Potent Chimeric Antimicrobial Derivatives of the Medicago truncatula NCR247 Symbiotic Peptide

作者：Sándor Jenei, Hilda Tiricz, János Szolomájer, Edit Tímár, Éva Klement, Mohamad Anas Al Bouni, Rui M. Lima, D Kata, Mária Harmati, Krisztina Buzás, Imre Földesi, Gábor Tóth, Gabriella Endré, Éva Kondorosi · 发表于：Frontiers in Microbiology · 年份：2020 · DOI：10.3389/fmicb.2020.00270 · 被引用次数：36 · 研究领域：Legume Nitrogen Fixing Symbiosis、Biochemical and Structural Characterization、Antimicrobial Peptides and Activities

In Rhizobium-legume symbiosis, the bacteria are converted into nitrogen-fixing bacteroids. In many legume species, differentiation of the endosymbiotic bacteria is irreversible, culminating in definitive loss of their cell division ability. This terminal differentiation is mediated by plant peptides produced in the symbiotic cells. In Medicago truncatula more than ∼700 nodule-specific cysteine-rich (NCR) peptides are involved in this process. We have shown previously that NCR247 and NCR335 have strong antimicrobial activity on various pathogenic bacteria and identified interaction of NCR247 with many bacterial proteins, including FtsZ and several ribosomal proteins, which prevent bacterial cell division and protein synthesis. In this study we designed and synthetized various derivatives of NCR247, including shorter fragments and various chimeric derivatives. The antimicrobial activity of these peptides was tested on the ESKAPE bacteria; Enterococcus faecalis, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa and Escherichia coli as a member of Enterobacteriaceae and in addition Listeria monocytogenes and Salmonella enterica. The 12 amino acid long C-terminal half of NCR247, NCR247C partially retained the antimicrobial activity and preserved the multitarget interactions with partners of NCR247. Nevertheless NCR247C became ineffective on S. aureus, P. aeruginosa and L. monocytogenes. The chimeric derivatives obtained by fusion of NCR2...