• Biochem. Biophys. Res. Commun. · Oct 2000

    Cytotoxic activity of recombinant bFGF-rViscumin fusion proteins.

    • A Schmidt, B Möckel, J Eck, M Langer, M Gauert, and H Zinke.
    • BRAIN Aktiengesellschaft, Zwingenberg, 64673, Germany.
    • Biochem. Biophys. Res. Commun. 2000 Oct 22; 277 (2): 499-506.

    AbstractA fusion protein (bFGF-rMLA), containing the mitogen basic fibroblast growth factor (bFGF) and the cytotoxic component of rViscumin (recombinant mistletoe lectin), the enzymatic A-chain (rMLA), was expressed in Escherichia coli, purified, and functionally characterized. bFGF-rMLA is cytotoxic for mouse B16 melanoma cells expressing the FGF receptor with an IC(50) value of approximately 1 nM. rMLA shows no significant effect on the viability of the B16 cells up to a concentration of 141 nM. Additionally, bFGF-rMLA was associated with the rViscumin B-chain (rMLB) in an in vitro folding procedure. The IC(50) value of bFGF-rMLA/rMLB to B16 cells in the presence of lactose-to block rMLB lectin activity-was 134 pM. Thus, it was possible to enhance the efficacy of a rViscumin A-chain mitotoxin through addition of rMLB. We conclude that rViscumin fusion proteins may be generally applicable for the receptor-specific inactivation of target cells and point out their potential in drug development.Copyright 2000 Academic Press.

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