Release of Periplasmic Nucleotidase Induced by Human Antimicrobial Peptide in E. coli Causes Accumulation of the Immunomodulator Adenosine.
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AbstractPrevious work by our group described that human β-defensin-2 induces accumulation of extracellular adenosine (Ado) in E. coli cultures through a non-lytic mechanism causing severe plasmolysis. Here, we investigate the presence of AMP as a direct precursor and the involvement of a bacterial enzyme in the generation of extracellular Ado by treated bacteria. Following hBD-2 treatment, metabolites were quantified in the supernatants using targeted HPLC-MS/MS analysis. Microbial growth was monitored by optical density and cell viability was determined by colony forming units counts. Phosphatase activity was measured using chromogenic substrate pNPP. The results demonstrate that defensin-treated E. coli strain W releases AMP in the extracellular space, where it is converted to Ado by a bacterial soluble factor. An increase in phosphatase activity in the supernatant was observed after peptide treatment, similar to the effect of sucrose-induced osmotic stress, suggesting that the periplasmic 5'nucleotidase (5'-NT) is released following the plasmolysis event triggered by the peptide. Ado accumulation was enhanced in the presence of Co2+ ion and inhibited by EDTA, further supporting the involvement of a metallo-phosphatase such as 5'-NT in extracellular AMP conversion into Ado. The comparative analysis of hBD-induced Ado accumulation in different E. coli strains and in Pseudomonas aeruginosa revealed that the response is not correlated to the peptide's effect on cell viability, but indicates it might be dependent on the subcellular distribution of the nucleotidase. Taken together, these data shed light on a yet undescribed mechanism of host-microbial interaction: a human antimicrobial peptide inducing selective release of a bacterial enzyme (E. coli 5'-NT), leading to the formation of a potent immunomodulator metabolite (Ado).
CitationRelease of Periplasmic Nucleotidase Induced by Human Antimicrobial Peptide in E. coli Causes Accumulation of the Immunomodulator Adenosine. 2015, 10 (9):e0138033 PLoS ONE
AffiliationHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
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- Human β-defensin 2 induces extracellular accumulation of adenosine in Escherichia coli.
- Authors: Estrela AB, Rohde M, Gutierrez MG, Molinari G, Abraham WR
- Issue date: 2013 Sep
- Uptake of AMP, ADP, and ATP in Escherichia coli W.
- Authors: Watanabe K, Tomioka S, Tanimura K, Oku H, Isoi K
- Issue date: 2011
- Soluble expression of active human beta-defensin-3 in Escherichia coli and its effects on the growth of host cells.
- Authors: Si LG, Liu XC, Lu YY, Wang GY, Li WM
- Issue date: 2007 Apr 20
- Introduction of human β-defensin-3 into cultured human keratinocytes and fibroblasts by infection of a recombinant adenovirus vector.
- Authors: Suzuki Y, Inokuchi S, Takazawa K, Umezawa K, Saito T, Kidokoro M, Tanaka M, Matsuzawa H, Inoue S, Tuchiya I, Ando K
- Issue date: 2011 Feb
- Murine beta-defensin-3 is an inducible peptide with limited tissue expression and broad-spectrum antimicrobial activity.
- Authors: Burd RS, Furrer JL, Sullivan J, Smith AL
- Issue date: 2002 Nov