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Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide
The search for effective and bioactive antimicrobial molecules to encounter the medical need for new antibiotics is an encouraging area of research. Plant defensins are small cationic, cysteine-rich peptides with a stabilized tertiary structure by disulfide-bridges and characterized by a wide range...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7688885/ https://www.ncbi.nlm.nih.gov/pubmed/33237335 http://dx.doi.org/10.1186/s13568-020-01146-9 |
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author | Al Kashgry, Najla Amin T. Abulreesh, Hussein H. El-Sheikh, Iman A. Almaroai, Yaser A. Salem, Reda Mohamed, Ismail Waly, Fatma R. Osman, Gamal Mohamed, Mahmoud S. M. |
author_facet | Al Kashgry, Najla Amin T. Abulreesh, Hussein H. El-Sheikh, Iman A. Almaroai, Yaser A. Salem, Reda Mohamed, Ismail Waly, Fatma R. Osman, Gamal Mohamed, Mahmoud S. M. |
author_sort | Al Kashgry, Najla Amin T. |
collection | PubMed |
description | The search for effective and bioactive antimicrobial molecules to encounter the medical need for new antibiotics is an encouraging area of research. Plant defensins are small cationic, cysteine-rich peptides with a stabilized tertiary structure by disulfide-bridges and characterized by a wide range of biological functions. The heterologous expression of Egyptian maize defensin (MzDef) in Escherichia coli and subsequent purification by glutathione affinity chromatography yielded 2 mg/L of recombinant defensin peptide. The glutathione-S-transferase (GST)-tagged MzDef of approximately 30 kDa in size (26 KDa GST + ~ 4 KDa MzDef peptide) was immunodetected with anti-GST antibodies. The GST-tag was successfully cleaved from the MzDef peptide by thrombin, and the removal was validated by the Tris-Tricine gel electrophoresis. The MzDef induced strong growth inhibition of Rhizoctonia solani, Fusarium verticillioides, and Aspergillus niger by 94.23%, 93.34%, and 86.25%, respectively, whereas relatively weak growth inhibitory activity of 35.42% against Fusarium solani was recorded. Moreover, strong antibacterial activities were demonstrated against E. coli and Bacillus cereus and the moderate activities against Salmonella enterica and Staphylococcus aureus at all tested concentrations (0.1, 0.2, 0.4, 0.8, 1.6, and 3.2 µM). Furthermore, the in vitro MTT assay exhibited promising anticancer activity against all tested cell lines (hepatocellular carcinoma, mammary gland breast cancer, and colorectal carcinoma colon cancer) with IC(50) values ranging from 14.85 to 29.85 µg/mL. These results suggest that the recombinant peptide MzDef may serve as a potential alternative antimicrobial and anticancer agent to be used in medicinal application. |
format | Online Article Text |
id | pubmed-7688885 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-76888852020-11-30 Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide Al Kashgry, Najla Amin T. Abulreesh, Hussein H. El-Sheikh, Iman A. Almaroai, Yaser A. Salem, Reda Mohamed, Ismail Waly, Fatma R. Osman, Gamal Mohamed, Mahmoud S. M. AMB Express Original Article The search for effective and bioactive antimicrobial molecules to encounter the medical need for new antibiotics is an encouraging area of research. Plant defensins are small cationic, cysteine-rich peptides with a stabilized tertiary structure by disulfide-bridges and characterized by a wide range of biological functions. The heterologous expression of Egyptian maize defensin (MzDef) in Escherichia coli and subsequent purification by glutathione affinity chromatography yielded 2 mg/L of recombinant defensin peptide. The glutathione-S-transferase (GST)-tagged MzDef of approximately 30 kDa in size (26 KDa GST + ~ 4 KDa MzDef peptide) was immunodetected with anti-GST antibodies. The GST-tag was successfully cleaved from the MzDef peptide by thrombin, and the removal was validated by the Tris-Tricine gel electrophoresis. The MzDef induced strong growth inhibition of Rhizoctonia solani, Fusarium verticillioides, and Aspergillus niger by 94.23%, 93.34%, and 86.25%, respectively, whereas relatively weak growth inhibitory activity of 35.42% against Fusarium solani was recorded. Moreover, strong antibacterial activities were demonstrated against E. coli and Bacillus cereus and the moderate activities against Salmonella enterica and Staphylococcus aureus at all tested concentrations (0.1, 0.2, 0.4, 0.8, 1.6, and 3.2 µM). Furthermore, the in vitro MTT assay exhibited promising anticancer activity against all tested cell lines (hepatocellular carcinoma, mammary gland breast cancer, and colorectal carcinoma colon cancer) with IC(50) values ranging from 14.85 to 29.85 µg/mL. These results suggest that the recombinant peptide MzDef may serve as a potential alternative antimicrobial and anticancer agent to be used in medicinal application. Springer Berlin Heidelberg 2020-11-25 /pmc/articles/PMC7688885/ /pubmed/33237335 http://dx.doi.org/10.1186/s13568-020-01146-9 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Original Article Al Kashgry, Najla Amin T. Abulreesh, Hussein H. El-Sheikh, Iman A. Almaroai, Yaser A. Salem, Reda Mohamed, Ismail Waly, Fatma R. Osman, Gamal Mohamed, Mahmoud S. M. Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide |
title | Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide |
title_full | Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide |
title_fullStr | Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide |
title_full_unstemmed | Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide |
title_short | Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide |
title_sort | utilization of a recombinant defensin from maize (zea mays l.) as a potential antimicrobial peptide |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7688885/ https://www.ncbi.nlm.nih.gov/pubmed/33237335 http://dx.doi.org/10.1186/s13568-020-01146-9 |
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