Ribosome-inactivating proteins from plant cells in culture

Author:

Barbieri L1,Bolognesi A1,Cenini P1,Falasca A I2,Minghetti A3,Garofano L4,Guicciardi A4,Lappi D4,Miller S P5,Stirpe F1

Affiliation:

1. Dipartimento di Patologia sperimentale, dell'Università di Bologna, 1-40126 Bologna, Italia.

2. tDipartimento di Biochimica dell'Università di Bologna, 1-40126 Bologna, Italia.

3. Dipartimento di Scienze farmaceutiche dell'Università di Bologna, 1-40126 Bologna, Italia.

4. Laboratorio di Biologia molecolare, Farmitalia Carlo Erba, 1-20149 Milano, Italia

5. Department of Biochemistry, University of Minnesota, Minneapolis, MN 55455, U.S.A.

Abstract

1. Ribosome-inactivating proteins were found in high amounts in one line of cells of Phytolacca americana (pokeweed) cultured in vitro and, in less quantity, in lines of Saponaria officinalis (soapwort) and of Zea mays (corn) cells. 2. The main ribosome-inactivating protein from pokeweed cells was purified to homogeneity. It is a protein with Mr 29,000 and basic pI, similar to the ‘pokeweed antiviral protein’ (PAP), a ribosome-inactivating protein from pokeweed leaves. We propose to call the pokeweed antiviral protein isolated from pokeweed cells PAP-C. 3. PAP-C inactivates ribosomes in a less-than-equimolar ratio, thus inhibiting protein synthesis by a rabbit reticulocyte lysate with an IC50 (concentration causing 50% inhibition) of 0.067 nM (2 ng/ml), and modifies rRNA in a manner apparently identical to that of ricin and other ribosome-inactivating proteins. It inhibits protein synthesis by intact cells with an IC50 of 0.7-3.4 microM, and is toxic to mice with an LD50 of 0.95 mg/kg.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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