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single-domain antibody

from Biotechnology11

Single domains represent the smallest known fragment still capable of binding antigen that can be isolated from a full-sized immunoglobulin. In work on the cloning of antibody genes and construction of human antibody libraries, Greg Winter and his colleagues found that single domains comprised of either VH or VL derived from human antibodies could also be stabilized as stand-alone, antibody fragments. Shortly thereafter, heavy-chain-only antibodies (HCAbs) were discovered to occur naturally in camelids where the binding domains constitute paired VHs with no light chains. HCAbs are thought to represent up to 50–80% of the antibody repertoire in camels and up to 10–25% of the antibody repertoire in other members of the Camelidae family such as llamas. Similar antibodies also lacking a CH1 domain and a light chain termed Ig-NAR have also been identified in nurse sharks, although these will not be discussed further in this overview (Figure 1). More recently, a new type of “domain antibody” was constructed using the CH2 domain of an IgG as the base scaffold into which CDR loops were grafted. These antibodies with unpaired antigen binding domains, and the single domain versions derived from them, have unique properties and have already shown promise as potential therapeutic antibodies. For the purposes of this review, these molecules (whether derived from VH or VL variable regions or isolated from camelids) will be described as single-domain antibodies (sdAbs).

about 2 years ago

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