期刊
MABS
卷 7, 期 1, 页码 15-25出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/19420862.2015.989032
关键词
antibody technology; biologic therapeutic; heavy chain antibody; IgNAR; shark; single chain binding domain; CDR; complementarity-determining region; HV; hypervariable region; IgNAR; immunoglobulin new antigen receptor; IgNAR V domain; variable domain of IgNAR; mAbs; monoclonal antibodies; scFv; single chain variable fragment; VL; variable domain of the light chain; VH; variable domain of the heavy chain; VHH; variable domain of camelid heavy chain antibodies; vNAR; variable domain of IgNAR
资金
- Federal Ministry of Education and Research (BMBF) in frame of the consortium Nanokat
- BBSRC [BB/K010905/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K010905/1] Funding Source: researchfish
In addition to antibodies with the classical composition of heavy and light chains, the adaptive immune repertoire of sharks also includes a heavy-chain only isotype, where antigen binding is mediated exclusively by a small and highly stable domain, referred to as vNAR. In recent years, due to their high affinity and specificity combined with their small size, high physicochemical stability and low-cost of production, vNAR fragments have evolved as promising target-binding scaffolds that can be tailor-made for applications in medicine and biotechnology. This review highlights the structural features of vNAR molecules, addresses aspects of their generation using immunization or in vitro high throughput screening methods and provides examples of therapeutic, diagnostic and other biotechnological applications.
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