[Chimeric toxin of the A-subunit of viscumin and the B-subunit of ricin].
A chimeric toxic protein was prepared from the mistletoe lectin I A-chain and ricin B-chain by using the disulfide exchange reaction. Ricin and chimeric protein were indistinguishable in binding to immobilized asialofetuin in ELISA. The chimeric protein was more toxic for Jurkat cells than native mistletoe lectin I, but not as effective as native ricin. In the presence of NH4Cl, which enhances the toxicity of some toxins and immunotoxins, but does not influence ricin toxicity, both ricin and chimeric toxin had equal cytotoxic activity. The possibility is discussed that the ricin B-chain protects the ricin A-chain from degradation during delivery from the cell surface to the place where it is translocated into the cytosol.
Tonevitskiĭ
A G
AG
University Witten/Herdecke, Berlin, Germany,
Toptygin
A Iu
AIu
Agapov
I I
II
Shamshiev
A T
AT
Pfuller
U
U
Ershova
G V
GV
Prokof'ev
S A
SA
Rakhmanova
V A
VA
D001212:Asialoglycoproteins / Q000378:metabolism; D001692:Biological Transport; D002478:Cells, Cultured; D003600:Cytosol / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D060748:Fetuins; D037102:Lectins / Q000737:chemistry*; D014784:Mistletoe / Q000737:chemistry*; D037121:Plant Lectins; D028321:Plant Preparations; D010940:Plant Proteins; D010946:Plants, Medicinal; D011993:Recombinant Fusion Proteins / Q000138:chemical synthesis* / Q000378:metabolism; D054790:Ribosome Inactivating Proteins, Type 2; D012276:Ricin / Q000737:chemistry* / Q000378:metabolism; D014118:Toxins, Biological / Q000737:chemistry*; D000509:alpha-Fetoproteins / Q000378:metabolism
D001212:Asialoglycoproteins; D060748:Fetuins; D037102:Lectins; D037121:Plant Lectins; D028321:Plant Preparations; D010940:Plant Proteins; D011993:Recombinant Fusion Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological; D000509:alpha-Fetoproteins; C017029:asialofetuin; C009674:ribosome inactivating protein, Viscum; D012276:Ricin