Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
- PMID: 11295555
- DOI: 10.1016/s0968-0004(01)01790-x
Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
Abstract
The antigen-binding site of antibodies from vertebrates is formed by combining the variable domains of a heavy chain (VH) and a light chain (VL). However, antibodies from camels and llamas are an important exception to this in that their sera contain, in addition, a unique kind of antibody that is formed by heavy chains only. The antigen-binding site of these antibodies consists of one single domain, referred to as VHH. This article reviews the mutations and structural adaptations that have taken place to reshape a VH of a VH-VL pair into a single-domain VHH with retention of a sufficient variability. The VHH has a potent antigen-binding capacity and provides the advantage of interacting with novel epitopes that are inaccessible to conventional VH-VL pairs.
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