The
need to increase agricultural yield has led to an extensive
use of antibiotics against plant pathogens, which has resulted in
the emergence of resistant strains. Therefore, there is an increasing
demand for new methods, preferably with lower chances of developing
resistant strains and a lower risk to the environment or public health.
Many Gram-negative bacterial pathogens use quorum sensing, a population-density-dependent
regulatory mechanism, to monitor the secretion of N-acyl-homoserine lactones (AHLs) and pathogenicity. Therefore, quorum
sensing represents an attractive antivirulence target. AHL lactonases
hydrolyze AHLs and have potential antibacterial properties; however,
their use is limited by thermal instability and durability, or low
activity. Here, we demonstrate that an AHL lactonase from the phosphotriesterase-like
lactonase family exhibits high activity with the AHL secreted from
the plant pathogen Erwinia amylovora and attenuates infection in planta. Using directed
enzyme evolution, we were able to increase the enzyme’s temperature
resistance (T
50, the temperature at which
50% of the activity is retained) by 8 °C. Then, by performing
enzyme encapsulation in nanospherical capsules composed of tertbutoxycarbonyl-Phe-Phe-OH
peptide, the shelf life was extended for more than 5 weeks. Furthermore,
the encapsulated and free mutant were able to significantly inhibit
up to 70% blossom’s infection in the field, achieving the same
efficacy as seen with antibiotics commonly used today to treat the
plant pathogen. We conclude that specific AHL lactonase can inhibit E. amylovora infection in the field, as it degrades
the AHL secreted by this plant pathogen. The combination of directed
enzyme evolution and peptide nanostructure encapsulation significantly
improved the thermal resistance and shelf life of the enzyme, respectively,
increasing its potential in future development as antibacterial treatment.
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