Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1
Plant defensins have attracted much attention in the development of new antimicrobials. Yet the elucidation of their modes of action against bacterial pathogens is still incipient. The available recombinant systems to obtain plant defensin mutants with enhanced or optimized antibacterial activity ma...
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Polish Academy of Sciences
2024-10-01
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| Series: | Journal of Plant Protection Research |
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| Online Access: | https://journals.pan.pl/Content/133852/PDF/OA_2_JPPR_64_4_1915_Perez.pdf |
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| author | Gilberto Andrés Muñoz-Pérez Francisco A. Guillén-Chable Gerardo Corzo Ivan Arenas-Sosa Lucila A. Sánchez-Cach Georgina Estrada |
| author_facet | Gilberto Andrés Muñoz-Pérez Francisco A. Guillén-Chable Gerardo Corzo Ivan Arenas-Sosa Lucila A. Sánchez-Cach Georgina Estrada |
| author_sort | Gilberto Andrés Muñoz-Pérez |
| collection | DOAJ |
| description | Plant defensins have attracted much attention in the development of new antimicrobials. Yet the elucidation of their modes of action against bacterial pathogens is still incipient. The available recombinant systems to obtain plant defensin mutants with enhanced or optimized antibacterial activity may help to accelerate the knowledge of their action mechanisms and their applications against pathogens. In this work, the point mutant defensin K45E (J1-1_K45E) was obtained by the same recombinant system as J1-1 defensin. The characterized peptide conserved antibacterial activity against the gram-negative Pseudomonas aeruginosa and showed a dose improvement relative to J1-1. Furthermore, the mutant J1-1_K45E exhibited a gain in function against the gram-positive Staphylococcus aureus. Finally, to correlate structural changes and antibacterial activity, two properties involved in defensins’ modes of action were measured. First, the mutant J1-1_K45E which oligomerizes in a distinct pattern was compared with J1-1 and secondly, J1-1_K45E shows a distinct lipid binding profile because it binds preferentially to phosphatidylserine. Together, our findings support the idea that amino acid sequence variability in plant defensins superfamily can generate major functional changes, and highlight the relevant role of charged residues, beyond the g-core loop, in the improvement of J1-1 antibacterial activity. |
| format | Article |
| id | doaj-art-e0396e69f5ed4ab5960d46cf2e1331aa |
| institution | Kabale University |
| issn | 1427-4345 1899-007X |
| language | English |
| publishDate | 2024-10-01 |
| publisher | Polish Academy of Sciences |
| record_format | Article |
| series | Journal of Plant Protection Research |
| spelling | doaj-art-e0396e69f5ed4ab5960d46cf2e1331aa2025-01-10T14:11:06ZengPolish Academy of SciencesJournal of Plant Protection Research1427-43451899-007X2024-10-01vol. 64No 4https://doi.org/10.24425/jppr.2024.151817Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1Gilberto Andrés Muñoz-Pérez0Francisco A. Guillén-Chable1Gerardo Corzo2Ivan Arenas-Sosa3Lucila A. Sánchez-Cach4Georgina Estrada5https://orcid.org/0000-0002-1492-4672Unidad de Biología Integrativa, Centro de Investigación Científica de Yucatán, A.C., Yucatán, MexicoFacultad de Ciencias, Universidad Nacional Autónoma de México, Unidad Multidisciplinaria de Docencia e Investigación, UMIDI-Sisal, MexicoInstituto de Biotecnología, Universidad Nacional Autónoma de México, MexicoInstituto de Biotecnología, Universidad Nacional Autónoma de México, MexicoUnidad de Biología Integrativa, Centro de Investigación Científica de Yucatán, A.C., Yucatán, MexicoUnidad de Biología Integrativa, Centro de Investigación Científica de Yucatán, A.C., Yucatán, MexicoPlant defensins have attracted much attention in the development of new antimicrobials. Yet the elucidation of their modes of action against bacterial pathogens is still incipient. The available recombinant systems to obtain plant defensin mutants with enhanced or optimized antibacterial activity may help to accelerate the knowledge of their action mechanisms and their applications against pathogens. In this work, the point mutant defensin K45E (J1-1_K45E) was obtained by the same recombinant system as J1-1 defensin. The characterized peptide conserved antibacterial activity against the gram-negative Pseudomonas aeruginosa and showed a dose improvement relative to J1-1. Furthermore, the mutant J1-1_K45E exhibited a gain in function against the gram-positive Staphylococcus aureus. Finally, to correlate structural changes and antibacterial activity, two properties involved in defensins’ modes of action were measured. First, the mutant J1-1_K45E which oligomerizes in a distinct pattern was compared with J1-1 and secondly, J1-1_K45E shows a distinct lipid binding profile because it binds preferentially to phosphatidylserine. Together, our findings support the idea that amino acid sequence variability in plant defensins superfamily can generate major functional changes, and highlight the relevant role of charged residues, beyond the g-core loop, in the improvement of J1-1 antibacterial activity.https://journals.pan.pl/Content/133852/PDF/OA_2_JPPR_64_4_1915_Perez.pdfantibacterial defensingram-positive bacteriagram-negative bacteriapeptide-lipid interactionspolyclonal antibodies |
| spellingShingle | Gilberto Andrés Muñoz-Pérez Francisco A. Guillén-Chable Gerardo Corzo Ivan Arenas-Sosa Lucila A. Sánchez-Cach Georgina Estrada Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1 Journal of Plant Protection Research antibacterial defensin gram-positive bacteria gram-negative bacteria peptide-lipid interactions polyclonal antibodies |
| title | Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1 |
| title_full | Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1 |
| title_fullStr | Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1 |
| title_full_unstemmed | Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1 |
| title_short | Antibacterial activity improvement in a point mutant K45E of the pepper defensin J1-1 |
| title_sort | antibacterial activity improvement in a point mutant k45e of the pepper defensin j1 1 |
| topic | antibacterial defensin gram-positive bacteria gram-negative bacteria peptide-lipid interactions polyclonal antibodies |
| url | https://journals.pan.pl/Content/133852/PDF/OA_2_JPPR_64_4_1915_Perez.pdf |
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