Bacterial and plant-produced scFv proteins have similar antigen-binding properties

被引:47
作者
Bruyns, AM [1 ]
DeJaeger, G [1 ]
DeNeve, M [1 ]
DeWilde, C [1 ]
VanMontagu, M [1 ]
Depicker, A [1 ]
机构
[1] STATE UNIV GHENT VIB, DEPT GENET, GENET LAB, B-9000 GHENT, BELGIUM
关键词
antibody affinity; Escherichia coli; heterologous gene expression; Nicotiana tabacum; single-chain variable fragment; transgenic plant;
D O I
10.1016/0014-5793(96)00372-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A gene encoding a single-chain variable (scFv) antibody fragment was expressed as a cytoplasmic and endoplasmic reticulum-targeted protein in transgenic tobacco plants, In both cases, the scFv accumulated up to 0.01% of total soluble protein (TSP), The same scFv fragment was also produced in the periplasm of Escherichia coli, Measurement of the affinity by ELISA indicates that the affinity of the bacterially made scFv is about 80-fold lower than that of the parental F-ab fragment, The results suggest that the affinity of the plant-produced scFv fragments is reduced to a similar extent, implying that all the plant-produced scFv fragments are antigen binding.
引用
收藏
页码:5 / 10
页数:6
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