Most aminoglycoside resistance in Acinetobacter spp. involves producti
on of aminoglycoside-modifying enzymes. Previous studies have shown th
at the genes encoding these enzymes can be present on plasmids, transp
osons or within integron-type structures. To determine whether particu
lar mechanisms of aminoglycoside resistance have developed in strains
from specific geographical locations (with subsequent clonal spread),
or whether common mechanisms have been acquired by genotypically disti
nct clinical isolates of Acinetobacter spp. throughout the world, a ge
notypically heterogeneous collection of 24 multiresistant clinical iso
lates of Acinetobacter spp. from 15 hospitals in 11 countries worldwid
e was studied. All were resistant to two or more aminoglycoside antibi
otics. The full aminoglycoside resistance profile was determined for e
ach isolate, allowing a putative enzyme content to be inferred, with s
ubsequent confirmation of enzyme content and genetic location by polym
erase chain reaction (PCR) and hybridisation techniques. All produced
at least one aminoglycoside-modifying enzyme, most commonly AAC(3)-I a
nd ANT(3 '')-I in various combinations. Other enzymes found were AAC(3
)-II, AAC(6')-I, ANT(2 ''), APH(3')-I and APH(3')-VI. None was confine
d to strains from a particular geographical area. Nine isolates transf
erred resistance mediated by AAC(3)-I, ANT(2 '')-I, APH(3 '')-I or APH
(3)'-VI by conjugation to a sensitive strain of A. baumannii, but most
resistance was non-transferable. PCR mapping revealed an integron loc
ation in six isolates for the aac(3)-Ia gene and in three isolates for
the ant(3 '')-Ia gene. Overall, the study demonstrated that similar a
minoglycoside-modifying enzymes are found in unrelated isolates of Aci
netobacter spp., and that particular genes are not restricted to speci
fic areas of the world. The demonstration of certain genes on plasmids
and integrons emphasises the probable importance of these structures
in the dissemination of certain types of aminoglycoside resistance in
Acinetobacter spp.