Translational inhibition of CTX-M extended spectrum β-lactamase in clinical strains of Escherichia coli by synthetic antisense oligonucleotides partially restores sensitivity to cefotaxime
Frontiers in Microbiology, ISSN: 1664-302X, Vol: 7, Issue: MAR, Page: 373
2016
- 18Citations
- 39Captures
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Metrics Details
- Citations18
- Citation Indexes17
- 17
- CrossRef6
- Patent Family Citations1
- Patent Families1
- Captures39
- Readers39
- 39
Article Description
Synthetic antisense oligomers are DNA mimics that can specifically inhibit gene expression at the translational level by ribosomal steric hindrance. They bind to their mRNA targets by Watson-Crick base pairing and are resistant to degradation by both nucleases and proteases. A 25-mer phosphorodiamidate morpholino oligomer (PMO) and a 13-mer polyamide (peptide) nucleic acid (PNA) were designed to target mRNA (positions -4 to +21, and -17 to -5, respectively) close to the translational initiation site of the extended-spectrum β-lactamase resistance genes of CTX-M group 1. These antisense oligonucleotides were found to inhibit β-lactamase activity by up to 96% in a cell-free translation-transcription coupled system using an expression vector carrying a bla gene cloned from a clinical isolate. Despite evidence for up-regulation of CTX-M gene expression, they were both found to significantly restore sensitivity to cefotaxime (CTX) in E. coli AS19, an atypical cell wall permeable mutant, in a dose dependant manner (0-40 nM). The PMO and PNA were covalently bound to the cell penetrating peptide (CPP; (KFF)K) and both significantly (P < 0.05) increased sensitivity to CTX in a dose dependent manner (0-40 nM) in field and clinical isolates harboring CTX-M group 1 β-lactamases. Antisense oligonucleotides targeted to the translational initiation site and Shine-Dalgarno region of bla inhibited gene expression, and when conjugated to a cell penetrating delivery vehicle, partially restored antibiotic sensitivity to both field and clinical isolates.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84964335844&origin=inward; http://dx.doi.org/10.3389/fmicb.2016.00373; http://www.ncbi.nlm.nih.gov/pubmed/27047482; http://journal.frontiersin.org/Article/10.3389/fmicb.2016.00373/abstract; https://dx.doi.org/10.3389/fmicb.2016.00373; https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2016.00373/full
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