Unexpected tobacco etch virus (TEV) protease cleavage of recombinant human proteins

被引：1

作者：

Beaumont, Lauren P. ^{[1
]}

Mehalko, Jennifer ^{[1
]}

Johnson, Adam ^{[1
]}

Wall, Vanessa E. ^{[1
]}

Esposito, Dominic ^{[1
]}

机构：

[1] Frederick Natl Lab Canc Res, Prot Express Lab, NCI RAS Initiat, Frederick, MD 21702 USA

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2024年 / 220卷

基金：

美国国家卫生研究院;

关键词：

Tobacco etch virus protease; TEV; Solubility tags; Recombinant protein; protein purification; SPECIFICITY;

D O I：

10.1016/j.pep.2024.106488

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The tobacco etch virus (TEV) protease is a commonly used reagent for removal of solubility and purification tags from recombinant proteins and is cited as being highly specific for its canonical cleavage site. Flexibility in some amino acids within this recognition sequence has been described in the literature but researchers generally assume few native human proteins will carry off-target sequences for TEV cleavage. We report here the aberrant cleavage of three human proteins with non-canonical TEV protease cleavage sites and identify broader sequence specificity rules that can be used to predict unwanted cleavage of recombinant proteins. Using these rules, 456 human proteins were identified that could be substrates for unwanted TEV protease cleavage.

引用

页数：5

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