NDLI: Analysis of recombinant protein toxicity in E. coli through a phage λ-based genetic screening system

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Analysis of recombinant protein toxicity in E. coli through a phage λ-based genetic screening system

Content Provider	Springer Nature Link
Author	Fernández, Guerau Vera, Andrea Villaverde, Antonio Martínez, Miguel Ángel
Copyright Year	2007
Abstract	The aspartic protease from the human immunodeficiency virus type 1 (HIV-1) is highly toxic to E. coli, thus impairing its yield in production processes. Proteolytic cleavage of essential cellular proteins is probably a major contributor to the bacteriocidal effect but this has not been proven. Through an adapted high-throughput λ-based screening system, we have analyzed a set of HIV-1 protease mutants with distinguishable catalytic properties and we show that inactive enzymes are as toxic to E. coli cells as the wild-type enzyme. Together with additional data from directed molecular evolution approaches, these results indicate that the toxicity of the viral protease is not linked to its proteolytic activity. Our study also reveals that the λ-based screening system is a robust new tool for the genetic analysis of highly toxic recombinant products in E. coli.
Starting Page	1381
Ending Page	1386
Page Count	6
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	29
Issue Number	9
e-ISSN	15736776
Language	English
Publisher	Springer Netherlands
Publisher Date	2007-05-04
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	E. coli Genetic screening HIV-1 Protease Protein production Toxicity Biochemistry Applied Microbiology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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