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Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
isoleucyl-tRNA synthetase
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| V588F | V588 is located in a hydrophobic pocket that interacts directly with the fatty acid side chain of mupirocin, mutation of this residue causes steric repulsion to mupirocin, Target modification, single resistance variant, isoleucine--tRNA ligase IleS | Staphylococcus aureus | mupirocin | ReslitResFinder DatabaseCard DatabaseReference Gene Catalog | Candidate | |
| V631F | - | Target modification, single resistance variant, isoleucine--tRNA ligase IleS | Staphylococcus aureus | mupirocin | ReslitResFinder DatabaseCard DatabaseReference Gene Catalog | Candidate |
| Y723H | - | - | Staphylococcus aureus, Escherichia coli | vancomycin | Reslit | Candidate |
| I637V | - | - | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| P187F | - | mutation of this residue causes steric repulsion to mupirocin | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| K226T | - | K226T are on the outer surface adjacent to the tRNA molecule about 20 Å from the editing active site | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| F227L | - | F227L are on the outer surface adjacent to the tRNA molecule about 20 Å from the editing active site | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| Q612H | - | Q612H has potential to interact with mupirocin. Q612 sits close to the core of IleS Rossman fold motif, where it forms a water-bridged hydrogen bond with the side chain of D635 | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| V767D | - | V767D lies in the interior surface of the cylindrical central helical domain of the IleS, distal to the tRNA binding site | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| G593A | - | - | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| G591S | - | - | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| N213D | - | - | Staphylococcus aureus | mupirocin | Reslit | Candidate |
| H67Q | - | isoleucine--tRNA ligase IleS | Staphylococcus aureus | mupirocin | Reference Gene Catalog | Candidate |
| F563L | - | isoleucine--tRNA ligase IleS | Staphylococcus aureus | mupirocin | Reference Gene Catalog | Candidate |
| G593V | - | isoleucine--tRNA ligase IleS | Staphylococcus aureus | mupirocin | Reference Gene Catalog | Candidate |
| R816C | - | isoleucine--tRNA ligase IleS | Staphylococcus aureus | mupirocin | Reference Gene Catalog | Candidate |
Mutations affecting the Rossman fold of isoleucyl-tRNA synthetase are correlated with low-level mupirocin resistance in Staphylococcus aureus.
Other mutations were found but not directly linked to mupirocin resistance
Staphylococcus aureus ileS with mutation conferring resistance to mupirocin; CARD accession: CARD:3003729
In Vitro Tolerance of Drug-Naive Staphylococcus aureus Strain FDA209P to Vancomycin.
Mutation in ileS was associated with vancomycin tolerance
Dissemination of macrolides, fusidic acid and mupirocin resistance among Staphylococcus aureus clinical isolates.
Associated with both low and high level mupirocin resistance
Genomic analysis of Staphylococcus aureus isolates from bacteremia reveals genetic features associated with the COVID-19 pandemic.
Molecular analysis of isoleucyl-tRNA synthetase mutations in clinical isolates of methicillin-resistant Staphylococcus aureus with low-level mupirocin resistance.
All mutations were identified in low-level mupirocin-resistant MRSA isolates.
The mutational landscape of Staphylococcus aureus during colonisation.
Five of the eight protein-altering mutations in ileS were associated with mupirocin resistance.
High prevalence of heterogeneous mupirocin-resistant Staphylococcus aureus and its molecular characterization.
Prevalence and molecular characterization of methicillin-resistant Staphylococcus aureus with mupirocin, fusidic acid and/or retapamulin resistance.
Epistasis analysis uncovers hidden antibiotic resistance-associated fitness costs hampering the evolution of MRSA.
The mutation leads to reduced toxin production and hidden fitness costs.