Abstract
Escherichia coli clones expressing recombinant shiga toxin (Stx1) and its derivatives Stx1-A and Stx1-B subunits were established to release the proteins into periplasmic space. The expression was examined by SDS-PAGE to visualize the subunits. The secreted assembled subunits were extracted with polymyxin B and assessed for biological activity. The results showed that the presence of N-terminus leader sequence of the gene is essential for assembly of the subunits to yield biologically active holotoxin (AB5). The absence of the leader sequence did not affect the expression of the subunits but did disrupt the holotoxin assembly.
Keywords: Recombinant shiga toxin, Holotoxin assembly, N-terminus leader sequence
Protein & Peptide Letters
Title: N-Terminus Leader Sequence of Shiga Toxin (Stx) 1 Is Essential for Production of Active Recombinant Protein in E. coli
Volume: 13 Issue: 5
Author(s): Mana Oloomi, Saeid Bouzari and Mania Arshadi
Affiliation:
Keywords: Recombinant shiga toxin, Holotoxin assembly, N-terminus leader sequence
Abstract: Escherichia coli clones expressing recombinant shiga toxin (Stx1) and its derivatives Stx1-A and Stx1-B subunits were established to release the proteins into periplasmic space. The expression was examined by SDS-PAGE to visualize the subunits. The secreted assembled subunits were extracted with polymyxin B and assessed for biological activity. The results showed that the presence of N-terminus leader sequence of the gene is essential for assembly of the subunits to yield biologically active holotoxin (AB5). The absence of the leader sequence did not affect the expression of the subunits but did disrupt the holotoxin assembly.
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Cite this article as:
Oloomi Mana, Bouzari Saeid and Arshadi Mania, N-Terminus Leader Sequence of Shiga Toxin (Stx) 1 Is Essential for Production of Active Recombinant Protein in E. coli, Protein & Peptide Letters 2006; 13 (5) . https://dx.doi.org/10.2174/092986606776819538
DOI https://dx.doi.org/10.2174/092986606776819538 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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