Related Experiment Video
Updated: Apr 2, 2026

Isolation and Identification of Waterborne Antibiotic-Resistant Bacteria and Molecular Characterization of their Antibiotic Resistance Genes
Published on: March 3, 2023
The Pathogen-Derived Aminoglycoside Resistance 16S rRNA Methyltransferase NpmA Possesses Dual m1A1408/m1G1408
Natalia Zelinskaya1, Marta A Witek1, Graeme L Conn2
1Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, USA.
Abstract:
Chemical modification of 16S rRNA can confer exceptionally high-level resistance to a diverse set of aminoglycoside antibiotics. Here, we show that the pathogen-derived enzyme NpmA possesses dual m(1)A1408/m(1)G1408 activity, an unexpected property apparently unique among the known aminoglycoside resistance 16S rRNA (m(1)A1408) methyltransferases. Although the biological significance of this activity remains to be determined, such mechanistic variation in enzymes acquired by pathogens has significant implications for development of inhibitors of these emerging resistance determinants.
Insights
Pathogen enzyme NpmA uniquely modifies both adenine and guanine on 16S rRNA, conferring high-level aminoglycoside antibiotic resistance. This discovery has implications for developing new inhibitors against emerging resistance mechanisms.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Chemical modification of 16S ribosomal RNA (rRNA) is a key mechanism for high-level aminoglycoside antibiotic resistance.
- Aminoglycoside resistance 16S rRNA methyltransferases are critical targets for understanding and combating antibiotic resistance.
Purpose of the Study:
- To investigate the enzymatic activity of the pathogen-derived enzyme NpmA.
- To characterize the specific modifications NpmA confers on 16S rRNA and their implications for antibiotic resistance.
Main Methods:
- Enzymatic assays to determine NpmA activity.
- Biochemical analysis of 16S rRNA modifications.
- Assessment of antibiotic resistance conferred by NpmA-mediated modifications.
Main Results:
- NpmA exhibits a unique dual methylation activity, modifying both adenine at position 1408 (m(1)A1408) and guanine at position 1408 (m(1)G1408) on 16S rRNA.
- This dual activity is unprecedented among known aminoglycoside resistance 16S rRNA methyltransferases.
- The biological significance of this dual m(1)A1408/m(1)G1408 activity requires further investigation.
Conclusions:
- The discovery of NpmA's unique dual methylation activity highlights mechanistic diversity in acquired antibiotic resistance enzymes.
- Understanding such variations is crucial for the development of novel inhibitors targeting emerging resistance determinants in pathogens.
More Related Videos
Related Concept Videos
Mechanism of Antibiotic Resistance in MRSA
Clinical Significance of Antibiotic Resistance
Inhibitors of Bacterial Protein Synthesis
Development of Antibiotic Resistance
Gene Regulation in Microbial Communities: Quorum Sensing

