Abstract:
:Bispecific 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Müller KM,Arndt KM,Strittmatter W,Plückthun Adoi
10.1016/s0014-5793(98)00021-0subject
Has Abstractpub_date
1998-01-30 00:00:00pages
259-64issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00021-0journal_volume
422pub_type
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