Neutralization and binding activity of a human single-chain antibody to ricin toxin

Ricin toxin (RT), extracted from castor bean, is a type II ribosome-inactivating protein (RIP). As a biothreat agent, there is no effective antidote for RT to date, but recent advances in antibody research may have meet this need. This study aimed to produce human single-chain antibody variable frag...

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Veröffentlicht in:Food and agricultural immunology 2020-01, Vol.31 (1), p.63-74
Hauptverfasser: Yu, Haotian, Chang, Ying, Dong, Mingxin, Wang, Yan, Sun, Chengbiao, Liu, Zhongliang, Wang, Xin, Xu, Na, Liu, Wensen
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Sprache:eng
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Zusammenfassung:Ricin toxin (RT), extracted from castor bean, is a type II ribosome-inactivating protein (RIP). As a biothreat agent, there is no effective antidote for RT to date, but recent advances in antibody research may have meet this need. This study aimed to produce human single-chain antibody variable fragments (HuscFvs) that bind to and interfere with RT activity for further clinical use. The purified RT component was used in phage biopanning to select ricin-bound HuscFv-displayed phage clones from synthetic (Tomlinson I + J) phage display libraries. The selected HuscFv, named JE11, showed an almost 100% protective effect to HeLa cells by mixing with RT at a 1:1000 ratio in vitro. The antibody showed an 83% protection against injection of 2 × LD 50 RT dose mice within 72 h. This research has therapeutic potential for the diagnosis and treatment of RT poisoning.
ISSN:0954-0105
1465-3443
DOI:10.1080/09540105.2019.1698521