4.6 Article

A Synergic Potential of Antimicrobial Peptides against Pseudomonas syringae pv. actinidiae

Journal

MOLECULES
Volume 26, Issue 5, Pages -

Publisher

MDPI
DOI: 10.3390/molecules26051461

Keywords

3; 1; Actinidia sp; antimicrobial peptides; bacterial canker of kiwifruit; BP100; CA-M; Dhvar-5; Pseudomonas syringae pv; actinidiae; RW-BP100

Funding

  1. Fundacao para a Ciencia e Tecnologia (FCT)
  2. FEDER Fundo Europeu de Desenvolvimento Regional funds through the COMPETE 2020-Operacional Programme for Competitiveness and Internationalization (POCI) [UIDB/50006/2020]
  3. Fundo Europeu de Desenvolvimento Regional (FEDER) through the Programa Operacional Regional do Norte (NORTE2020) [NORTE-01-0247-FEDER-033647]
  4. European Union's Horizon 2020 Research and Innovation Programme [857251]
  5. [SFRH/BD/138187/2018]
  6. [PTDC/BAA-AGR/31798/2017 (POCI-01-0145-FEDER31798)]

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Pseudomonas syringae pv. actinidiae (Psa) is the pathogen responsible for bacterial canker of kiwifruit, causing significant production losses. Despite the lack of effective treatments for this disease, this study found that BP100 and CA-M have strong inhibitory and bactericidal effects against Psa, with peptide 3.1 showing faster membrane permeation. Additionally, the mixture of AMPs BP100:3.1 demonstrated high efficiency in reducing Psa viability at low concentrations.
Pseudomonas syringae pv. actinidiae (Psa) is the pathogenic agent responsible for the bacterial canker of kiwifruit (BCK) leading to major losses in kiwifruit productions. No effective treatments and measures have yet been found to control this disease. Despite antimicrobial peptides (AMPs) having been successfully used for the control of several pathogenic bacteria, few studies have focused on the use of AMPs against Psa. In this study, the potential of six AMPs (BP100, RW-BP100, CA-M, 3.1, D4E1, and Dhvar-5) to control Psa was investigated. The minimal inhibitory and bactericidal concentrations (MIC and MBC) were determined and membrane damaging capacity was evaluated by flow cytometry analysis. Among the tested AMPs, the higher inhibitory and bactericidal capacity was observed for BP100 and CA-M with MIC of 3.4 and 3.4-6.2 mu M, respectively and MBC 3.4-10 mu M for both. Flow cytometry assays suggested a faster membrane permeation for peptide 3.1, in comparison with the other AMPs studied. Peptide mixtures were also tested, disclosing the high efficiency of BP100:3.1 at low concentration to reduce Psa viability. These results highlight the potential interest of AMP mixtures against Psa, and 3.1 as an antimicrobial molecule that can improve other treatments in synergic action.

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