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Molecular analysis of isoleucyl-tRNA synthetase mutations in clinical isolates of methicillin-resistant Staphylococcus aureus with low-level mupirocin resistance.

PMID: 170434142006

Key Findings

All mutations were identified in low-level mupirocin-resistant MRSA isolates.

0gene entries

6mutation entries

AMR Mutations

Gene	Protein Change	Nucleotide Change	Mechanism	Organism	Resistance To	Database	Validation Status
ileS	K226T	-	K226T are on the outer surface adjacent to the tRNA molecule about 20 Å from the editing active site	Staphylococcus aureus	Mupirocin	Reslit	-
ileS	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	-
ileS	F227L	-	F227L are on the outer surface adjacent to the tRNA molecule about 20 Å from the editing active site	Staphylococcus aureus	Mupirocin	Reslit	-
ileS	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	-
ileS	P187F	-	mutation of this residue causes steric repulsion to mupirocin	Staphylococcus aureus	Mupirocin	Reslit	-
ileS	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	Staphylococcus aureus	Mupirocin	Reslit	-