Abstract
Both donors and acceptors of communication-mediating (COM) domains are essential for coordinating intermolecular communication within nonribosomal peptides synthetases (NRPSs) complexes. Different sets of COM domains provide selectivity, allowing NRPSs to utilize different natural biosynthetic templates. In this study, novel lipopeptides were synthesized by reprogramming the plipastatin biosynthetic machinery. A Thr-to-Asp point mutation was sufficient to shift the selectivity of the donor COM domain of ppsB toward that of ppsD. Deletion and/or interchangeability established donor and acceptor function. Variations in acceptor COM domain did not result in novel product formation in the presence of its partner donor, whereas plipastatin formation was completely abrogated by altering donor modules. Five novel lipopeptides (cyclic pentapeptide, linear hexapeptide, nonapeptide, heptapeptide, and cyclic octapeptide) were identified and verified by high-resolution LC-ESI-MS/MS. In addition, we demonstrated the potential to generate novel strains with the antimicrobial activity by selecting compatible COM domains, and the novel lipopeptides exhibited antimicrobial activity against five of the fungal species at a contention of 31.25–125 μg/ml.
Highlights
Bacillus subtilis is a Gram-positive bacterium that produces broad spectrum amphiphilic lipopeptides with excellent biosurfactant properties and antifungal, antibacterial and antiviral activities (Marahiel et al, 1997; Schwarzer et al, 2003; Batool et al, 2011)
The goal of this study was to investigate the influence on protein–protein communication based on the converting donor and acceptor of COM domains sequences, which maintain or prevent the selective interaction between partner nonribosomal peptides synthetases (NRPSs), the influence on the novel lipopeptides formation
We evaluated the impact of COMDppsB point mutants on lipopeptide biosynthesis
Summary
Bacillus subtilis is a Gram-positive bacterium that produces broad spectrum amphiphilic lipopeptides with excellent biosurfactant properties and antifungal, antibacterial and antiviral activities (Marahiel et al, 1997; Schwarzer et al, 2003; Batool et al, 2011). Iturins (Hiradate et al, 2002; Yu et al, 2002; Jin et al, 2014), fengycins (Vanittanakom et al, 1986; Guo et al, 2014) and surfactins (Bonmatin et al, 2003; Liu et al, 2015) are the three most well-known families of lipopeptides, which produced by Bacilli. All of them are synthesized by nonribosomal peptide synthetases via a thioesterase chain release mechanism (Tosato et al, 1997; Finking and Marahiel, 2004; Calcott and Ackerley, 2014). The fengycin is identical compounds to plipastatin that display slightly structural variations at different salty conditions (Honma et al, 2012).
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