2016
DOI: 10.1002/ange.201608482
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Berichtigung: Muropeptides in Pseudomonas aeruginosa and their Role as Elicitors of β‐Lactam‐Antibiotic Resistance

Abstract: In Abbildung 2B dieser Zuschrift wurden die Produkte der Reaktionen von 2e mit PBP4 und AmpDh3 verwechselt. Die Reaktion von 2e mit PBP4 führt zu 2d,und die Reaktion von 2e mit AmpDh3 zu 2a,w ie in der korrigierten Abbildung 2unten gezeigt. In Haupttext und Abbildungslegende ergeben sich dadurch keine ¾nderungen.

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Cited by 2 publications
(3 citation statements)
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“…Conversely, when the d , d ‐carboxypeptidase activity of PBP4 is inactivated by the antibiotic the derepressor metabolite is dominant, leading to induction of expression of the ampC gene. Although the fundamental operation of this regulation was long surmised, it is nonetheless gratifying that our crystallographic studies of the effector‐binding domain of P. aeruginosa AmpR complement studies with the same domain of the Citrobacter freundii AmpR, and further match to our analysis of the structural fluctuation within the muropeptide pool in the absence and presence of β‐lactams …”
Section: Abetting the β‐Lactam Antibiotics Against Gram‐negative Bactsupporting
confidence: 65%
“…Conversely, when the d , d ‐carboxypeptidase activity of PBP4 is inactivated by the antibiotic the derepressor metabolite is dominant, leading to induction of expression of the ampC gene. Although the fundamental operation of this regulation was long surmised, it is nonetheless gratifying that our crystallographic studies of the effector‐binding domain of P. aeruginosa AmpR complement studies with the same domain of the Citrobacter freundii AmpR, and further match to our analysis of the structural fluctuation within the muropeptide pool in the absence and presence of β‐lactams …”
Section: Abetting the β‐Lactam Antibiotics Against Gram‐negative Bactsupporting
confidence: 65%
“…These muropeptides are transported to the cytoplasm by the inner-membrane protein AmpG (Johnson et al , 2013; Fisher & Mobashery, 2014). In the cytoplasm, pentapeptide-containing muropeptides derepress (in P. aeruginosa and many Enterobacteriaceae ) the AmpR transcription regulator so as to initiate β-lactamase expression (among other effects) as a key resistance mechanism (Wiedemann et al , 1998; Balcewich et al , 2010; Balasubramanian et al , 2015; Vadlamani et al , 2015; Lee et al , 2016a; Dik et al , 2017). The enabling function of LTs intimately links muropeptide recycling to antibiotic resistance (Figure 2).…”
Section: The Reaction Products Of Lts Initiate Both Offensive and Defmentioning
confidence: 99%
“…The value of this strategy for further extending the clinical life of β-lactams arises from the appreciation that LTs and PBPs cooperate during cell-wall biosynthesis, in a homeostatic balancing act between construction and demolition of the cell wall (Johnson et al , 2013). The inhibition of PBPs by β-lactams disturbs this equilibrium, and in many pathogenic Gram-negative bacteria the resulting change in the pool of the recycling cell-wall fragments triggers β-lactamase expression (Jacobs et al , 1994; Fisher & Mobashery, 2014; Vadlamani et al , 2015; Lee et al , 2016a; Dik et al , 2017) These observations raise two central questions with respect to LT inhibition. The first is whether an LT inhibitor might suppress the ability of these Gram-negative bacteria to induce β-lactamases.…”
Section: Lts As Targets For Antibiotic Developmentmentioning
confidence: 99%