Plant defensin antibacterial mode of action against Pseudomonas species
Plant defensin antibacterial mode of action against Pseudomonas species
复制标题
DOI:
10.1186/s12866-020-01852-1
复制
发表时间:
2020-06-19
期刊:
影响因子:
4.2
通讯作者:
Samac, Deborah A.
中科院分区:
文献类型:
--
作者:
Sathoff, Andrew E.;Lewenza, Shawn;Samac, Deborah A.
Background Though many plant defensins exhibit antibacterial activity, little is known about their antibacterial mode of action (MOA). Antimicrobial peptides with a characterized MOA induce the expression of multiple bacterial outer membrane modifications, which are required for resistance to these membrane-targeting peptides. Mini-Tn5-luxmutant strains ofPseudomonas aeruginosawith Tn insertions disrupting outer membrane protective modifications were assessed for sensitivity against plant defensin peptides. These transcriptionalluxreporter strains were also evaluated forluxgene expression in response to sublethal plant defensin exposure. Also, a plant pathogen,Pseudomonas syringaepv.syringaewas modified through transposon mutagenesis to create mutants that are resistant to in vitro MtDef4 treatments. Results Plant defensins displayed specific and potent antibacterial activity against strains ofP. aeruginosa. A defensin fromMedicago truncatula, MtDef4, induced dose-dependent gene expression of the aminoarabinose modification of LPS and surface polycation spermidine production operons. The ability for MtDef4 to damage bacterial outer membranes was also verified visually through fluorescent microscopy. Another defensin fromM. truncatula, MtDef5, failed to induceluxgene expression and limited outer membrane damage was detected with fluorescent microscopy. The transposon insertion site on MtDef4 resistantP. syringaepv.syringaemutants was sequenced, and modifications of ribosomal genes were identified to contribute to enhanced resistance to plant defensin treatments. Conclusions MtDef4 damages the outer membrane similar to polymyxin B, which stimulates antimicrobial peptide resistance mechanisms to plant defensins. MtDef5, appears to have a different antibacterial MOA. Additionally, the MtDef4 antibacterial mode of action may also involve inhibition of translation.