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Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L.

1993; Elsevier BV; Volume: 1216; Issue: 1 Linguagem: Inglês

10.1016/0167-4781(93)90035-c

1879-2634

Augusto Parente, Paolo De Luca, Andrea Bolognesi, Luigi Barbieri, Maria Giulia Battelli, Ada Abbondanza, Manuela J.W. Sande, Gesualdo Siniscalco Gigliano, Pier Luigi Tazzari, Fiorenzo Stirpe,

Plant tissue culture and regeneration

Three ribosome-inactivating proteins (RIPs) similar to those already known (Stirpe et al. (1992) Bio/Technology 10, 405–412) were purified from the seeds of Phytolacca dioica. These proteins, called Phytolacca dioica RIPs (PD-S1, PD-S2 and PD-S3 RIPs), are glycoproteins, with Mr approx. 30 000, inhibit protein synthesis by a rabbit reticulocyte lysate and phenylalanine polymerization by isolated ribosomes, and depurinate rat liver rRNA in an apparently identical manner as the A-chain of ricin and other RIPs (Endo et al. (1987) J. Biol. Chem. 262, 5908–5912). Part of the purified rat liver ribosomes appeared resistant to the action of PD-S RIPs. The most abundant protein, PD-S2 RIP, gave a weak or nil cross-reaction with sera against various other RIPs, including a pokeweed antiviral protein from the roots of Phytolacca americana. PD-S2 RIP was linked to a monoclonal antibody (Ber-H2) against the CD30 human lymphocyte antigen and the resulting immunotoxin was selectively toxic to the CD30+ Hodgkin's lymphoma-derived L540 cell line.