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논문 기본 정보

자료유형
학술저널
저자정보
Pillay Tahir S. (Department of Chemical Pathology and NHLS- Tshwane Academic Division University of Pretoria Pretori) Muyldermans Serge (Cellular and Molecular Immunology Vrije Universiteit Brussel Brussels BelgiumLiaoning Key Laborator)
저널정보
대한진단검사의학회 Annals of Laboratory Medicine Annals of Laboratory Medicine 제41권 제6호
발행연도
2021.11
수록면
549 - 558 (10page)
DOI
10.3343/alm.2021.41.6.549

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Antibodies have proven to be central in the development of diagnostic methods over decades, moving from polyclonal antibodies to the milestone development of monoclonal antibodies. Although monoclonal antibodies play a valuable role in diagnosis, their production is technically demanding and can be expensive. The large size of monoclonal antibodies (150 kDa) makes their re-engineering using recombinant methods a challenge. Single-domain antibodies, such as “nanobodies,” are a relatively new class of diagnostic probes that originated serendipitously during the assay of camel serum. The immune system of the camelid family (camels, llamas, and alpacas) has evolved uniquely to produce heavy-chain antibodies that contain a single monomeric variable antibody domain in a smaller functional unit of 12?15 kDa. Interestingly, the same biological phenomenon is observed in sharks. Since a single-domain antibody molecule is smaller than a conventional mammalian antibody, recombinant engineering and protein expression in vitro using bacterial production systems are much simpler. The entire gene encoding such an antibody can be cloned and expressed in vitro. Single-domain antibodies are very stable and heat-resistant, and hence do not require cold storage, especially when incorporated into a diagnostic kit. Their simple genetic structure allows easy re-engineering of the protein to introduce new antigen-binding characteristics or attach labels. Here, we review the applications of single-domain antibodies in laboratory diagnosis and discuss the future potential in this area.

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