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J. Biol. Chem., Vol. 276, Issue 10, 7346-7350, March 9, 2001
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From the Department of Ultrastructure, Vlaams Interuniversitair
Instituut voor Biotechnologie, Vrije Universiteit Brussel,
Paardenstraat 65, B-1640 Sint Genesius Rode, Belgium
Single-domain antibodies against various antigens
are isolated from the unique heavy-chain antibodies of immunized camels and llamas. These minimal sized binders are very robust and bind the
antigen with high affinity in a monomeric state. We evaluated the
feasibility to produce soluble, functional bispecific and bivalent
antibodies in Escherichia coli with camel single-domain antibody fragments as building blocks. Two single-domain antibody fragments were tethered by the structural upper hinge of a natural antibody to generate bispecific molecules. This linker was chosen for
its protease resistance in serum and its natural flexibility to
reorient the upstream and downstream located domains. The expression levels, ease of purification, and the solubility of the recombinant proteins were comparable with those of the constituent monomers. The
individual moieties fully retain the binding capacity and the
binding characteristics within the recombinant bispecific constructs.
The easy generation steps and the biophysical properties of these
bispecific and bivalent constructs based on camel single-domain antibody fragments makes them particularly attractive for use in
therapeutic or diagnostic programs.
Camel Single-domain Antibodies as Modular Building Units in
Bispecific and Bivalent Antibody Constructs*
,
*
This work was supported by a predoctoral grant from the
Fonds Wetenschappelijk Onderzoek-Vlaanderen (FWO) (to C. K.), by
Instelling voor Wetenschap en Technologie (IWT), and by
Onderzoeksraad-Vrije Universiteit Brussel.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. E-mail:
kconrath@vub.ac.be.
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