C-terminal deletion mutant of pokeweed antiviral protein inhibits viral infection but does not depurinate host ribosomes.

Pokeweed antiviral protein (PAP), a 29-kDa protein isolated from Phytolacca americana, inhibits translation by catalytically removing a specific adenine residue from the large rRNA of the 60S subunit of eukaryotic ribosomes. In addition to its ribosome-inactivating ability, PAP has potent antiviral activity against many plant and animal viruses, including HIV. We recently described the isolation and characterization of nontoxic PAP mutants, NT123-2, which has a point mutation (E176V) in the active site that abolishes enzymatic activity, and NT124-3, which has a nonsense mutation that results in deletion of the C-terminal 25 aa (W237Stop).

Protoplasts from Phytolacca dodecandra L'Herit (endod) and P. americana L. (pokeweed).

Pokeweed (Phytolacca americana L.) and endod (P. dodecandra L'Herit) produce ribosome-inactivating proteins which are sequestered in leaf cell walls.

Enzymes of B-ring-deoxy flavonoid biosynthesis in elicited cell cultures of "old man" cactus (Cephalocereus senilis).

Elicited cell cultures of the cactus Cephalocereus senilis produce a group of flavonoids with unsubstituted B-rings, including an aurone which represents a new class of phytoalexin. Preliminary enzymological studies indicated that the chalcone synthase (CHS) and chalcone isomerase (CHI) from cultures of C. senilis were active with cinnamoyl-CoA and 2',4',6'-trihydroxychalcone, respectively, probable intermediates for synthesis of flavonoids with unsubstituted B-rings.