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Article: BING, a novel antimicrobial peptide isolated from Japanese medaka plasma, targets bacterial envelope stress response by suppressing cpxR expression

TitleBING, a novel antimicrobial peptide isolated from Japanese medaka plasma, targets bacterial envelope stress response by suppressing cpxR expression
Authors
Issue Date2021
PublisherNature Research: Fully open access journals. The Journal's web site is located at http://www.nature.com/srep/index.html
Citation
Scientific Reports, 2021, v. 11, p. article no. 12219 How to Cite?
AbstractAntimicrobial 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.
Persistent Identifierhttp://hdl.handle.net/10722/305258
ISSN
2023 Impact Factor: 3.8
2023 SCImago Journal Rankings: 0.900
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorDong, M-
dc.contributor.authorKwok, SH-
dc.contributor.authorHumble, JL-
dc.contributor.authorLiang, Y-
dc.contributor.authorTang, SW-
dc.contributor.authorTang, KH-
dc.contributor.authorTse, MK-
dc.contributor.authorLei, JH-
dc.contributor.authorRamalingam, R-
dc.contributor.authorKoohimoghadam, M-
dc.contributor.authorAu, DWT-
dc.contributor.authorSun, H-
dc.contributor.authorLam, YW-
dc.date.accessioned2021-10-20T10:06:52Z-
dc.date.available2021-10-20T10:06:52Z-
dc.date.issued2021-
dc.identifier.citationScientific Reports, 2021, v. 11, p. article no. 12219-
dc.identifier.issn2045-2322-
dc.identifier.urihttp://hdl.handle.net/10722/305258-
dc.description.abstractAntimicrobial 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.-
dc.languageeng-
dc.publisherNature Research: Fully open access journals. The Journal's web site is located at http://www.nature.com/srep/index.html-
dc.relation.ispartofScientific Reports-
dc.rightsScientific Reports. Copyright © Nature Research: Fully open access journals.-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleBING, a novel antimicrobial peptide isolated from Japanese medaka plasma, targets bacterial envelope stress response by suppressing cpxR expression-
dc.typeArticle-
dc.identifier.emailKoohimoghadam, M: koohi@hku.hk-
dc.identifier.authorityKoohimoghadam, M=rp02665-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1038/s41598-021-91765-4-
dc.identifier.pmid34108601-
dc.identifier.pmcidPMC8190156-
dc.identifier.scopuseid_2-s2.0-85107515301-
dc.identifier.hkuros327234-
dc.identifier.volume11-
dc.identifier.spagearticle no. 12219-
dc.identifier.epagearticle no. 12219-
dc.identifier.isiWOS:000663771500030-
dc.publisher.placeUnited Kingdom-

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