A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear Plants
In this paper, peptide conjugates were designed and synthesized by incorporating the antimicrobial undecapeptide <b>BP16</b> at the C- or N-terminus of the plant defense elicitor peptide <b>flg15</b>, leading to <b>BP358</b> and <b>BP359</b>, respectiv...
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2021-06-01
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author | Pau Caravaca-Fuentes Cristina Camó Àngel Oliveras Aina Baró Jesús Francés Esther Badosa Marta Planas Lidia Feliu Emilio Montesinos Anna Bonaterra |
author_facet | Pau Caravaca-Fuentes Cristina Camó Àngel Oliveras Aina Baró Jesús Francés Esther Badosa Marta Planas Lidia Feliu Emilio Montesinos Anna Bonaterra |
author_sort | Pau Caravaca-Fuentes |
collection | DOAJ |
description | In this paper, peptide conjugates were designed and synthesized by incorporating the antimicrobial undecapeptide <b>BP16</b> at the C- or N-terminus of the plant defense elicitor peptide <b>flg15</b>, leading to <b>BP358</b> and <b>BP359</b>, respectively. The evaluation of their in vitro activity against six plant pathogenic bacteria revealed that <b>BP358</b> displayed MIC values between 1.6 and 12.5 μM, being more active than <b>flg15</b>, <b>BP16</b>, <b>BP359</b>, and an equimolar mixture of <b>BP16</b> and <b>flg15</b>. Moreover, <b>BP358</b> was neither hemolytic nor toxic to tobacco leaves. <b>BP358</b> triggered the overexpression of 6 out of the 11 plant defense-related genes tested. Interestingly, <b>BP358</b> inhibited <i>Erwinia amylovora</i> infections in pear plants, showing slightly higher efficacy than the mixture of <b>BP16</b> and <b>flg15</b>, and both treatments were as effective as the antibiotic kasugamycin. Thus, the bifunctional peptide conjugate <b>BP358</b> is a promising agent to control fire blight and possibly other plant bacterial diseases. |
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spelling | doaj.art-83fb8e2e9e7745fb9bbcb1174674961b2023-11-21T22:55:07ZengMDPI AGMolecules1420-30492021-06-012611342610.3390/molecules26113426A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear PlantsPau Caravaca-Fuentes0Cristina Camó1Àngel Oliveras2Aina Baró3Jesús Francés4Esther Badosa5Marta Planas6Lidia Feliu7Emilio Montesinos8Anna Bonaterra9LIPPSO, Department of Chemistry, Campus Montilivi, University of Girona, 17003 Girona, SpainLIPPSO, Department of Chemistry, Campus Montilivi, University of Girona, 17003 Girona, SpainLIPPSO, Department of Chemistry, Campus Montilivi, University of Girona, 17003 Girona, SpainLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, Campus Montilivi, University of Girona, 17003 Girona, SpainLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, Campus Montilivi, University of Girona, 17003 Girona, SpainLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, Campus Montilivi, University of Girona, 17003 Girona, SpainLIPPSO, Department of Chemistry, Campus Montilivi, University of Girona, 17003 Girona, SpainLIPPSO, Department of Chemistry, Campus Montilivi, University of Girona, 17003 Girona, SpainLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, Campus Montilivi, University of Girona, 17003 Girona, SpainLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, Campus Montilivi, University of Girona, 17003 Girona, SpainIn this paper, peptide conjugates were designed and synthesized by incorporating the antimicrobial undecapeptide <b>BP16</b> at the C- or N-terminus of the plant defense elicitor peptide <b>flg15</b>, leading to <b>BP358</b> and <b>BP359</b>, respectively. The evaluation of their in vitro activity against six plant pathogenic bacteria revealed that <b>BP358</b> displayed MIC values between 1.6 and 12.5 μM, being more active than <b>flg15</b>, <b>BP16</b>, <b>BP359</b>, and an equimolar mixture of <b>BP16</b> and <b>flg15</b>. Moreover, <b>BP358</b> was neither hemolytic nor toxic to tobacco leaves. <b>BP358</b> triggered the overexpression of 6 out of the 11 plant defense-related genes tested. Interestingly, <b>BP358</b> inhibited <i>Erwinia amylovora</i> infections in pear plants, showing slightly higher efficacy than the mixture of <b>BP16</b> and <b>flg15</b>, and both treatments were as effective as the antibiotic kasugamycin. Thus, the bifunctional peptide conjugate <b>BP358</b> is a promising agent to control fire blight and possibly other plant bacterial diseases.https://www.mdpi.com/1420-3049/26/11/3426fire blightantimicrobial peptidesplant-defense elicitorspeptide conjugate |
spellingShingle | Pau Caravaca-Fuentes Cristina Camó Àngel Oliveras Aina Baró Jesús Francés Esther Badosa Marta Planas Lidia Feliu Emilio Montesinos Anna Bonaterra A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear Plants Molecules fire blight antimicrobial peptides plant-defense elicitors peptide conjugate |
title | A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear Plants |
title_full | A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear Plants |
title_fullStr | A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear Plants |
title_full_unstemmed | A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear Plants |
title_short | A Bifunctional Peptide Conjugate That Controls Infections of <i>Erwinia amylovora</i> in Pear Plants |
title_sort | bifunctional peptide conjugate that controls infections of i erwinia amylovora i in pear plants |
topic | fire blight antimicrobial peptides plant-defense elicitors peptide conjugate |
url | https://www.mdpi.com/1420-3049/26/11/3426 |
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