Mutations in the aph(2")-Ic gene are responsible for increased levels of aminoglycoside resistance.
Random PCR mutagenesis of the enterococcal aph(2")-Ic gene followed by selection for mutant enzymes that confer enhanced levels of aminoglycoside resistance resulted in mutants of APH(2")-Ic with His-258-Leu and Phe-108-Leu substitutions, all of which conferred rises in the MICs of several aminoglycosides. The mutated residues are located outside conserved regions of aminoglycoside phosphotransferases.
Lee
Hae Kyung
HK
Division of Infectious Diseases, Wayne State University, Detroit, Michigan 48201, USA.
Vakulenko
Sergei B
SB
Clewell
Don B
DB
Lerner
Stephen A
SA
Chow
Joseph W
JW
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000617:Aminoglycosides; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001426:Bacterial Proteins; D024881:Drug Resistance, Bacterial; D016983:Enterococcus / Q000187:drug effects* / Q000201:enzymology; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000235:genetics*; D016133:Polymerase Chain Reaction; D017422:Sequence Analysis, DNA
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; C425933:APH(2'')-Ic protein, Enterococcus faecalis; D017853:Phosphotransferases (Alcohol Group Acceptor)