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16S rRNA (adenine(1408)-N(1))-methyltransferase NpmA
Overview
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| NpmA | Card DatabaseReference Gene CatalogReslit | 20 | AMINOGLYCOSIDE, Amikacin +9 | Escherichia coli +5 | Japan|India|Brazil|United States|China|Saudi Arabia|Europe, northeast India, Japan|South America|United States|Europe|Asia, global|Greece|India|Morocco|Pakistan, China |
| 2007, 2011, 2014, 2016, 2017, 2020, 2022, 2024, 2025, 2026 |
| AB261016.2 |
| BAF80809.1 |
| npmA | Card DatabaseResFinder Database | 2 | TOBRAMYCIN, ISEPAMICIN +8 | Escherichia coli | - | 2007 | AB261016 | BAF80809.1 |
Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides.
Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides.
Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides.
Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides.
The study identifies NpmA, a novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, which confers resistance to multiple aminoglycosides by methylating the A1408 position in 16S rRNA.
Expression, purification and crystallization of adenosine 1408 aminoglycoside-resistance rRNA methyltransferases for structural studies.
The study describes the expression, purification, and crystallization of KamB and NpmA, two adenosine 1408 aminoglycoside-resistance rRNA methyltransferases, which confer resistance to aminoglycosides such as kanamycin, neomycin, and apramycin.
Structural basis for the methylation of A1408 in 16S rRNA by a panaminoglycoside resistance methyltransferase NpmA from a clinical isolate and analysis of the NpmA interactions with the 30S ribosomal subunit.
NpmA, a methyltransferase from a clinical isolate, confers resistance to kanamycin by specifically methylating A1408 in 16S rRNA. Key residues D30, W107, and W197 were found to be essential for its activity.
Aminoglycoside resistance 16S rRNA methyltransferases block endogenous methylation, affect translation efficiency and fitness of the host.
The study identifies ArmA and NpmA as 16S rRNA methyltransferases that confer high-level aminoglycoside resistance by modifying G1405 and A1408, respectively. Both enzymes interfere with endogenous methylation processes, impacting cellular fitness and translation accuracy.
Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA.
The study characterizes the aminoglycoside-resistance methyltransferase NpmA, which modifies the 16S rRNA at position A1408, thereby conferring resistance to kanamycin. The structural and functional analysis of NpmA provides insight into the molecular mechanism of resistance.
Aminoglycoside Resistance: The Emergence of Acquired 16S Ribosomal RNA Methyltransferases.
The paper discusses the emergence and characteristics of acquired 16S ribosomal RNA methyltransferases (16S-RMTases) that confer resistance to aminoglycosides, particularly in gram-negative bacteria. It highlights the importance of these genes in multidrug-resistant organisms and their association with other resistance mechanisms such as carbapenemases.
KlebSeq, a Diagnostic Tool for Surveillance, Detection, and Monitoring of Klebsiella pneumoniae.
The study presents KlebSeq, a diagnostic tool for detecting and monitoring Klebsiella pneumoniae, including its AMR and virulence profiles. It identified various AMR genes such as aac(6')-Ib, aac(6')-Ib-cr, gyrA, npmA, blaCTX-M, and blaKPC, demonstrating the effectiveness of amplicon sequencing for AMR detection.
Rapid Aminoglycoside NP Test for Rapid Detection of Multiple Aminoglycoside Resistance in Enterobacteriaceae.
The study presents a rapid colorimetric test for detecting multiple aminoglycoside resistance in Enterobacteriaceae, focusing on the identification of 16S rRNA methylases (armA, rmtB, rmtC, rmtF, rmtG, npmA) and aminoglycoside-modifying enzymes (aac(3)-IV, aac(3)-Ia, aac(3)-V, aph(3')-I, aph(3')-Ib, ant(2'')).
Substrate Recognition and Modification by a Pathogen-Associated Aminoglycoside Resistance 16S rRNA Methyltransferase.
The study identifies NpmA as a pathogen-associated 16S rRNA methyltransferase that confers resistance to aminoglycosides by modifying the 16S rRNA at position A1408.
A structural basis for the antibiotic resistance conferred by an N1-methylation of A1408 in 16S rRNA.
The study identifies the NpmA methyltransferase, which confers resistance to aminoglycosides by N1-methylation of A1408 in 16S rRNA, and shows that this modification reduces susceptibility to aminoglycosides with a 6'-NH3+ group while maintaining effectiveness against those with a 6'-OH group.
Expansion of acquired 16S rRNA methytransferases along with CTX-M-15, NDM and OXA-48 within three sequence types of Escherichia coli from northeast India.
The study identified ten different 16S rRNA methyltransferase genes (rmtA, rmtB, rmtC, rmtD, rmtE, rmtF, rmtG, rmtH, armA, npmA) along with CTX-M-15, NDM, and OXA-48 beta-lactamases in three sequence types of Escherichia coli from northeast India.
Aminoglycoside Resistance: Updates with a Focus on Acquired 16S Ribosomal RNA Methyltransferases.
The paper discusses the global spread of 16S rRNA methyltransferases (ArmA, RmtB, RmtC, and NpmA) that confer high-level aminoglycoside resistance in various gram-negative bacteria. These genes are responsible for modifying the 16S rRNA, leading to resistance against multiple aminoglycosides.
Antibiotic Resistance in Bacteria-A Review.
The review discusses various mechanisms of antibiotic resistance in bacteria, including resistance genes such as blaCTX-M, ermB, tet(O), vanA, vanB, and aac(6')-Ie-aph(2")-Ia, as well as mutations in gyrA, gyrB, and 23S rRNA associated with resistance to fluoroquinolones, macrolides, and other antibiotics.
Effects of Neolamarckia cadamba leaves extract on microbial community and antibiotic resistance genes in cecal contents and feces of broilers challenged with lipopolysaccharides.
The study found that Neolamarckia cadamba leaves extract (NCLE) reduced the abundance of antibiotic resistance genes (ARGs) in cecal contents of lipopolysaccharide (LPS)-induced broilers by maintaining microbial balance.
Discovery of First-in-Class Inhibitors Targeting a Pathogen-Associated Aminoglycoside-Resistance 16S rRNA Methyltransferase.
The study identifies NpmA as a key mediator of aminoglycoside resistance through 16S rRNA methylation and reports the discovery of first-in-class inhibitors targeting a unique Y-shaped pocket in NpmA.
Biological cost of aminoglycoside resistance Arm/Kam 16S rRNA methyltransferases from natural antibiotic producers and clinical pathogens.
The study characterizes the biological cost of 16S rRNA methyltransferases (ArmA, RmtA, RmtB, RmtC, RmtD, Sgm, KamB, and NpmA) in Escherichia coli, demonstrating their role in conferring high-level aminoglycoside resistance and their impact on bacterial fitness, translational fidelity, and stress response.
Biological cost of aminoglycoside resistance Arm/Kam 16S rRNA methyltransferases from natural antibiotic producers and clinical pathogens.
The study characterizes the biological cost of 16S rRNA methyltransferases (ArmA, RmtA, RmtB, RmtC, RmtD, Sgm, KamB, and NpmA) in Escherichia coli, demonstrating their role in conferring high-level aminoglycoside resistance and their impact on bacterial fitness, translational fidelity, and stress response.
Design, Synthesis, and Evaluation of Novel Inhibitors of Aminoglycoside-Resistance 16S Ribosomal RNA Methyltransferases.
The study reports the design, synthesis, and evaluation of novel inhibitors targeting 16S rRNA methyltransferases NpmA and RmtB, which confer resistance to aminoglycosides. Compounds with a (Z)-dehydroamino amide core showed higher activity against these enzymes compared to (E) isomers.
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