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Cmyc tag 펩타이드에 특이적인 9E10 VHH 나노바디의 개발
김진규,한승희,김수현,홍선나 한국미생물학회 2022 미생물학회지 Vol.58 No.3
Based on structure of murine 9E10 antibody bound to cmyc tag peptide antigen, It was found that the complementarity determining region 3 of the heavy chain variable region of the 9E10 antibody consists of 18 long amino acids, which dominantly involves in cmyc tag peptide binding. This finding led us to engineer heavy chain variable domain of original mouse-derived 9E10 antibody into a camelid 9E10 nanobody. Since the camelid antibody consists only of a heavy chain variable domain with a size of only about 15 kDa and high solubility, it is called as 9E10 VHH nanobody. To produce 9E10 VHH nanobody, the cDNA for the heavy chain variable domain of murine 9E10 antibody was extracted from the hybridoma 9E10 cell line and its translated amino acids sequences was aligned with the camelid heavy chain variable domain sequences to replace mismatched murine amino acids with camelid amino acids. After completion of cloning of each gene into pUC119 expression vector, both original murine 9E10 heavy chain variable domain and 9E10 VHH nanobody were expressed and purified as a soluble protein in Escherichia coli. As expected, only camelid 9E10 VHH nanobody was expressed as a soluble protein. It showed the cmyc tag peptide binding activity in both enzyme-linked immunosorbent assay and Western blot. In addition, the range of dissociation constant for the interaction with the cmyc tag peptide was determined from 4.43 × 10-7 to 4.77 × 10-6 M by using bio-layer interferometry.
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