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Peer-reviewedCC BY-NC 4.0Molecular Biology Research Communications

Cloning and heterologous expression of recombinant microcin S in Escherichia coli

  • Vahid Dianatpur1
  • Seyed Shahram Shekarforoush2
  • Abdollah Derakhshandeh1
  • Azar Motamedi-Boroojeni1
  • Vida Eraghi3
  • Farhid Hemmatzadeh4
4 affiliations
  1. 1Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
  2. 2Department of Food Hygiene and Public Health, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
  3. 3Department of Veterinary Pathology, Faculty of Veterinary Medicine, University of Zagreb, Zagreb, Croatia
  4. 4School of Animal and Veterinary Sciences, Adelaide University, Roseworthy, SA, Australia
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Abstract

New antibacterial agents against antibiotic-resistant pathogens have clearly attracted global attention. Microcins, as peptide antibiotics, offer novel antimicrobial strategies for therapeutic uses. This study aimed to assess heterologous expression of recombinant microcin S (MccS) from Escherichia coli G3/10 in E. coli BL21 Star™ (DE3). The physicochemical properties of the MccS protein were analyzed using bioinformatics methods. The desired sequence of the MccS gene was optimized and synthesized in the pMAL-p5X expression vector, positioned downstream and in frame with the maltose-binding protein (MBP) coding sequence. Verification of recombinant protein expression in E. coli BL21 Star™ (DE3) was carried out using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Based on the results, the expression of MBP fusion MccS protein with a molecular weight of ~52.742 KDa was achieved in E. coli BL21 Star™ (DE3). Furthermore, the expressed protein exhibited 60% solubility, which could be partially attributed to its fusion with MBP. In the current study, the production of recombinant MccS was reported for the first time. The designed expression system proved to be efficient in producing the desired protein. Therefore, in future studies, it will be important to investigate the antibacterial and probiotic activity of MccS. Additionally, it may also act as an efficient biological preservative.

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Cite

BibTeXRIS
BibTeX
@article{dianatpur2026cloning,
  title = {{Cloning and heterologous expression of recombinant microcin S in Escherichia coli}},
  author = {Vahid Dianatpur and Seyed Shahram Shekarforoush and Abdollah Derakhshandeh and Azar Motamedi-Boroojeni and Vida Eraghi and Farhid Hemmatzadeh},
  journal = {Molecular Biology Research Communications},
  year = {2026},
  month = nov,
  doi = {10.22099/mbrc.2026.56252.2306},
  url = {https://doi.org/10.22099/mbrc.2026.56252.2306},
  note = {CC BY-NC 4.0},
}
RIS
TY  - JOUR
TI  - Cloning and heterologous expression of recombinant microcin S in Escherichia coli
AU  - Vahid Dianatpur
AU  - Seyed Shahram Shekarforoush
AU  - Abdollah Derakhshandeh
AU  - Azar Motamedi-Boroojeni
AU  - Vida Eraghi
AU  - Farhid Hemmatzadeh
PY  - 2026
DA  - 2026/11/04
JO  - Molecular Biology Research Communications
DO  - 10.22099/mbrc.2026.56252.2306
UR  - https://doi.org/10.22099/mbrc.2026.56252.2306
AB  - New antibacterial agents against antibiotic-resistant pathogens have clearly attracted global attention. Microcins, as peptide antibiotics, offer novel antimicrobial strategies for therapeutic uses. This study aimed to assess heterologous expression of recombinant microcin S (MccS) from Escherichia coli G3/10 in E. coli BL21 Star™ (DE3). The physicochemical properties of the MccS protein were analyzed using bioinformatics methods. The desired sequence of the MccS gene was optimized and synthesized in the pMAL-p5X expression vector, positioned downstream and in frame with the maltose-binding protein (MBP) coding sequence. Verification of recombinant protein expression in E. coli BL21 Star™ (DE3) was carried out using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Based on the results, the expression of MBP fusion MccS protein with a molecular weight of ~52.742 KDa was achieved in E. coli BL21 Star™ (DE3). Furthermore, the expressed protein exhibited 60% solubility, which could be partially attributed to its fusion with MBP. In the current study, the production of recombinant MccS was reported for the first time. The designed expression system proved to be efficient in producing the desired protein. Therefore, in future studies, it will be important to investigate the antibacterial and probiotic activity of MccS. Additionally, it may also act as an efficient biological preservative.
SN  - 2322-181X
SN  - 2345-2005
ER  -