Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i>
Antimicrobial peptides (AMPs) are present in a wide range of plants, animals, and microorganisms. Since AMPs are characterized by their effectiveness against emergent antibiotic-resistant bacteria, they are attracting attention as next-generation antimicrobial compounds that could solve the problem...
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MDPI AG
2024-02-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/12/2/412 |
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| author | So Shimoda Junya Ito Tasuke Ando Ryuta Tobe Kiyotaka Nakagawa Hiroshi Yoneyama |
| author_facet | So Shimoda Junya Ito Tasuke Ando Ryuta Tobe Kiyotaka Nakagawa Hiroshi Yoneyama |
| author_sort | So Shimoda |
| collection | DOAJ |
| description | Antimicrobial peptides (AMPs) are present in a wide range of plants, animals, and microorganisms. Since AMPs are characterized by their effectiveness against emergent antibiotic-resistant bacteria, they are attracting attention as next-generation antimicrobial compounds that could solve the problem of drug-resistant bacteria. Persulcatusin (IP), an antibacterial peptide derived from the hard tick <i>Ixodes persulcatus</i>, shows high antibacterial activity against various Gram- positive bacteria as well as multidrug-resistant bacteria. However, reports on the antibacterial action and resistance mechanisms of IP are scarce. In this study, we spontaneously generated mutants showing increased a minimum inhibitory concentration (MIC) of IP and analyzed their cross-resistance to other AMPs and antibiotics. We also used fluorescent probes to investigate the target of IP activity by evaluating IP-induced damage to the bacterial cytoplasmic membrane. Our findings suggest that the antimicrobial activity of IP on bacterial cytoplasmic membranes occurs via a mechanism of action different from that of known AMPs. Furthermore, we screened for mutants with high susceptibility to IP using a transposon mutant library and identified 16 genes involved in IP resistance. Our results indicate that IP, like other AMPs, depolarizes the bacterial cytoplasmic membrane, but it may also alter membrane structure and inhibit cell-wall synthesis. |
| first_indexed | 2024-03-07T22:20:07Z |
| format | Article |
| id | doaj.art-ad2f0bd46af34b79be8fbce585753eb0 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-07T22:20:07Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-ad2f0bd46af34b79be8fbce585753eb02024-02-23T15:28:28ZengMDPI AGMicroorganisms2076-26072024-02-0112241210.3390/microorganisms12020412Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i>So Shimoda0Junya Ito1Tasuke Ando2Ryuta Tobe3Kiyotaka Nakagawa4Hiroshi Yoneyama5Laboratory of Animal Microbiology, Department of Animal Science, Graduate School of Agricultural Science, Tohoku University, 468-1, Aramaki Aza Aoba, Aoba-ku, Sendai 980-0845, JapanLaboratory of Food and Biodynamic Chemistry, Graduate School of Agricultural Science, Tohoku University, 468-1, Aramaki Aza Aoba, Aoba-ku, Sendai 980-0845, JapanLaboratory of Animal Microbiology, Department of Animal Science, Graduate School of Agricultural Science, Tohoku University, 468-1, Aramaki Aza Aoba, Aoba-ku, Sendai 980-0845, JapanLaboratory of Animal Microbiology, Department of Animal Science, Graduate School of Agricultural Science, Tohoku University, 468-1, Aramaki Aza Aoba, Aoba-ku, Sendai 980-0845, JapanLaboratory of Food and Biodynamic Chemistry, Graduate School of Agricultural Science, Tohoku University, 468-1, Aramaki Aza Aoba, Aoba-ku, Sendai 980-0845, JapanLaboratory of Animal Microbiology, Department of Animal Science, Graduate School of Agricultural Science, Tohoku University, 468-1, Aramaki Aza Aoba, Aoba-ku, Sendai 980-0845, JapanAntimicrobial peptides (AMPs) are present in a wide range of plants, animals, and microorganisms. Since AMPs are characterized by their effectiveness against emergent antibiotic-resistant bacteria, they are attracting attention as next-generation antimicrobial compounds that could solve the problem of drug-resistant bacteria. Persulcatusin (IP), an antibacterial peptide derived from the hard tick <i>Ixodes persulcatus</i>, shows high antibacterial activity against various Gram- positive bacteria as well as multidrug-resistant bacteria. However, reports on the antibacterial action and resistance mechanisms of IP are scarce. In this study, we spontaneously generated mutants showing increased a minimum inhibitory concentration (MIC) of IP and analyzed their cross-resistance to other AMPs and antibiotics. We also used fluorescent probes to investigate the target of IP activity by evaluating IP-induced damage to the bacterial cytoplasmic membrane. Our findings suggest that the antimicrobial activity of IP on bacterial cytoplasmic membranes occurs via a mechanism of action different from that of known AMPs. Furthermore, we screened for mutants with high susceptibility to IP using a transposon mutant library and identified 16 genes involved in IP resistance. Our results indicate that IP, like other AMPs, depolarizes the bacterial cytoplasmic membrane, but it may also alter membrane structure and inhibit cell-wall synthesis.https://www.mdpi.com/2076-2607/12/2/412antimicrobial peptides<i>Staphylococcus aureus</i>persulcatusin |
| spellingShingle | So Shimoda Junya Ito Tasuke Ando Ryuta Tobe Kiyotaka Nakagawa Hiroshi Yoneyama Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i> Microorganisms antimicrobial peptides <i>Staphylococcus aureus</i> persulcatusin |
| title | Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i> |
| title_full | Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i> |
| title_fullStr | Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i> |
| title_full_unstemmed | Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i> |
| title_short | Identification of Genes Associated with Resistance to Persulcatusin, a Tick Defensin from <i>Ixodes persulcatus</i> |
| title_sort | identification of genes associated with resistance to persulcatusin a tick defensin from i ixodes persulcatus i |
| topic | antimicrobial peptides <i>Staphylococcus aureus</i> persulcatusin |
| url | https://www.mdpi.com/2076-2607/12/2/412 |
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