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Construction and characterization of a bispecific diabody for retargeting T cells to human carcinomas by Wijnand Helfrich; Bart Jan Kroesen; Rob C. Roovers; Lidia Westers; Grietje Molema; Hennie R. Hoogenboom; Lou de Leij is a Medicine article available to read on EtoBox.

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We describe the construction of a recombinant bispecific antibody fragment in the diabody format with specificity for both the well-established human pancarcinoma associated target antigen EGP2 (epithelial glycoprotein 2, also known as the CO17-1A antigen or KSA) and the CD3⑀ chain of human TCR/CD3 complex. The murine anti-EGP2 (MOC31) single chain variable fragment (scFv) and the humanized anti-CD3 (Ucht1v9) scFv were cast into a diabody format (designated Dia5v9) using a short 5 amino acid Gly-Ser linker between immunoglobulin heavy-chain and light-chain variable domains. Purification of the poly-histidine tagged Dia5v9 was achieved from extracts of protease deficient Escerichia coli by IMAC chromatography. The Dia5v9 diabody showed strong binding to both EGP2 and CD3 in transfected cells. The in vitro efficacy of Dia5v9 in mediating tumor cell lysis by interleukin-2 activated human T cells appeared to be similar to that of the hybrid-hybridoma-derived BsF(abЈ) 2 Bis1 (anti-EGP2/anti-CD3) in a standard 4-hr 51 Cr-release assay. This small and partially humanized recombinant bispecific antibody fragment may be valuable for T-cell-based immunotherapeutical treatment protocols, reta

Who reads Construction and characterization of a bispecific diabody for retargeting T cells to human carcinomas?

Author

Wijnand Helfrich; Bart Jan Kroesen; Rob C. Roovers; Lidia Westers; Grietje Molema; Hennie R. Hoogenboom; Lou de Leij

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley; Research Square; Test accounts (ISSN 0020-7136)

Published

1998

Language

EN

Field

Medicine (Health Sciences)