Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums
Abstract Background Recently, researchers have focused on the search for alternatives to conventional antibiotics. Antimicrobial peptides are small bioactive peptides that regulate immune activation and have antibacterial activity with a reduced risk of bacterial resistance. Porcine myeloid antibact...
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| Format: | Article |
| Language: | English |
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BMC
2023-08-01
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| Series: | Microbial Cell Factories |
| Subjects: | |
| Online Access: | https://doi.org/10.1186/s12934-023-02164-5 |
| _version_ | 1797555548948791296 |
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| author | Chunming Dong Lijun Xu Weitao Lu Mengru Li Rui Zhang Yanyan Sun Jian Liu Xinlei Chu |
| author_facet | Chunming Dong Lijun Xu Weitao Lu Mengru Li Rui Zhang Yanyan Sun Jian Liu Xinlei Chu |
| author_sort | Chunming Dong |
| collection | DOAJ |
| description | Abstract Background Recently, researchers have focused on the search for alternatives to conventional antibiotics. Antimicrobial peptides are small bioactive peptides that regulate immune activation and have antibacterial activity with a reduced risk of bacterial resistance. Porcine myeloid antibacterial peptide 37 (PMAP-37) is a small-molecule peptide with broad-spectrum antibacterial activity isolated from pig bone marrow, and PMAP-37(F34-R) is its analogue. In this study, PMAP-37(F34-R) was recombinantly expressed in Pichia pastoris, and the recombinant peptide was further investigated for its antibacterial properties, mechanism and preservative in plums. Results To obtain a Pichia pastoris strain expressing PMAP-37(F34-R), we constructed a plasmid expressing recombinant PMAP-37(F34-R) (pPICZα-PMAP-37(F34-R)-A) and introduced it into Pichia pastoris. Finally, we obtained a highly active recombinant peptide, PMAP-37(F34-R), which inhibited the activity of both Gram-positive and Gram-negative bacteria. The minimum inhibitory concentration is 0.12–0.24 µg/mL, and it can destroy the integrity of the cell membrane, leading to cell lysis. It has good stability and is not easily affected by the external environment. Hemolysis experiments showed that 0.06 µg/mL-0.36 µg/mL PMAP-37(F34-R) had lower hemolysis ability to mammalian cells, and the hemolysis rate was below 1.5%. Additionally, 0.36 µg/mL PMAP-37(F34-R) showed a good preservative effect in plums. The decay and weight loss rates of the treated samples were significantly lower than those of the control group, and the respiratory intensity of the fruit was delayed in the experimental group. Conclusions In this study, we constructed a recombinant Pichia pastoris strain, which is a promising candidate for extending the shelf life of fruits and has potential applications in the development of new preservatives. Graphical Abstract |
| first_indexed | 2024-03-10T16:49:06Z |
| format | Article |
| id | doaj.art-c2beaf68c42548dfb9738b81350d80ec |
| institution | Directory Open Access Journal |
| issn | 1475-2859 |
| language | English |
| last_indexed | 2024-03-10T16:49:06Z |
| publishDate | 2023-08-01 |
| publisher | BMC |
| record_format | Article |
| series | Microbial Cell Factories |
| spelling | doaj.art-c2beaf68c42548dfb9738b81350d80ec2023-11-20T11:22:35ZengBMCMicrobial Cell Factories1475-28592023-08-0122111210.1186/s12934-023-02164-5Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plumsChunming Dong0Lijun Xu1Weitao Lu2Mengru Li3Rui Zhang4Yanyan Sun5Jian Liu6Xinlei Chu7College of Marine and Environmental Sciences, Tianjin University of Science and TechnologyCollege of Marine and Environmental Sciences, Tianjin University of Science and TechnologyCollege of Marine and Environmental Sciences, Tianjin University of Science and TechnologyCollege of Marine and Environmental Sciences, Tianjin University of Science and TechnologyCollege of Marine and Environmental Sciences, Tianjin University of Science and TechnologyJinan Deheng Medical Technology Co., LtdCollege of Agriculture and Bioengineering, Heze UniversityDepartment of Epidemiology and Biostatistics, Tianjin Medical University Cancer Institute and HospitalAbstract Background Recently, researchers have focused on the search for alternatives to conventional antibiotics. Antimicrobial peptides are small bioactive peptides that regulate immune activation and have antibacterial activity with a reduced risk of bacterial resistance. Porcine myeloid antibacterial peptide 37 (PMAP-37) is a small-molecule peptide with broad-spectrum antibacterial activity isolated from pig bone marrow, and PMAP-37(F34-R) is its analogue. In this study, PMAP-37(F34-R) was recombinantly expressed in Pichia pastoris, and the recombinant peptide was further investigated for its antibacterial properties, mechanism and preservative in plums. Results To obtain a Pichia pastoris strain expressing PMAP-37(F34-R), we constructed a plasmid expressing recombinant PMAP-37(F34-R) (pPICZα-PMAP-37(F34-R)-A) and introduced it into Pichia pastoris. Finally, we obtained a highly active recombinant peptide, PMAP-37(F34-R), which inhibited the activity of both Gram-positive and Gram-negative bacteria. The minimum inhibitory concentration is 0.12–0.24 µg/mL, and it can destroy the integrity of the cell membrane, leading to cell lysis. It has good stability and is not easily affected by the external environment. Hemolysis experiments showed that 0.06 µg/mL-0.36 µg/mL PMAP-37(F34-R) had lower hemolysis ability to mammalian cells, and the hemolysis rate was below 1.5%. Additionally, 0.36 µg/mL PMAP-37(F34-R) showed a good preservative effect in plums. The decay and weight loss rates of the treated samples were significantly lower than those of the control group, and the respiratory intensity of the fruit was delayed in the experimental group. Conclusions In this study, we constructed a recombinant Pichia pastoris strain, which is a promising candidate for extending the shelf life of fruits and has potential applications in the development of new preservatives. Graphical Abstracthttps://doi.org/10.1186/s12934-023-02164-5Antimicrobial peptidesAntibacterial mechanismPreservation |
| spellingShingle | Chunming Dong Lijun Xu Weitao Lu Mengru Li Rui Zhang Yanyan Sun Jian Liu Xinlei Chu Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums Microbial Cell Factories Antimicrobial peptides Antibacterial mechanism Preservation |
| title | Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums |
| title_full | Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums |
| title_fullStr | Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums |
| title_full_unstemmed | Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums |
| title_short | Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums |
| title_sort | antibacterial peptide pmap 37 f34 r expressed in pichia pastoris is effective against pathogenic bacteria and preserves plums |
| topic | Antimicrobial peptides Antibacterial mechanism Preservation |
| url | https://doi.org/10.1186/s12934-023-02164-5 |
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