This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Chovnick, A. Articles by Chang, C. N. Search for Related Content PubMed PubMed Citation Articles by Chovnick, A. Articles by Chang, C. N.

A Recombinant, Membrane-acting Immunotoxin

Protein Design Labs, Mountain View, California 94043

The anti-Tac antibody is known to bind to the p55 chain of the human interleukin 2 receptor. An immunotoxin was produced by genetically linking Clostridium perfringens phospholipase C (PLC) to the Fab domain of anti-Tac. For this purpose, the PLC gene, with its own promoter and signal sequence, was fused to the 5' end of the V_HC_H1 segment of the anti-Tac heavy chain gene. The anti-Tac light chain gene, with an attached bacterial signal sequence, was made part of the same transcriptional unit. Escherichia coli transformed with the construct secreted a recombinant immunotoxin, anti-Tac(Fab)-PLC, in an active form. Anti-Tac(Fab)-PLC bound to cells expressing the interleukin 2 receptor and inhibited protein synthesis, with a 50% inhibitory concentration of 0.02 nM (1.8 ng/ml).

Received 9/ 6/90. Accepted 10/30/90.

This article has been cited by other articles:

				M. Better, S. L. Bernhard, R. E. Williams, S. D. Leigh, R. J. Bauer, A. H. C. Kung, S. F. Carroll, and D. M. Fishwild T Cell-targeted Immunofusion Proteins from Escherichia coli J. Biol. Chem., June 23, 1995; 270(25): 14951 - 14957. [Abstract] [Full Text] [PDF]