Purification and characterization of an erythromycin esterase from an erythromycin-resistant Pseudomonas sp.

Kim, Y

doi:10.1016/s0378-1097(02)00611-0

Cited by 15 publications

(28 citation statements)

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“…In addition, the macrolide esterase and a fosfomycin-specific epoxide hydrolase were also shown to mediate the related drug resistance (10,12,23). The Cm hydrolase activity has been reported in the Cm-producing actinomycetes; however, its exact mechanism remains unclear (16,19).…”

Section: Discussionmentioning

confidence: 99%

Inactivation of Chloramphenicol and Florfenicol by a Novel Chloramphenicol Hydrolase

Wang

Lee

et al. 2012

Appl Environ Microbiol

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ABSTRACTChloramphenicol and florfenicol are broad-spectrum antibiotics. Although the bacterial resistance mechanisms to these antibiotics have been well documented, hydrolysis of these antibiotics has not been reported in detail. This study reports the hydrolysis of these two antibiotics by a specific hydrolase that is encoded by a gene identified from a soil metagenome. Hydrolysis of chloramphenicol has been recognized in cell extracts ofEscherichia coliexpressing a chloramphenicol acetate esterase gene,estDL136. A hydrolysate of chloramphenicol was identified asp-nitrophenylserinol by liquid chromatography-mass spectroscopy and proton nuclear magnetic resonance spectroscopy. The hydrolysis of these antibiotics suggested a promiscuous amidase activity of EstDL136. WhenestDL136was expressed inE. coli, EstDL136 conferred resistance to both chloramphenicol and florfenicol onE. coli, due to their inactivation. In addition,E. colicarryingestDL136deactivated florfenicol faster than it deactivated chloramphenicol, suggesting that EstDL136 hydrolyzes florfenicol more efficiently than it hydrolyzes chloramphenicol. The nucleotide sequences flankingestDL136encode proteins such as amidohydrolase, dehydrogenase/reductase, major facilitator transporter, esterase, and oxidase. The most closely related genes are found in the bacterial familySphingomonadaceae, which contains many bioremediation-related strains. Whether the gene cluster withestDL136inE. coliis involved in further chloramphenicol degradation was not clear in this study. While acetyltransferases for chloramphenicol resistance and drug exporters for chloramphenicol or florfenicol resistance are often detected in numerous microbes, this is the first report of enzymatic hydrolysis of florfenicol resulting in inactivation of the antibiotic.

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Section: Discussionmentioning

confidence: 99%

Inactivation of Chloramphenicol and Florfenicol by a Novel Chloramphenicol Hydrolase

Wang

Lee

et al. 2012

Appl Environ Microbiol

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“…This last TP was also detected in other enzymatic study (with ERY esterase) carried out by Kim et al (2004b) in aquaculture sediment containing ERY-resistant Pseudomonas species. Moreover, other biodegradation studies have reported this compound (Feldman et al, 1963;Flickinger and Perlman, 1975;Kim et al, 2002).…”

Section: Identification Of Transformation Products Of Erythromycinmentioning

confidence: 91%

Identification of new transformation products during enzymatic treatment of tetracycline and erythromycin antibiotics at laboratory scale by an on-line turbulent flow liquid-chromatography coupled to a high resolution mass spectrometer LTQ-Orbitrap

et al. 2015

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33In the case of Tc, the tentative molecular formulas with errors mass within 2 ppm have been 34 based on the hypothesis of dehydroxylation, (bi)demethylation and oxidation of the rings A and 35C as major reactions. In contrast, the major TP detected for ERY has been identified as the 36 "dehydration ERY-A", with the same molecular formula of its parent compound. In addition, the 37 evaluation of the antibiotic activity of the samples along the enzymatic treatments showed a 38 decrease around 100% in both cases.

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“…In recent years, the ere(A2) gene, a variant of ere(A) located in a class 1 integron cassette, has been found in Enterobacter aerogenes, E. cloacae, E. coli, Klebsiella oxytoca, K. pneumoniae, Providencia stuartii, Pseudomonas spp., Salmonella enterica, and Vibrio cholera (Chang et al 2000;Peters et al 2001;Kim et al 2002;Thungapathra et al 2002;Plante et al 2003;Verdet et al 2006;Abbassi et al 2008;Chen et al 2009;Krauland et al 2010). Although macrolide antibiotics are generally not used in the treatment of nongastrointestinal infections caused by enteric bacteria, the spread of ere(A2) in Enterobacteriaceae is concerning because macrolides are often used in the treatment of traveler's diarrhea, and erythromycin is a common treatment of cholera in children and pregnant women (see cdc.gov/ cholera/doc/recommend-anitbiotics-treatment .docx).…”

Section: Macrolide Inactivation Macrolide Esterasesmentioning

confidence: 99%

Resistance to Macrolide Antibiotics in Public Health Pathogens

Fyfe

Grossman

Kerstein

et al. 2016

Cold Spring Harb Perspect Med

163

140

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Macrolide resistance mechanisms can be target-based with a change in a 23S ribosomal RNA (rRNA) residue or a mutation in ribosomal protein L4 or L22 affecting the ribosome's interaction with the antibiotic. Alternatively, mono-or dimethylation of A2058 in domain V of the 23S rRNA by an acquired rRNA methyltransferase, the product of an erm (erythromycin ribosome methylation) gene, can interfere with antibiotic binding. Acquired genes encoding efflux pumps, most predominantly mef(A) þ msr(D) in pneumococci/streptococci and msr(A/B) in staphylococci, also mediate resistance. Drug-inactivating mechanisms include phosphorylation of the 2 0 -hydroxyl of the amino sugar found at position C5 by phosphotransferases and hydrolysis of the macrocyclic lactone by esterases. These acquired genes are regulated by either translation or transcription attenuation, largely because cells are less fit when these genes, especially the rRNA methyltransferases, are highly induced or constitutively expressed. The induction of gene expression is cleverly tied to the mechanism of action of macrolides, relying on antibiotic-bound ribosomes stalled at specific sequences of nascent polypeptides to promote transcription or translation of downstream sequences. Macrolide antibiotics are polyketides composed of a 14-, 15-, or 16-membered macrocyclic lactone ring (14-, 15-, and 16-membered) to which several sugars and/or side chains have been attached by the producing organism or as modifications during semisynthesis in the laboratory (Figs. 1 and 2). Newer semisynthetic derivations, like ketolides telithromycin, and solithromycin, have a C3-keto group in place of the C3 cladinose (akin to naturally occurring pikromycin) (Brockmann and Henkel 1950) and an 11,12-cyclic carbamate with an extended alkyl -aryl side chain that increases the affinity of the antibiotic for the ribosome by 10-to 100-fold (Hansen et al. 1999;Dunkle et al. 2010); in the case of solithromycin, a fluorine substituent at C2 provides an additional ribosomal interaction (Llano-Sotelo et al. 2010). Macrolides continue to be important in the therapeutic treatment of community-acquired pneumonia (Streptococcus pneumoniae, Haemophilus influenzae, Moraxella catarrhalis, and atypicals Legionella pneumophila, Mycoplasma pneumoniae, Chlamydia pneumoniae), sexually transmitted diseases (Neiserria gonorhoeae, Chlamydia trachomatis, Mycoplasma genitalium), shigellosis, and salmonellosis. With solithromycin heading for a new drug application (NDA) filing in 2016 and having the in vitro potency to treat erythromycin-resistant

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Purification and characterization of an erythromycin esterase from an erythromycin-resistant Pseudomonas sp.

Cited by 15 publications

References 15 publications

Inactivation of Chloramphenicol and Florfenicol by a Novel Chloramphenicol Hydrolase

Inactivation of Chloramphenicol and Florfenicol by a Novel Chloramphenicol Hydrolase

Identification of new transformation products during enzymatic treatment of tetracycline and erythromycin antibiotics at laboratory scale by an on-line turbulent flow liquid-chromatography coupled to a high resolution mass spectrometer LTQ-Orbitrap

Resistance to Macrolide Antibiotics in Public Health Pathogens

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