The first constant domain (C H 1 and C L ) of an antibody used as heterodimerization domain for bispecific miniantibodies
1998; Wiley; Volume: 422; Issue: 2 Linguagem: Inglês
10.1016/s0014-5793(98)00021-0
ISSN1873-3468
AutoresKristian M. Müller, Katja M. Arndt, Wolfgang Strittmatter, Andreas Plückthun,
Tópico(s)Advanced Biosensing Techniques and Applications
ResumoBispecific miniantibodies were constructed by genetically fusing the C H 1 domain of an IgG1 to the C‐terminus of a single‐chain Fv fragment (scFv‐425), specific for the EGF receptor, and fusing the C L domain of a kappa light chain to the C‐terminus of a scFv specific for CD2 (scFv‐M1). An efficient dicistronic gene arrangement for functional expression in Escherichia coli was constructed. Immunoblots demonstrated correct domain assembly and the formation of the natural C H 1‐C L disulfide bridge. Gel filtration confirmed the correct size, sandwich ELISAs demonstrated bispecific functionality, and SPR biosensor measurements determined binding to EGF‐R in comparison to bivalent constructs. Bispecific anti‐EGF‐R/anti‐CD2 miniantibodies are candidates for the immunotherapy of cancer.
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