas tritin and barley RIP were inactive. PAP and dianthin 32 were highly effective in inhibiting the formation of local lesions caused by tobacco mosaic virus (TMV) on tobacco leaves, whereas tritin, barley RIP and ricin A-chain were ineffective. The apparent anomaly between the in vitro rRNA depurination activity, but lack of antiviral activity of ricin A-chain was further investigated by assaying for rRNA depurination in situ following the topical application of the RIP to leaves. No activity was detected, a finding consistent with the apparent lack of antiviral activity of this RIP. Thus, it is concluded that there is a positive correlation between RIP-catalysed depurination of tobacco ribosomes and antiviral activity which gives strong support to the hypothesis that the antiviral activity of RIPs works through ribosome inactivation.
authors.affiliation: Department of Biological Sciences, University of Warwick, UK.
authors.forename: S
authors.initials: S
authors.lastname: Taylor
authors.forename: A
authors.initials: A
authors.lastname: Massiah
authors.forename: G
authors.initials: G
authors.lastname: Lomonossoff
authors.forename: L M
authors.initials: LM
authors.lastname: Roberts
authors.forename: J M
authors.initials: JM
authors.lastname: Lord
authors.forename: M
authors.initials: M
authors.lastname: Hartley
mesh_terms: D000814:Aniline Compounds; D000998:Antiviral Agents / Q000494:pharmacology; D001483:Base Sequence; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases; D037121:Plant Lectins; D010940:Plant Proteins / Q000494:pharmacology*; D010947:Plants, Toxic; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D011687:Purines / Q000737:chemistry; D012335:RNA, Ribosomal / Q000737:chemistry / Q000187:drug effects*; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000187:drug effects*; D012276:Ricin / Q000737:chemistry / Q000494:pharmacology; D014026:Nicotiana / Q000378:metabolism*; D014027:Tobacco Mosaic Virus / Q000187:drug effects* / Q000502:physiology; D015003:Yeasts / Q000378:metabolism
chemical_list: D000814:Aniline Compounds; D000998:Antiviral Agents; D037121:Plant Lectins; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D011687:Purines; D012335:RNA, Ribosomal; D054789:Ribosome Inactivating Proteins, Type 1; C031676:tritin protein, Triticum aestivum; D012276:Ricin; D009699:N-Glycosyl Hydrolases; C024275:pokeweed antiviral protein; C023650:aniline