Renaturation and purification of ApxII toxin of Actinobacillus pleuropneumoniae

文献类型: 外文期刊

第一作者: Wang, Chunlai

作者: Wang, Chunlai;Liu, Siguo;Peng, Yonggang;Shao, Meili;Wang, Yong;Gong, Qiang;Chang, Yuehong;Liu, Jiandong;Liu, Huifang;Liu, Di;Kong, Xiangang

作者机构:

关键词: expression;renaturation;purification;ApxII toxin;hemolytic activity;PORCINE CONTAGIOUS PLEUROPNEUMONIA;ESCHERICHIA-COLI;RTX-TOXINS;VIRULENCE;SEROTYPE-1;EXPRESSION;PIGS;HEMOLYSINS;SUBUNIT;OPERONS

期刊名称:PROTEIN EXPRESSION AND PURIFICATION ( 影响因子:1.65; 五年影响因子:1.548 )

ISSN:

年卷期:

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收录情况: SCI

摘要: ApxII toxin is the only Apx toxin that is produced by Actinobacillus pleuropneumoniae serotype 7. In order to determine whether the recombinant ApxII that derived from Escherichia coli (E. coli) expression is faithful to the natural ApxII so that can be used as additional component in vaccine preparation, the structure gene apxIIA of ApxII toxin was expressed in E coli with prokaryotic expression vector pGEX-6p-1 (formed pGEX-6p-A). pGZRS-C which is A. pleuropneunionicte-E. coli shuttle vector pGZRS-38 expressing the post-transcriptional activation gene apxII C was co-expressed with pGEX-6p-A. The expression product of rApxII A formed inclusion. The inclusion protein was oxidized, refolded and restored hemolytic activity after denaturation, renaturation and purification. The result indicated that E. coli expressed recombinant ApxII toxin has good fidelity, which makes it possible to produce this valuable antigen for vaccine preparation or diagnosis. (c) 2006 Elsevier Inc. All rights reserved.

分类号: Q51

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