R. Del Campo et al., Aminoglycoside-modifying enzymes in high-level streptomycin and gentamicinresistant Enterococcus spp. in Spain, INT J ANT A, 15(3), 2000, pp. 221-226
Aminoglycoside resistance was evaluated in 690 enterococcus strains isolate
d from different clinical sources originating from patients at the Universi
ty Clinic Hospital of Zaragoza (Spain). The enterococci obtained from clini
cally significant samples (blood, urine, or exudates) showed more high-leve
l resistance to gentamicin and streptomycin (65 and 42%, respectively) than
those isolated from faecal samples (49 and 23%, respectively). Aminoglycos
ide-modifying enzymes (AME) from 119 of these high-level gentamicin and str
eptomycin resistant enterococcus strains were studied. The most frequent AM
Es found were APH(3') and AAC(6')-APH(2 "). More than one enzyme was detect
ed in 71% of the strains (four different enzymes in 5% of the strains). Thr
ee Enterococcus faecalis strains had ANT(4')(4 ") enzymatic activity. Diffe
rent enzymatic expressions of the bifunctional enzyme AAC(6')-APH(2 ") were
demonstrated in strains in which the complete aac(6')-aph(2 ") gene was de
tected by PCR and hybridization: (i) AAC(6') + APH(2 ") activity; (ii) AAC(
6') only; (iii) APH(2 ") only; and (iv) no activity of AAC(6') or APH(2 ").
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