Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses
The rapid evolution of highly infectious pathogens is a major threat to global public health. In the front line of defense against bacteria, fungi, and viruses, antimicrobial peptides (AMPs) are naturally produced by all living organisms and offer new possibilities for next-generation antibiotic dev...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-05-01
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| Series: | Frontiers in Immunology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fimmu.2022.851642/full |
| _version_ | 1817987428502208512 |
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| author | Rongrong Liu Ziyu Liu Haoran Peng Yunhua Lv Yunan Feng Junjun Kang Naining Lu Ruixue Ma Shiyuan Hou Wenjie Sun Qikang Ying Fang Wang Qikang Gao Ping Zhao Cheng Zhu Yixing Wang Xingan Wu |
| author_facet | Rongrong Liu Ziyu Liu Haoran Peng Yunhua Lv Yunan Feng Junjun Kang Naining Lu Ruixue Ma Shiyuan Hou Wenjie Sun Qikang Ying Fang Wang Qikang Gao Ping Zhao Cheng Zhu Yixing Wang Xingan Wu |
| author_sort | Rongrong Liu |
| collection | DOAJ |
| description | The rapid evolution of highly infectious pathogens is a major threat to global public health. In the front line of defense against bacteria, fungi, and viruses, antimicrobial peptides (AMPs) are naturally produced by all living organisms and offer new possibilities for next-generation antibiotic development. However, the low yields and difficulties in the extraction and purification of AMPs have hindered their industry and scientific research applications. To overcome these barriers, we enabled high expression of bomidin, a commercial recombinant AMP based upon bovine myeloid antimicrobial peptide-27. This novel AMP, which can be expressed in Escherichia coli by adding methionine to the bomidin sequence, can be produced in bulk and is more biologically active than chemically synthesized AMPs. We verified the function of bomidin against a variety of bacteria and enveloped viruses, including severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), herpes simplex virus (HSV), dengue virus (DENV), and chikungunya virus (CHIKV). Furthermore, based on the molecular modeling of bomidin and membrane lipids, we elucidated the possible mechanism by which bomidin disrupts bacterial and viral membranes. Thus, we obtained a novel AMP with an optimized, efficient heterologous expression system for potential therapeutic application against a wide range of life-threatening pathogens. |
| first_indexed | 2024-04-14T00:22:11Z |
| format | Article |
| id | doaj.art-d5bee77d1fd141769b104baa36993488 |
| institution | Directory Open Access Journal |
| issn | 1664-3224 |
| language | English |
| last_indexed | 2024-04-14T00:22:11Z |
| publishDate | 2022-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Immunology |
| spelling | doaj.art-d5bee77d1fd141769b104baa369934882022-12-22T02:22:55ZengFrontiers Media S.A.Frontiers in Immunology1664-32242022-05-011310.3389/fimmu.2022.851642851642Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped VirusesRongrong Liu0Ziyu Liu1Haoran Peng2Yunhua Lv3Yunan Feng4Junjun Kang5Naining Lu6Ruixue Ma7Shiyuan Hou8Wenjie Sun9Qikang Ying10Fang Wang11Qikang Gao12Ping Zhao13Cheng Zhu14Yixing Wang15Xingan Wu16Department of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, Second Military Medical University, Shanghai, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Neurobiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Neurobiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaAnalysis Center of Agrobiology and Environmental Sciences, Zhejiang University, Hangzhou, ChinaDepartment of Microbiology, Second Military Medical University, Shanghai, ChinaTianjin Key Laboratory of Function and Application of Biological Macromolecular Structures, School of Life Sciences, Tianjin University, Tianjin, ChinaJiangsu Genloci Biotech Inc., Nanjing, ChinaDepartment of Microbiology, School of Basic Medicine, Fourth Military Medical University, Xi’an, ChinaThe rapid evolution of highly infectious pathogens is a major threat to global public health. In the front line of defense against bacteria, fungi, and viruses, antimicrobial peptides (AMPs) are naturally produced by all living organisms and offer new possibilities for next-generation antibiotic development. However, the low yields and difficulties in the extraction and purification of AMPs have hindered their industry and scientific research applications. To overcome these barriers, we enabled high expression of bomidin, a commercial recombinant AMP based upon bovine myeloid antimicrobial peptide-27. This novel AMP, which can be expressed in Escherichia coli by adding methionine to the bomidin sequence, can be produced in bulk and is more biologically active than chemically synthesized AMPs. We verified the function of bomidin against a variety of bacteria and enveloped viruses, including severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), herpes simplex virus (HSV), dengue virus (DENV), and chikungunya virus (CHIKV). Furthermore, based on the molecular modeling of bomidin and membrane lipids, we elucidated the possible mechanism by which bomidin disrupts bacterial and viral membranes. Thus, we obtained a novel AMP with an optimized, efficient heterologous expression system for potential therapeutic application against a wide range of life-threatening pathogens.https://www.frontiersin.org/articles/10.3389/fimmu.2022.851642/fullantimicrobial peptideAVPSARS-CoV-2HSV-2DENV-2CHIKV |
| spellingShingle | Rongrong Liu Ziyu Liu Haoran Peng Yunhua Lv Yunan Feng Junjun Kang Naining Lu Ruixue Ma Shiyuan Hou Wenjie Sun Qikang Ying Fang Wang Qikang Gao Ping Zhao Cheng Zhu Yixing Wang Xingan Wu Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses Frontiers in Immunology antimicrobial peptide AVP SARS-CoV-2 HSV-2 DENV-2 CHIKV |
| title | Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses |
| title_full | Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses |
| title_fullStr | Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses |
| title_full_unstemmed | Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses |
| title_short | Bomidin: An Optimized Antimicrobial Peptide With Broad Antiviral Activity Against Enveloped Viruses |
| title_sort | bomidin an optimized antimicrobial peptide with broad antiviral activity against enveloped viruses |
| topic | antimicrobial peptide AVP SARS-CoV-2 HSV-2 DENV-2 CHIKV |
| url | https://www.frontiersin.org/articles/10.3389/fimmu.2022.851642/full |
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