TY - JOUR
T1 - Effects of altering aminoglycoside structures on bacterial resistance enzyme activities
AU - Green, Keith D.
AU - Chen, Wenjing
AU - Garneau-Tsodikova, Sylvie
PY - 2011/7
Y1 - 2011/7
N2 - Aminoglycoside-modifying enzymes (AMEs) constitute the most prevalent mechanism of resistance to aminoglycosides by bacteria. We show that aminoglycosides can be doubly modified by the sequential actions of AMEs, with the activity of the second AME in most cases unaffected, decreased, or completely abolished. We demonstrate that the bifunctional enzyme AAC(3)-Ib/AAC(6′)-Ib′ can diacetylate gentamicin. Since single acetylation does not always inactivate the parent drugs completely, two modifications likely provide morerobust inactivation in vivo.
AB - Aminoglycoside-modifying enzymes (AMEs) constitute the most prevalent mechanism of resistance to aminoglycosides by bacteria. We show that aminoglycosides can be doubly modified by the sequential actions of AMEs, with the activity of the second AME in most cases unaffected, decreased, or completely abolished. We demonstrate that the bifunctional enzyme AAC(3)-Ib/AAC(6′)-Ib′ can diacetylate gentamicin. Since single acetylation does not always inactivate the parent drugs completely, two modifications likely provide morerobust inactivation in vivo.
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U2 - 10.1128/AAC.00312-11
DO - 10.1128/AAC.00312-11
M3 - Article
C2 - 21537023
AN - SCOPUS:79959277696
SN - 0066-4804
VL - 55
SP - 3207
EP - 3213
JO - Antimicrobial Agents and Chemotherapy
JF - Antimicrobial Agents and Chemotherapy
IS - 7
ER -