ArticleFrontiers in microbiology2013
Rise and dissemination of aminoglycoside resistance: the aac(6')-Ib paradigm.
Article in Frontiers in microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed, 181 citations in OpenAlex.
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- Integrating computational approaches to uncover β-lactamase-associated resistance in diarrheagenic Escherichia coli from pediatric patients.Scientific reports · 2025Article
- Inhibiting Amikacin Resistance in Multidrug-Resistant Bacteria with Cadmium and Pyrithione.Current microbiology · 2025Review
- Total Synthesis of Kanamycins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
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46 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Enzymatic modification is a prevalent mechanism by which bacteria defeat the action of antibiotics. Aminoglycosides are often inactivated by aminoglycoside modifying enzymes encoded by genes present in the chromosome, plasmids, and other genetic elements. The AAC(6')-Ib (aminoglycoside 6'-N-acetyltransferase type Ib) is an enzyme of clinical importance found in a wide variety of gram-negative pathogens. The AAC(6')-Ib enzyme is of interest not only because of his ubiquity but also because of other characteristics, it presents significant microheterogeneity at the N-termini and the aac(6')-Ib gene is often present in integrons, transposons, plasmids, genomic islands, and other genetic structures. Excluding the highly heterogeneous N-termini, there are 45 non-identical AAC(6')-Ib related entries in the NCBI database, 32 of which have identical name in spite of not having identical amino acid sequence. While some variants conserved similar properties, others show dramatic differences in specificity, including the case of AAC(6')-Ib-cr that mediates acetylation of ciprofloxacin representing a rare case where a resistance enzyme acquires the ability to utilize an antibiotic of a different class as substrate. Efforts to utilize antisense technologies to turn off expression of the gene or to identify enzymatic inhibitors to induce phenotypic conversion to susceptibility are under way.
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