Acidic Peptide-Mediated Expression of the Antimicrobial Peptide Buforin II as Tandem Repeats inEscherichia coli

Lee, Jae H.; Minn, Il; Park, Chan B.; Kim, Sun C.

doi:10.1006/prep.1997.0814

Cited by 83 publications

(47 citation statements)

References 39 publications

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“…Buforin II is a 21-amino acids antimicrobial agent from the amphibian Bufo bufo gargarizans. This very basic peptide is lethal to E. coli but can be produced as a fusion with a neutralizing acidic peptide [42]. The target peptide can be cleaved from its protecting part, at methionine positions, by using cyanogen bromide.…”

Section: Ii3 Expression As Fusion Proteinsmentioning

confidence: 99%

Expression of Highly Toxic Genes in E. coli: Special Strategies and Genetic Tools

Saïda¹,

Uzan²,

Odaert³

et al. 2006

Current Protein and Peptide Science

138

112

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Escherichia coli (E. coli) remains the most efficient widely-used host for recombinant protein production. Well-known genetics, high transformation efficiency, cultivation simplicity, rapidity and inexpensiveness are the main factors that contribute to the selection of this host. With the advent of the post-genomic era has come the need to express in this bacterium a growing number of genes originating from different organisms. Unfortunately, many of these genes severely interfere with the survival of E. coli cells. They lead to bacteria death or cause significant defects in bacteria growth that dramatically decrease expression capabilities. In this paper, we review special strategies and genetics tools successfully used to express, in E. coli, highly toxic genes. Suppression of basal expression from leaky inducible promoters, suppression of read-through transcription from cryptic promoters, tight control of plasmids copy numbers and proteins production as inactive (but reversible) forms are among the solutions presented and discussed. Special expression vectors and modified E. coli strains are listed and their effectiveness illustrated with key examples, some of which are related to our study of the highly toxic phage T4 restriction endoribonuclease RegB. We mainly selected those strategies and tools that permit E. coli normal growth until the very moment of highly toxic gene induction. Expression then occurs efficiently before cells die. Because they do not target a particular toxic effect, these strategies and tools can be used to express a wide variety of highly toxic genes.

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Section: Ii3 Expression As Fusion Proteinsmentioning

confidence: 99%

Expression of Highly Toxic Genes in E. coli: Special Strategies and Genetic Tools

Saïda¹,

Uzan²,

Odaert³

et al. 2006

Current Protein and Peptide Science

138

112

View full text Add to dashboard Cite

show abstract

“…It cannot be said in advance which carrier protein will be suited well for this task in the case of each specific AMP. Incomplete list of the carrier proteins tested for this purpose includes: L-ribulokinase fragment, 15 glutathione-S-transferase, 16 Pseudomonas aeruginosa outer membrane protein, 16 Staphylococcus aureus protein A, and the dimer of its IgG-binding domain, 17 subtilisin inhibitor, 18 b-galactosidase, 18 maltose-binding protein, 18 prochymosin, 19 E.coli replication protein RepA and its fragment, 20 cellulose-binding domains, 20 human defensin HNP-1 preprodomain, 20 modified magainin intervening sequence (MIS), 21 GABA-transaminase, 22 truncated E.coli amidophosphoribosyltransferase, 23 Pseudomonas testosteroni ketosteroid isomerase, 24 fluorescent proteins GFP and obelin, 25 31 and ubiquitin. 32 An intein-based expression and purification system was also described.…”

Section: Arenicin-2 Expression and Purificationmentioning

confidence: 99%

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

et al. 2007

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Arenicins are 21‐residue cationic antimicrobial peptides isolated from marine polychaeta Arenicola marina. The peptides exhibit potent broad‐spectrum antimicrobial activity. In water solution arenicin‐2 adopts a β‐hairpin conformation, stabilized by one disulfide and nine hydrogen bonds. To determine the propensity for the peptide oligomerization in membrane mimetic systems, the recombinant arenicin‐2 was overexpressed as a fused form in Escherichia coli. The arenicin‐2 oligomerization and intermolecular packing in membrane mimicking environment were investigated using high‐resolution NMR spectroscopy. The present studies show that arenicin‐2 preserves a β‐hairpin structure and forms asymmetric dimers upon incorporation into the dodecylphosphocholine micelle. Two monomers of arenicin‐2 are aligned parallel to each other by the N‐terminal strands of the β‐hairpin (CN↑↑NC type of association). Polyacrylamide gel electrophoresis analysis indicated that in environment of anionic SDS micelles the arenicin‐2 might undergo further oligomerization and form tetramers. Our results afford further molecular insight into possible mechanism of antimicrobial action of arenicins. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 455–464, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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“…Este é o principal entrave para a introdução dos peptídeos como fármacos, pois a sua produção custa de cinco a vinte vezes mais do que a dos antibióticos usuais (LEE et al, 1998; VAN'T HOF et al, 2001, HANCOCK;SAHL, 2006). As metodologias mais utilizadas para síntese de peptídeos antimicrobianos são a síntese química e a tecnologia do DNA recombinante (ver ítem 1.2).…”

Section: Custo Altounclassified

Estudo da relação estrutura-atividades e de propriedades do Hb40-61a, uma hemocidina sintética

Nogueira¹

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Acidic Peptide-Mediated Expression of the Antimicrobial Peptide Buforin II as Tandem Repeats inEscherichia coli

Cited by 83 publications

References 39 publications

Expression of Highly Toxic Genes in E. coli: Special Strategies and Genetic Tools

Expression of Highly Toxic Genes in E. coli: Special Strategies and Genetic Tools

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

Estudo da relação estrutura-atividades e de propriedades do Hb40-61a, uma hemocidina sintética

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