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Vibrio  sp. is the most serious pathogen in marine aquaculture, and the development of anti- Vibrio  agents is urgently needed. However, it is extreme lack of high-throughput screening (HTS) model for searching anti- Vibrio  compounds. Here, we established a protein-based HTS screening model to identify agents targeting peptide deformylase (PDF) of  Vibrio anguillarum . To find potential anti- Vibrio  compounds, crude extracts derived from marine actinomycetes were applied for screening with this model. Notably, crude extract of strain  Streptomyces  sp. NHF165 inhibited dramatically both on  V. anguillarum  PDF (VaPDF) activity and  V. anguillarum  cell growth. And actinonin was further identified as the functional component. Anti-VaPDF and anti- V. anguillarum  activities of actinonin were dose-dependent, and the IC 50  values were 6.94 and 2.85 μM, respectively. To understand the resistance of  V. anguillarum  against actinonin, spontaneous  V. anguillarum  mutants with resistance against actinonin were isolated. Surprisingly, for the resistant strains, the region between 774 and 852 base pairs was found to be absent in the gene  folD  which produces 10-formyl-tetrahydrofolate, a donor of  N -formyl to Met-tRNA fmet . When compared to the wild type strain, Δ folD  mutant showed eight times of minimum inhibition concentration on actinonin, however, the  folD  complementary strain could not grow on the medium supplemented with actinonin, which suggested that  folD  gene mutation was mainly responsible for the actinonin resistance. To our knowledge, this is the first report showing that marine derived  Streptomyces  sp. could produce actinonin with anti-VaPDF activity and the resistance against actinonin by  V. anguillarum  is mediated by mutation in  folD  gene.

The Inhibition and Resistance Mechanisms of Actinonin, Isolated from Marine Streptomyces sp. NHF165, against Vibrio anguillarum