Article ; Online: BING, a novel antimicrobial peptide isolated from Japanese medaka plasma, targets bacterial envelope stress response by suppressing cpxR expression.
2021 Volume 11, Issue 1, Page(s) 12219
Abstract: ... residue peptide named BING, shows a broad-spectrum toxicity against pathogenic bacteria including drug ... medaka. Proteomic analysis indicated that BING treatment induced a deregulation of periplasmic ... peptidyl-prolyl isomerases in gram-negative bacteria. We observed that BING reduced the RNA level of cpxR, an upstream ...
| Abstract | Antimicrobial peptides (AMPs) have emerged as a promising alternative to small molecule antibiotics. Although AMPs have previously been isolated in many organisms, efforts on the systematic identification of AMPs in fish have been lagging. Here, we collected peptides from the plasma of medaka (Oryzias latipes) fish. By using mass spectrometry, 6399 unique sequences were identified from the isolated peptides, among which 430 peptides were bioinformatically predicted to be potential AMPs. One of them, a thermostable 13-residue peptide named BING, shows a broad-spectrum toxicity against pathogenic bacteria including drug-resistant strains, at concentrations that presented relatively low toxicity to mammalian cell lines and medaka. Proteomic analysis indicated that BING treatment induced a deregulation of periplasmic peptidyl-prolyl isomerases in gram-negative bacteria. We observed that BING reduced the RNA level of cpxR, an upstream regulator of envelope stress responses. cpxR is known to play a crucial role in the development of antimicrobial resistance, including the regulation of genes involved in drug efflux. BING downregulated the expression of efflux pump components mexB, mexY and oprM in P. aeruginosa and significantly synergised the toxicity of antibiotics towards these bacteria. In addition, exposure to sublethal doses of BING delayed the development of antibiotic resistance. To our knowledge, BING is the first AMP shown to suppress cpxR expression in Gram-negative bacteria. This discovery highlights the cpxR pathway as a potential antimicrobial target. |
|---|---|
| MeSH term(s) | Animals ; Anti-Bacterial Agents/pharmacology ; Antimicrobial Cationic Peptides/isolation & purification ; Antimicrobial Cationic Peptides/pharmacology ; Bacteria/drug effects ; Bacteria/growth & development ; Bacterial Proteins/antagonists & inhibitors ; Drug Resistance, Multiple, Bacterial/drug effects ; Gene Expression Regulation, Bacterial/drug effects ; Oryzias ; Stress, Physiological |
| Chemical Substances | Anti-Bacterial Agents ; Antimicrobial Cationic Peptides ; Bacterial Proteins ; CpxR protein, Bacteria (153554-07-5) |
| Language | English |
| Publishing date | 2021-06-09 |
| Publishing country | England |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 2615211-3 |
| ISSN | 2045-2322 ; 2045-2322 |
| ISSN (online) | 2045-2322 |
| ISSN | 2045-2322 |
| DOI | 10.1038/s41598-021-91765-4 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
More links
Kategorien
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.