Differential sensitivity of HELA cells to the type 2 ribosome-inactivating proteins ebulin l, nigrin b and nigrin f as compared with ricin.
The new type 2 RIPs ebulin l, nigrin b and nigrin f present in Sambucus display toxicity to HELA cells several orders of magnitude lower than that displayed by ricin. Despite N-terminal amino acid homology between the three RIPs in both the A and the B chains, these compounds display very different degrees of toxicity to HELA cells that does not seem to be paralleled by immunologic correlations. It is suggested that small changes in the protein structure are most probably responsible for the different degrees of toxicity.
Citores
L
L
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Valladolid, Spain.
Muñoz
R
R
De Benito
F M
FM
Iglesias
R
R
Ferreras
J M
JM
Girbes
T
T
D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D006367:HeLa Cells; D006801:Humans; D009699:N-Glycosyl Hydrolases; D010940:Plant Proteins / Q000633:toxicity*; D011500:Protein Synthesis Inhibitors / Q000633:toxicity*; D054790:Ribosome Inactivating Proteins, Type 2; D012276:Ricin / Q000633:toxicity*
D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D054790:Ribosome Inactivating Proteins, Type 2; D012276:Ricin; D009699:N-Glycosyl Hydrolases