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Antimicrobial Agents and Chemotherapy, June 2006, p. 2270-2271, Vol. 50, No. 6
0066-4804/06/$08.00+0 doi:10.1128/AAC.01450-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Gene Cassette Encoding a 3-N-Aminoglycoside Acetyltransferase in a Chromosomal Integron

LETTER
The large number and variety of antibiotic resistance genes
found in gene cassettes associated with class 1 integrons in
multiply antibiotic-resistant organisms have always indicated
the existence of a large pool of gene cassettes from which they
are drawn (
10). The discovery of integrons, sometimes harboring
very large arrays of gene cassettes, in the chromosomes of many
different bacteria has confirmed the existence of this pool,
but to date very few cassettes containing resistance genes have
been found among these cassettes. Known examples are the
catB9 (
12) and
blaP7 (
blaP9) (
7,
8) cassettes found in the cassette
arrays of different
Vibrio cholerae strains.
Though 3-N-aminoglycoside acetyltransferases [AAC(3) enzymes] have been classified into several groups based on differences in the spectrum of aminoglycosides they modify, they fall into only two groups based on the relationships between the proteins (6). The five characterized aacC genes found in gene cassettes (see Table 1) encode proteins of 154 to 158 amino acids that are related to one another and form family A (6). They belong to the aac(3)-I phenotypic group and confer resistance to gentamicin, sisomicin, and fortimicin but not to tobramycin, amikacin, or kanamycin (1, 3, 6, 11, 13, 15).
Our recent searches have revealed further potential
aacC-A-type
genes (Table
1). One is in a cassette found in a class 1 integron,
but three of them are in draft sequences of bacterial genomes.
The
aacC-A7 gene in the complete
Saccharophagus degradans (formerly
Microbulbifer degradans) genome also lies within an identifiable
gene cassette. The putative AacC-A7 [AAC(3)-Ig] acetyltransferase
encoded by this cassette is 51 to 60% identical to other cassette-encoded
AacC-A enzymes and most closely related to AacC-A5 [AAC(3)-Ie].
Alignment of the established and putative AacC-A sequences (Fig.
1) reveals 45 completely conserved amino acids, or 62 if only
AacC-A1 to AacC-A7 are considered. It therefore seems reasonable
to assume that
aacC-A7 also confers resistance to aminoglycoside
antibiotics.
This represents only the third identification of a potential
antibiotic resistance gene associated with a gene cassette that
is part of the genome of a microorganism that harbors an integron.
Though each
aacC-A cassette has an identifiable 59-be (sometimes
called an
attC site) made up of two simple sites and a central
region as is characteristic for 59-be (
14), in most cases they
are not close relatives of one another and some are not closely
related to ones found in any other known cassette (
6,
11). The
59-be of the
Saccharophagus aacC-A7 cassette is not closely
related to a 59-be in any of the many cassettes in that organism's
genome. Its closest relative is in a cassette from
Nitrosococcus oceani. Thus, if, as is generally assumed, cassettes that arose
in a particular organism have very similar 59-be, it is unlikely
that the
aacC-A7 cassette was originally formed in
S. degradans.

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Liam D. H. Elbourne
School of Molecular and Microbial Biosciences The University of Sydney Sydney, NSW 2006, Australia
Ruth M. Hall*
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* Phone: 61-2-9351-4365, Fax: 61-2-9351-4571, E-mail: Ruth.Hall{at}mmb.usyd.edu.au |
Antimicrobial Agents and Chemotherapy, June 2006, p. 2270-2271, Vol. 50, No. 6
0066-4804/06/$08.00+0 doi:10.1128/AAC.01450-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.