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Improved stability and yield of Fv targeted superantigen by introducing both linker and disulfide bond into the targeting moiety.

Abstract：

:Bacterial superantigens (SAg) are the most potent activators of human T lymphocytes and recombinant immunotoxin using bacterial SAg shows promising clinical values. To engineer superantigen for immunotherapy of hepatocellular carcinoma, we genetically fused the superantigen staphylococcus enterotoxin A (SEA(D(227)A)) to the single-chain disulfide-stabilized Fv (scdsFv) of anti-hepatoma monoclonal antibody HAb25 through a short peptide GGGSGGS. We expressed this recombinant protein in Escherichia coli and extract it from inclusion bodies. We found purified scdsFv-targeted SAg contains equivalent binding affinity with disulfide-stabilized Fv (dsFv) targeted SAg and single-chain Fvs (scFv) targeted SAg, but more stable and more suitable for large scale production. The MTS(3-(4,5-dimethylthiazole-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazoliu m, inner salt) assay shows that the scdsFv-targeted SAg also shares the ability to activate a large number of T lymphocytes and has cytotoxic activity on human hepatoma cell line SMMC-7721. Therefore, this novel generation of recombinant immunotoxins using scdsFv has a high potential in hepato cancer treatment and the same strategy may also be applied to other cancer treatments.

journal_name

Biochimie

journal_title

Biochimie

authors

Hao HJ,Jiang YQ,Zheng YL,Ma R,Yu DW

doi

10.1016/j.biochi.2005.04.005

keywords:

subject

Has Abstract

pub_date

2005-08-01 00:00:00

pages

661-7

issue

8

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(05)00100-8

journal_volume

87

pub_type

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