2.50
Hdl Handle:
http://hdl.handle.net/10033/301810
Title:
Human β-Defensin 2 Induces Extracellular Accumulation of Adenosine in Escherichia coli.
Authors:
Estrela, Andreia Bergamo; Rohde, Manfred ( 0000-0003-0522-3580 ) ; Gutierrez, Maximiliano Gabriel; Molinari, Gabriella ( 0000-0002-6781-1292 ) ; Abraham, Wolf-Rainer ( 0000-0002-2850-2649 )
Abstract:
Human β-defensins are host defense peptides performing antimicrobial as well as immunomodulatory functions. The present study investigated whether treatment of Escherichia coli with human β-defensin 2 could generate extracellular molecules of relevance for immune regulation. Mass spectrometry analysis of bacterial supernatants detected the accumulation of purine nucleosides triggered by β-defensin 2 treatment. Other cationic antimicrobial peptides tested presented variable outcomes with regard to extracellular adenosine accumulation; human β-defensin 2 was the most efficient at inducing this response. Structural and biochemical evidence indicated that a mechanism other than plain lysis was involved in the observed phenomenon. By use of isotope ((13)C) labeling, extracellular adenosine was found to be derived from preexistent RNA, and a direct interaction between the peptide and bacterial nucleic acid was documented for the first time for β-defensin 2. Taken together, the data suggest that defensin activity on a bacterial target may alter local levels of adenosine, a well-known immunomodulator influencing inflammatory processes.
Affiliation:
Chemical Microbiology.
Citation:
Human β-Defensin 2 Induces Extracellular Accumulation of Adenosine in Escherichia coli. 2013, 57 (9):4387-93 Antimicrob. Agents Chemother.
Journal:
Antimicrobial agents and chemotherapy
Issue Date:
Sep-2013
URI:
http://hdl.handle.net/10033/301810
DOI:
10.1128/AAC.00820-13
PubMed ID:
23817371
Type:
Article
Language:
en
ISSN:
1098-6596
Appears in Collections:
publications of the research group chemical microbiology (CMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorEstrela, Andreia Bergamoen_GB
dc.contributor.authorRohde, Manfreden_GB
dc.contributor.authorGutierrez, Maximiliano Gabrielen_GB
dc.contributor.authorMolinari, Gabriellaen_GB
dc.contributor.authorAbraham, Wolf-Raineren_GB
dc.date.accessioned2013-09-18T14:28:59Zen
dc.date.available2013-09-18T14:28:59Zen
dc.date.issued2013-09en
dc.identifier.citationHuman β-Defensin 2 Induces Extracellular Accumulation of Adenosine in Escherichia coli. 2013, 57 (9):4387-93 Antimicrob. Agents Chemother.en_GB
dc.identifier.issn1098-6596en
dc.identifier.pmid23817371en
dc.identifier.doi10.1128/AAC.00820-13en
dc.identifier.urihttp://hdl.handle.net/10033/301810en
dc.description.abstractHuman β-defensins are host defense peptides performing antimicrobial as well as immunomodulatory functions. The present study investigated whether treatment of Escherichia coli with human β-defensin 2 could generate extracellular molecules of relevance for immune regulation. Mass spectrometry analysis of bacterial supernatants detected the accumulation of purine nucleosides triggered by β-defensin 2 treatment. Other cationic antimicrobial peptides tested presented variable outcomes with regard to extracellular adenosine accumulation; human β-defensin 2 was the most efficient at inducing this response. Structural and biochemical evidence indicated that a mechanism other than plain lysis was involved in the observed phenomenon. By use of isotope ((13)C) labeling, extracellular adenosine was found to be derived from preexistent RNA, and a direct interaction between the peptide and bacterial nucleic acid was documented for the first time for β-defensin 2. Taken together, the data suggest that defensin activity on a bacterial target may alter local levels of adenosine, a well-known immunomodulator influencing inflammatory processes.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Antimicrobial agents and chemotherapyen_GB
dc.titleHuman β-Defensin 2 Induces Extracellular Accumulation of Adenosine in Escherichia coli.en
dc.typeArticleen
dc.contributor.departmentChemical Microbiology.en_GB
dc.identifier.journalAntimicrobial agents and chemotherapyen_GB

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