High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activity
Antibacterial peptides are endogenous polypeptides produced by multicellular organisms to protect the host against pathogenic microbes, they show broad spectrum antimicrobial activities against various microorganisms and possess low propensity for developing resistance. The purpose of this study is...
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Frontiers Media S.A.
2023-06-01
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Series: | Frontiers in Microbiology |
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Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1153365/full |
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author | Xufeng Dong Hu Shan Shubai Wang Zhengjun Jiang Shaojuan Wang Zhihua Qin |
author_facet | Xufeng Dong Hu Shan Shubai Wang Zhengjun Jiang Shaojuan Wang Zhihua Qin |
author_sort | Xufeng Dong |
collection | DOAJ |
description | Antibacterial peptides are endogenous polypeptides produced by multicellular organisms to protect the host against pathogenic microbes, they show broad spectrum antimicrobial activities against various microorganisms and possess low propensity for developing resistance. The purpose of this study is to develop recombinant antibacterial peptide cathelicidin-BF by genetic engineering and protein engineering technology, and study its antibacterial activity in vitro and in vivo, so as to provide reference for the production and application of recombinant antibacterial peptide cathelicidin-BF. In this study, on account of Pichia pastoris eukaryotic expression system, we expressed and prepared antibacterial peptide cathelicidin-BF. Then, the minimum inhibitory concentration of antibacterial peptide cathelicidin-BF and the comparison with the antibacterial activity of antibiotics were determined through the antibacterial experiment in vitro. Chickens as infection model were used to verify the antibacterial peptide activity in vivo. The results show that the bacteriostatic ability of antibacterial peptide cathelicidin-BF is similar to that of antibiotics in certain concentration, and can reach the treatment level of antibiotics. Although the mode of administration of antibacterial peptide is still limited, this study can provide reference for the future research of antibacterial peptide. |
first_indexed | 2024-03-13T06:35:55Z |
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id | doaj.art-5701defe3d494b66b7245559bb84d199 |
institution | Directory Open Access Journal |
issn | 1664-302X |
language | English |
last_indexed | 2024-03-13T06:35:55Z |
publishDate | 2023-06-01 |
publisher | Frontiers Media S.A. |
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series | Frontiers in Microbiology |
spelling | doaj.art-5701defe3d494b66b7245559bb84d1992023-06-09T04:52:32ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2023-06-011410.3389/fmicb.2023.11533651153365High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activityXufeng Dong0Hu Shan1Shubai Wang2Zhengjun Jiang3Shaojuan Wang4Zhihua Qin5College of Veterinary Medicine, Qingdao Agricultural University, Qingdao, Shandong, ChinaCollege of Veterinary Medicine, Qingdao Agricultural University, Qingdao, Shandong, ChinaCollege of Animal Science and Technology, Qingdao Agricultural University, Qingdao, Shandong, ChinaShandong Hwatson Biochem Co. Ltd, Weifang, Shandong, ChinaShandong Hwatson Biochem Co. Ltd, Weifang, Shandong, ChinaCollege of Veterinary Medicine, Qingdao Agricultural University, Qingdao, Shandong, ChinaAntibacterial peptides are endogenous polypeptides produced by multicellular organisms to protect the host against pathogenic microbes, they show broad spectrum antimicrobial activities against various microorganisms and possess low propensity for developing resistance. The purpose of this study is to develop recombinant antibacterial peptide cathelicidin-BF by genetic engineering and protein engineering technology, and study its antibacterial activity in vitro and in vivo, so as to provide reference for the production and application of recombinant antibacterial peptide cathelicidin-BF. In this study, on account of Pichia pastoris eukaryotic expression system, we expressed and prepared antibacterial peptide cathelicidin-BF. Then, the minimum inhibitory concentration of antibacterial peptide cathelicidin-BF and the comparison with the antibacterial activity of antibiotics were determined through the antibacterial experiment in vitro. Chickens as infection model were used to verify the antibacterial peptide activity in vivo. The results show that the bacteriostatic ability of antibacterial peptide cathelicidin-BF is similar to that of antibiotics in certain concentration, and can reach the treatment level of antibiotics. Although the mode of administration of antibacterial peptide is still limited, this study can provide reference for the future research of antibacterial peptide.https://www.frontiersin.org/articles/10.3389/fmicb.2023.1153365/fullantimicrobial peptideseukaryotic expressionbacteriostatic effectin vitro activityin vivo activity |
spellingShingle | Xufeng Dong Hu Shan Shubai Wang Zhengjun Jiang Shaojuan Wang Zhihua Qin High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activity Frontiers in Microbiology antimicrobial peptides eukaryotic expression bacteriostatic effect in vitro activity in vivo activity |
title | High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activity |
title_full | High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activity |
title_fullStr | High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activity |
title_full_unstemmed | High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activity |
title_short | High expression of antimicrobial peptides cathelicidin-BF in Pichia pastoris and verification of its activity |
title_sort | high expression of antimicrobial peptides cathelicidin bf in pichia pastoris and verification of its activity |
topic | antimicrobial peptides eukaryotic expression bacteriostatic effect in vitro activity in vivo activity |
url | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1153365/full |
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