Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
aminoglycoside acetyltransferase
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| V1V | - | - | - | kanamycin|amikacin | Reslit | Candidate |
| G10A | - | - | - | kanamycin|amikacin|capreomycin | Reslit | Candidate |
| C12T | - | - | - | kanamycin|amikacin|capreomycin | Reslit | Candidate |
| C14T | - | - | - | kanamycin|amikacin|capreomycinkanamycin | Reslit | Candidate |
| G37T | - | - | - | kanamycin|amikacin|capreomycin | Reslit | Candidate |
| R12Q | - | - | - | kanamycin | Reslit | Candidate |
| V163I | - | single resistance variant | Mycobacterium tuberculosis | kanamycin | ReslitCard Database | Candidate |
| A22G | - | - | kanamycin|amikacin | Reslit | Candidate | |
| D26A | - | modestly reduced the binding affinity of Eis to KAN | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate |
| W36A | - | modestly increased affinity of Eis to KAN | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate |
| F84A | - | modestly increased affinity of Eis to KAN | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate |
| W36R | - | modestly increased affinity of Eis to KAN | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate |
| R37G | - | insignificantly altered KAN acetylation | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate |
| S83G | - | statistically significantly increased (2-fold) the catalytic efficiency of the enzyme | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate |
| P86L | - | - | Mycobacterium tuberculosis | capreomycin | Reslit | Candidate |
| - | - | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate | |
| - | overexpression of the gene, resulting in kanamycin resistance | Mycobacterium tuberculosis | kanamycin | ReslitResFinder Database | Candidate | |
| - | - | - | kanamycin | Reslit | Candidate | |
| - | - | - | streptomycin | Reslit | Candidate | |
| - | overexpression of the gene, resulting in kanamycin resistance | Mycobacterium tuberculosis | kanamycinamikacin|kanamycin|capreomycinkanamycin|amikacin | ReslitResFinder Database | Candidate | |
| - | overexpression of the gene, resulting in kanamycin resistance | Mycobacterium tuberculosis | kanamycinkanamycin|amikacinkanamycin|amikacin|capreomycin+3 more | ReslitResFinder Database | Candidate | |
| - | - | Mycobacterium tuberculosis | amikacinkanamycin | ReslitResFinder Database | Candidate | |
| - | - | Mycobacterium africanum | kanamycin | Reslit | Candidate | |
| - | - | Mycobacterium tuberculosis | kanamycin | ResFinder Database | Candidate | |
| - | - | Mycobacterium tuberculosis | kanamycinamikacin | Reslit | Candidate | |
| - | - | - | amikacin | Reslit | Candidate | |
| - | overexpression of the gene, resulting in kanamycin resistance | Mycobacterium tuberculosis | kanamycinamikacin|kanamycinstreptomycin+1 more | ReslitResFinder Database | Candidate | |
| - | - | Mycobacterium tuberculosis | kanamycinamikacin | ReslitResFinder Database | Candidate | |
| - | - | Mycobacterium tuberculosis | kanamycin | Reslit | Candidate | |
| - | overexpression of the gene, resulting in kanamycin resistance | Mycobacterium tuberculosis | kanamycinamikacin|kanamycinamikacin+1 more | ReslitResFinder Database | Candidate | |
| - | - | Mycobacterium tuberculosis | kanamycin | ResFinder Database | Candidate | |
| - | - | - | amikacin | Reslit | Candidate | |
| - | - | - | streptomycin | Reslit | Candidate | |
| G11R | - | - | kanamycin|amikacin | Reslit | Candidate | |
| - | - | - | streptomycin | Reslit | Candidate | |
| - | - | Mycobacterium tuberculosis | kanamycin | ResFinder Database | Candidate | |
| - | - | Mycobacterium tuberculosis | aminoglycosides | Reslit | Candidate |
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| eis | Reslit | 34 | kanamycin, neomycin +4 | Mycobacterium tuberculosis +7 | Taiwan, China, Thailand, India|Moldova|South Africa, Georgia, France|Democratic Republic of the Congo|Benin|Cameroon|Ivory Coast|DR Congo|Western Africa|Central Africa, Eastern China, Europe|France, Europe, India, Russia, Georgia|Moldova|Peru|South Africa|Viet Nam, Brazil|Mato Grosso, five continents | 2009, 2011, 2013, 2014, 2015, 2016, 2017, 2018, 2019, 2021, 2022, 2023, 2024, 2025 | JF266640|JF266636|JF266637|JF266641|JF266638|JF266635|JF266639 | - |
| Eis | Reslit | 2 | neomycin, kanamycin +1 | Mycobacterium tuberculosis | - | 2012, 2023 | - | - |
Overexpression of the chromosomally encoded aminoglycoside acetyltransferase eis confers kanamycin resistance in Mycobacterium tuberculosis.
The study identifies mutations in the promoter region of the eis gene, which encode an aminoglycoside acetyltransferase, leading to kanamycin resistance in Mycobacterium tuberculosis through overexpression of the Eis protein.
Performance assessment of the GenoType MTBDRsl test and DNA sequencing for detection of second-line and ethambutol drug resistance among patients infected with multidrug-resistant Mycobacterium tuberculosis.
The study evaluated the GenoType MTBDR sl test and DNA sequencing for detecting resistance to second-line drugs and ethambutol in multidrug-resistant Mycobacterium tuberculosis. Key findings include the identification of specific mutations in gyrA, rrs, embB, and eis genes associated with resistance to fluoroquinolones, aminoglycosides/cyclic peptides, and ethambutol.
Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB.
The study identifies Eis as a novel acetyltransferase responsible for kanamycin resistance in XDR-TB by demonstrating its unique ability to multiacetylate a wide range of aminoglycosides.
Identification and characterization of inhibitors of the aminoglycoside resistance acetyltransferase Eis from Mycobacterium tuberculosis.
The study identifies and characterizes inhibitors of the aminoglycoside resistance acetyltransferase Eis from Mycobacterium tuberculosis, demonstrating their ability to inhibit Eis activity through various mechanisms including competitive and mixed inhibition.
Thermostable hexameric form of Eis (Rv2416c) protein of M. tuberculosis plays an important role for enhanced intracellular survival within macrophages.
The study identified that the hexameric form of the Eis protein, which has aminoglycoside acetyltransferase activity, is thermostable and contributes to the enhanced intracellular survival of Mycobacterium tuberculosis within macrophages.
Antimicrobial Resistance Mechanisms in Mycobacterium tuberculosis
The paper discusses the molecular mechanisms of drug resistance in Mycobacterium tuberculosis, focusing on genes like pncA, rspA, erm37, tlyA, eis, BlaC, mfpA, IniBAC, EfP, and Tap, which are involved in resistance to pyrazinamide, macrolides, lincosamides, capreomycin, viomycin, kanamycin, β-lactams, fluoroquinolones, isoniazid, ethambutol, and multiple antibiotics.
Triplex real-time PCR melting curve analysis for detecting Mycobacterium tuberculosis mutations associated with resistance to second-line drugs in a single reaction.
The study developed a triplex real-time PCR melting curve assay to detect mutations in gyrA, rrs, and the eis promoter associated with resistance to fluoroquinolones, aminoglycosides, and capreomycin in Mycobacterium tuberculosis.
A random sequential mechanism of aminoglycoside acetylation by Mycobacterium tuberculosis Eis protein.
The study characterizes the aminoglycoside acetyltransferase Eis from Mycobacterium tuberculosis, demonstrating its random sequential bisubstrate mechanism of action and its role in conferring resistance to kanamycin A and neomycin B.
Molecular characterization of amikacin, kanamycin and capreomycin resistance in M/XDR-TB strains isolated in Thailand.
Diagnostic Performance of the New Version (v2.0) of GenoType MTBDRsl Assay for Detection of Resistance to Fluoroquinolones and Second-Line Injectables Drugs: a Multicenter Study.
Potent Inhibitors of Acetyltransferase Eis Overcome Kanamycin Resistance in Mycobacterium tuberculosis.
The study identifies potent inhibitors of the Mycobacterium tuberculosis acetyltransferase Eis, which overcomes kanamycin resistance by blocking Eis-mediated acetylation of kanamycin.
Whole-Genome Sequencing Analysis of Serially Isolated Multi-Drug and Extensively Drug Resistant Mycobacterium tuberculosis from Thai Patients.
The study identified several AMR genes and mutations associated with drug resistance in M. tuberculosis, including rrs, gyrA, inhA, katG, rpoB, embB, pncA, and folC, as well as a novel mutation in Rv2477c linked to kanamycin and amikacin resistance.
Shedding light on the performance of a pyrosequencing assay for drug-resistant tuberculosis diagnosis.
The study evaluated the performance of a pyrosequencing assay for detecting drug-resistant tuberculosis, identifying key genes and mutations associated with resistance to isoniazid, rifampicin, fluoroquinolones, and injectable drugs like kanamycin and capreomycin.
Molecular Investigation of Resistance to Second-Line Injectable Drugs in Multidrug-Resistant Clinical Isolates of Mycobacterium tuberculosis in France.
Sulfonamide-Based Inhibitors of Aminoglycoside Acetyltransferase Eis Abolish Resistance to Kanamycin in Mycobacterium tuberculosis.
The study identifies sulfonamide inhibitors of the aminoglycoside acetyltransferase Eis, which is responsible for kanamycin resistance in Mycobacterium tuberculosis. These inhibitors effectively restore kanamycin susceptibility by blocking Eis activity.
Antimicrobial Resistance Mechanisms in Mycobacterium tuberculosis: Role of Efflux Pumps and Mutations
The study identified several AMR genes and mutations in M. tuberculosis, including rrs A1401G, katG S315T, inhA C-15T, rpoB D516Y, gyrA A90V, tlyA insertion, and eis G-10A, which contribute to resistance against various antibiotics such as isoniazid, rifampicin, amikacin, capreomycin, and ofloxacin.
Impact of gyrB and eis Mutations in Improving Detection of Second-Line-Drug Resistance among Mycobacterium tuberculosis Isolates from Georgia.
The study shows that mutations in gyrB and eis genes improve the detection of second-line drug resistance in Mycobacterium tuberculosis isolates. Specifically, gyrB mutations enhance the detection of ofloxacin resistance, while the eis C-14T mutation improves the detection of kanamycin resistance.
Potent 1,2,4-Triazino[5,6 b]indole-3-thioether Inhibitors of the Kanamycin Resistance Enzyme Eis from Mycobacterium tuberculosis.
The study identifies and characterizes 1,2,4-triazino[5,6 b]indole-3-thioether inhibitors of the Kanamycin resistance enzyme Eis from Mycobacterium tuberculosis, demonstrating their ability to restore KAN sensitivity in resistant strains.
Overexpression of eis without a mutation in promoter region of amikacin- and kanamycin-resistant Mycobacterium tuberculosis clinical strain.
The study identified the overexpression of the eis gene in the amikacin- and kanamycin-resistant M. tuberculosis MT433 strain without any mutations in the promoter region, indicating a novel resistance mechanism.
Unexpected Genomic and Phenotypic Diversity of Mycobacterium africanum Lineage 5 Affects Drug Resistance, Protein Secretion, and Immunogenicity.
The study identifies several AMR genes and mutations in Mycobacterium africanum Lineage 5, including rpoB, katG, inhA, pncA, embB, rrs, and eis, which are associated with resistance to rifampicin, isoniazid, pyrazinamide, ethambutol, and kanamycin. Additionally, a 33.8 kb deletion in the katG gene was found to confer isoniazid resistance.
Mycobacterial Aminoglycoside Acetyltransferases: A Little of Drug Resistance, and a Lot of Other Roles.
The study identifies aac(2′)-Ib and eis as aminoglycoside acetyltransferases in mycobacteria, highlighting their roles in drug resistance and other cellular functions.
Drug resistance gene mutations and treatment outcomes in MDR-TB: A prospective study in Eastern China.
The study identifies various AMR genes and mutations in MDR-TB patients, highlighting the significance of pncA gene mutations in predicting poor treatment outcomes and their association with resistance to pyrazinamide, as well as other genes like rpoB, katG, inhA, gyrA, and others linked to resistance against rifampin, isoniazid, and fluoroquinolones.
Role of Epistasis in Amikacin, Kanamycin, Bedaquiline, and Clofazimine Resistance in Mycobacterium tuberculosis Complex.
Performance Evaluation of GeneLEAD/Deeplex Myc-TB for Mycobacterium tuberculosis Complex Diagnosis and Drug Susceptibility Testing
The study evaluates the performance of the GeneLEAD VIII and Deeplex Myc-TB assay for detecting drug resistance in Mycobacterium tuberculosis complex. It identifies several AMR genes and mutations associated with resistance to various antituberculous drugs.
Accuracy of an amplicon-sequencing nanopore approach to identify variants in tuberculosis drug-resistance-associated genes.
The study evaluates the accuracy of a nanopore sequencing approach for detecting drug-resistance-associated variants in Mycobacterium tuberculosis, demonstrating high agreement with Illumina sequencing for known resistance variants and phylogenetic markers.
Molecular Epidemiology and Polymorphism Analysis in Drug-Resistant Genes in M. tuberculosis Clinical Isolates from Western and Northern India.
The study identified several mutations in the rrs, eis, whiB7, tlyA, and gyrA genes associated with resistance to kanamycin, capreomycin, and ofloxacin in Mycobacterium tuberculosis clinical isolates from western and northern India.
Antimicrobial Resistance in Mycobacterium tuberculosis Clinical Isolates from HIV-Positive and HIV-Negative Patients in Russia
The study identifies various AMR genes and mutations in Mycobacterium tuberculosis isolates from HIV-positive and HIV-negative patients in Russia, highlighting the association of specific mutations with resistance to ethambutol, isoniazid, rifampicin, kanamycin, amikacin, and capreomycin.
Investigating resistance in clinical Mycobacterium tuberculosis complex isolates with genomic and phenotypic antimicrobial susceptibility testing: a multicentre observational study.
The study identifies various AMR genes and mutations in Mycobacterium tuberculosis complex isolates, including rpoB, fabG1, inhA, ndh, katG, mshA, ahpC, gyrA, gyrB, rrs, eis, embCAB, pncA, and rpsA, which are associated with resistance to rifampicin, isoniazid, fluoroquinolones, aminoglycosides, ethambutol, and pyrazinamide.
Recent Advances in Methods to Detect Drug-Resistant Mtb
The paper discusses intrinsic and acquired drug resistance mechanisms in Mycobacterium tuberculosis, highlighting beta-lactamases (blaA, blaC, blaE), erm gene-mediated macrolide/lincosamide/streptogramin B resistance, mfpA-mediated fluoroquinolone/viomycin/capreomycin resistance, and the role of the Eis protein in aminoglycoside resistance. It also identifies mutations in rpoB and gyrA associated with rifampicin and fluoroquinolone resistance.
Genomic analysis of Mycobacterium tuberculosis variant bovis strains isolated from bovine in the state of Mato Grosso, Brazil.
The study identified multiple AMR genes and mutations in Mycobacterium tuberculosis variant bovis strains from Mato Grosso, Brazil, including resistance to pyrazinamide, isoniazid, rifampicin, streptomycin, ethambutol, ethionamide, fluoroquinolones, kanamycin, capreomycin, paraminosalicylic acid, cycloserine, bedaquiline, linezolid, and delamanid.
Direct detection of drug-resistant Mycobacterium tuberculosis using targeted next generation sequencing.
The study presents a targeted next-generation sequencing (tNGS) assay for detecting drug-resistant Mycobacterium tuberculosis directly from clinical specimens, demonstrating high concordance with whole genome sequencing (WGS) results and significantly reducing turnaround time compared to traditional methods.
Discovery and development of inhibitors of acetyltransferase Eis to combat Mycobacterium tuberculosis.
The study focuses on the discovery and development of inhibitors targeting the acetyltransferase Eis, which is responsible for aminoglycoside resistance in Mycobacterium tuberculosis. Eis was shown to confer resistance to kanamycin and amikacin.
Quantitative measurement of antibiotic resistance in Mycobacterium tuberculosis reveals genetic determinants of resistance and susceptibility in a target gene approach.
The study identifies numerous genetic determinants of resistance and susceptibility in Mycobacterium tuberculosis, including mutations in genes such as katG, rpoB, inhA, fabG1, embA, embB, gyrA, gyrB, rrs, and eis, which are associated with resistance to various antibiotics.
Leveraging large language models to predict antibiotic resistance in Mycobacterium tuberculosis.
The study introduces LLMTB, a large language model that predicts antibiotic resistance in Mycobacterium tuberculosis by analyzing genomic data. It identifies key resistance genes and intergenic regions associated with various antibiotics, demonstrating superior performance compared to existing methods.
Unraveling Epistatic Interactions Between Sites Under Drug-Dependent Selection in the Mycobacterium tuberculosis Genome.
Microevolutionary models and multi-omics analysis uncover the cross-drug resistance characteristics of capreomycin-selected Mycobacterium tuberculosis.
The study identifies tlyA mutations (Gly232Asp and Trp120fs) and eis promoter variant (c.−14c>t) as key contributors to capreomycin resistance in Mycobacterium tuberculosis. Additional mutations in rpmA (Gln19Arg) and mmaA2 (Ala48Val) are linked to cross-resistance.
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