Pokeweed antiviral protein: Ribosome inactivation and therapeutic applications

https://doi.org/10.1016/0163-7258(92)90053-3Get rights and content

Abstract

Pokeweed antiviral protein (PAP) is a ribosome-inactivating protein (RIP) that inactivates ribosomes by the removal of a single adenine from ribosomal RNA. The studies summarized in our review concern the nature and application of this novel therapeutic agent. We describe how researchers continue to elucidate the structure and biologic activity of RIPs. Pokeweed antiviral protein is among the RIPs that have been conjugated to selective monoclonal antibodies for the treatment of several human cancers and viral diseases. Clinical trials using PAP immunotoxins for the treatment of leukemia have been particularly encouraging.

References (130)

  • Y. Endo et al.

    RNA N-glycosidase acitvity of ricin A-chain: mechanism of action of the toxic lectin ricin on eukaryotic ribosomes

    J. biol. Chem.

    (1987)
  • Y. Endo et al.

    The RNA N-glycosidase activity of ricin A-chain: the characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA

    J. biol. Chem.

    (1988)
  • Y. Endo et al.

    The site of action of α-sarcin on eukaryotic ribosomes: the sequence at the α-sarcin cleavage site in 28S ribosomal ribonucleic acid

    J. Biol. Chem.

    (1982)
  • Y. Endo et al.

    The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes: the site and the characteristics of the modification in 28S ribosomal RNA caused by the toxins

    J. biol. Chem.

    (1987)
  • Y. Endo et al.

    The cytotoxins α-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28S ribosomal ribonucleic acid

    J. biol. Chem.

    (1988)
  • Y. Endo et al.

    The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes: the RNA N-Prmglycosidase activity of the proteins

    Biochem. biophys. Res. Commun.

    (1988)
  • Y. Endo et al.

    Ribosomal RNA identity elements for ricin A-chain recognitiion and catalysis

    J. molec. Biol.

    (1991)
  • G. Funatsu et al.

    Conserved amino acid residues in ribosome-inactivating proteins from plants

    Biochimie

    (1991)
  • N. Habuka et al.

    Expression and secretion of Mirabilis antiviral protein in Escherichia coli and its inhibition of in vitro eukaryotic and prokaryotic protein synthesis

    J. biol. Chem.

    (1990)
  • N. habuka et al.

    Substantial increase of the inhibitory activity of Mirabilis antiviral protein by an elimination of the disulfide bond with genetic engineering

    J. biol. Chem.

    (1991)
  • M.R. Hartley et al.

    Single-chain ribosome inactivating proteins from plants depurinate Escherichia coli 23S ribosomal RNA

    FEBS Lett.

    (1991)
  • W.K.K. Ho et al.

    Cloning of the cDNA of α-momorcharin: a ribosome inactivating protein

    Biochim. biophys. Acta

    (1991)
  • L.L. Houston et al.

    Seasonal variations in different forms of pokeweed antiviral protein, a potent inactivator of ribosomes

    J. biol. Chem.

    (1983)
  • J.D. Irvin

    Pokeweed antiviral protein

    Pharmac. Ther.

    (1983)
  • J.M. Lambert et al.

    Purified immunotoxins that are reactive with human lymphoid cells

    J. biol. Chem.

    (1985)
  • R. Leah et al.

    Biochemicla and molecular characterization of three barley seed proteins with antifungal properties

    J. biol. Chem.

    (1991)
  • S. Lee-Huang et al.

    A new class of antiHIV agents: GAP31, DAPs 30 and 32

    FEBS Lett.

    (1991)
  • G. Legname et al.

    Nucleotide sequence of cDNA coding for dianthin 30, a ribosome inactivating protein from Dianthus caryophyllus

    Biochim. biophys. Acta

    (1991)
  • Y. Masuho et al.

    Targeting of the antiviral protein from Phytolacca americana with an antibody

    Biochem. biophys. Res. Commun.

    (1982)
  • W. Montfort et al.

    The three-dimensional structure of ricin at 2.8 Å

    J. biol. Chem.

    (1987)
  • M. Piatak et al.

    Expresion of soluble and fully functional ricin A-chain in E. coli is temperature sensitive

    J. biol. Chem.

    (1988)
  • M. Ready et al.

    Requirements for antiribosomal activity of pokeweed antiviral protein

    Biochim. biophys. Acta

    (1983)
  • M.P. Ready et al.

    Dodecandrin; a new ribosome-inhibiting protein from Phytolacca dodecandra

    Biochim. biophys. Acta

    (1984)
  • R.R. Reisbig et al.

    The protein synthesis inhibitors from wheat, barley and rye have identical antigenic determinants

    Biochem. biophys. Res. Commun.

    (1983)
  • F. Stirpe et al.

    Ribosome-inactivating proteins up to date

    FEBS Lett.

    (1986)
  • R.C. Stong et al.

    Use of multiple T-cell directed intact ricin immunotoxins for autologous bone marrow transplantation

    Blood

    (1985)
  • J.P. Allison et al.

    Monoclonal antibody to tumor specific epitope for murine lymphoma cells: use in characterization of antigen and in immunotherapy

  • G.M. Aron et al.

    Cytotoxicity of pokeweed antiviral protein

    Cytobios

    (1988)
  • L. Barbieri et al.

    Purification and partial characterization of another form of the pokeweed antiviral protein from the seeds of Phytolacca americana L. (pokeweed)

    Biochem. J.

    (1982)
  • L. Barbieri et al.

    Ribosome-inactivating proteins from plant cells in culture

    Biochem. J.

    (1989)
  • H.B. Bass et al.

    A maize ribosome-inactivating protein is controlled by the transcriptional activator opaque-2

    Plant Cell

    (1992)
  • M.G. Battelli et al.

    Differenital effect of ribosome-inactivating proteins on plant ribosome activity and plant cells growth

    J. exp. Botany

    (1984)
  • L. Benatti et al.

    Nucleotide sequence of cDNA coding for saporin-6, a type-1 ribosome-inactivating protein from Saponaria officinalis

    Eur. J. Biochem.

    (1989)
  • V.S. Beyers et al.

    A phase I/II study of trichosanthin treatment of HIV disease

    AIDS

    (1990)
  • M.S. Bonness et al.

    Tissue culture of endod (Phytolacca dodecandra L'Herit): growth and production of ribosome-inactivating proteins

    Plant Cell Rep.

    (1992)
  • A. Bzowska et al.

    Comparison of acid- and enzyme-catalyzed cleavage of the glycosidic bond of N(7)-substituted gaunosines

    Nucleosides Nucleotides

    (1990)
  • T.P. Chwo et al.

    Isolation and DNA sequence fo a gene encoding α-trichosanthin, a type I ribosome-inactivating protein

    J. biol. Chem.

    (1990)
  • A. Falasca et al.

    Properties of the ribosome-inactivating proteins gelonin, Momordica charantia inhibitor and dianthins

    Biochem. J.

    (1982)
  • A.P. Fordham-Skelton et al.

    Characterization of saporin genes: in vitro expression and ribosome inactivation

    Molec. gen. Genet.

    (1991)
  • A. Frankel et al.

    Selection and characterization of mutants of ricin toxin A chain in Saccharomyces cerevisiae

    Molec. Cell Biol.

    (1989)
  • Cited by (106)

    • Advances and prospects in biogenic substances against plant virus: A review

      2017, Pesticide Biochemistry and Physiology
      Citation Excerpt :

      It is the main antiviral-active constituent from Phytolacca americana L., which exhibits a broad spectrum antiviral activity against TMV, poliovirus, herpes simplex virus (HSV), influenza virus, cytomegalovirus and human immunodeficiency virus (HIV) and so on. It can effectively inhibit replication of viruses at concentrations which do not suppress protein synthesis of the host cells [37–43]. Other plants in which the anti-plant-virus effective compounds are proteins include Chenopodium amaranticolor, and Mirabilis jalapa L. (see Table 1).

    • Ribosomal Protein L3: Gatekeeper to the A Site

      2007, Molecular Cell
      Citation Excerpt :

      Regions of two important rRNA helical structures are also anchored on this central extension (also called the “W finger” after the tryptophan residue): helix 95, and the structure formed by helices 90–92. Helix 95 contains the sarcin/ricin loop (SRL), one of the key structures recognized by the translation elongation factors, and the target of ribosome-inactivating proteins such as ricin (reviewed in Irvin and Uckun [1992]). The helix 90–92 structure is important because it forms one side of the corridor along which the 3′ ends of aa-tRNAs slide during the process of accommodation (Sanbonmatsu et al., 2005).

    View all citing articles on Scopus
    View full text