Characterization of a pathway−specific activator of edeine biosynthesis and improved edeine production by its overexpression in Brevibacillus brevis

Abstract

Edeines are a group of non-ribosomal antibacterial peptides produced by Brevibacillus brevis. Due to the significant antibacterial properties of edeines, increasing edeine yield is of great interest in biomedical research. Herein, we identified that EdeB, a member of the ParB protein family, significantly improved edeine production in B. brevis. First, overexpression of edeB in B. brevis X23 increased edeine production by 92.27%. Second, in vitro bacteriostasis experiment showed that edeB-deletion mutant exhibited less antibacterial activity. Third, RT-qPCR assay demonstrated that the expression of edeA, edeQ, and edeK, which are key components of the edeine biosynthesis pathway, in edeB-deletion mutant X23(ΔedeB) was significantly lower than that in wild-type B. brevis strain X23. Finally, electrophoretic mobility shift assay (EMSA) showed that EdeB directly bound to the promoter region of the edeine biosynthetic gene cluster (ede BGC), suggesting that EdeB improves edeine production through interaction with ede BGC in B. brevis.

Brevibacillus brevis HNCS-1: a biocontrol bacterium against tea plant diseases

“…The main species of edeine in the HNCS-1 strain differ from Br. brevis X23 (Du et al, 2022 ), which may be owing to the evolutionary tree's distant genetic relationship.…”

Polyamine-containing natural products: structure, bioactivity, and biosynthesis

“…brevis X23 strain isolated from our lab, which produces 225 and 226 , can be used as a biocontrol agent to inhibit bacterial wilt in Solanaceae crops such as tobacco and chilli. 198,202,203…”

“…200,201 It is worth noting that the B. brevis X23 strain isolated from our lab, which produces 225 and 226, can be used as a biocontrol agent to inhibit bacterial wilt in Solanaceae crops such as tobacco and chilli. 198,202,203 Paenilamicins, which belong to linear cationic heptapeptidepolyamine antibiotics, were identied from the honey bee pathogen Paenibacillus larvae. 204 Paenilamicins include paenilamicins A1, A2, B1, and B2 (229)(230)(231)(232), which bear a unique backbone consisting of N-terminal galantinamic acid (i.e., 6,10-diamino-2,3,5-trihydroxydecanoic acid, Glm) or agmatinamic acid (i.e., 6-amino-9-guanidino-2,3,5-trihydroxynonanoic acid, Aga), Ala, N-methyl-diaminopropionic acid (mDap), Lys or Orn, galantinic acid (Gla), a second mDap, and Gly coupled with a Cterminal tail Spd.…”

“…Intriguingly, the process of assembling Put to the C-terminus of the peptide was predicted to be responsible by the gene Achr_39030, which may locate somewhere in the chromosome encoding a VibHlike protein or near the cro gene cluster encoding an Adomain bearing protein. 189 In addition, the deacylase CroM plays a vital role in enhancing the iron-chelating capacity, which was suggested to be involved in "activating" acyl-crochelin such as crochelins B-D (200)(201)(202) with the lower iron-chelating activity prior to extracellular exportion. 189 3.4 Biosynthesis of NRP-(PK)-PA hybrids 3.4.1 Glidonin biosynthesis.…”