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Antimicrobial Agents and Chemotherapy, February 1999, p. 367-370, Vol. 43, No. 2
Unité des Agents Antibactériens,
Institut Pasteur, 75724 Paris Cedex 15, France
Received 24 June 1998/Returned for modification 26 October
1998/Accepted 17 November 1998
The sequences of the promoter regions and of the structural genes
for 13 penicillinase, extended-spectrum, and inhibitor-resistant TEM-type In members of the family
Enterobacteriaceae, the most prevalent mechanism of
resistance to broad-spectrum
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Updated Sequence Information for TEM
-Lactamase Genes
ABSTRACT
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Abstract
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References
-lactamases have been determined, and an updated
blaTEM gene nomenclature is proposed.
TEXT
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Abstract
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-lactams is detoxification of the drugs
by plasmid-mediated enzymes that are variants of TEM and SHV
penicillinases (4, 13). The TEM-derived extended-spectrum or
inhibitor-resistant -lactamases differ from the parental TEM-1 and
TEM-2 penicillinases by various combinations of amino acid substitutions. The structural genes for TEM-1 penicillinases are designated blaTEM-1a and
blaTEM-1b, and the structural gene for TEM-2 is
designated blaTEM-2 (10). As an aid
to the study of the mutational events which account for the sequence
diversity of TEM-type -lactamases and to the nomenclature of the
numerous variants, we have determined and analyzed the sequences of the structural genes and of the promoters of various
blaTEM genes. Amplification and direct
sequencing of the PCR product were as described previously
(15). The origins (Table 1)
and the nucleotide changes in the blaTEM genes
and the corresponding amino acid substitutions in the deduced sequence
of the enzymes (Tables
2 and
3) are summarized.
TABLE 1.
Origins of the enzymes studied
TABLE 2.
Substitutions in blaTEM genes and
derived penicillinases and extended-spectrum -lactamases
TABLE 3.
Substitutions in blaTEM genes and
derived inhibitor-resistant -lactamases
Two promoters for initiation of transcription of the blaTEM genes have been described: the weak P3 promoter for blaTEM-1 in Tn3 (20) and, following a C-to-T substitution at position 32, the two overlapping promoters (Pa and Pb) which lead to a ca. 10-fold increase in transcriptional levels (8).
Penicillinases. (i) blaTEM-1c.
Escherichia coli BM2729 was isolated in 1989 and has a
phenotype of resistance to -lactam antibiotics which corresponds to the synthesis of a penicillinase. The corresponding
blaTEM-1c gene differs from
blaTEM-1a by the nucleotide substitution
C436
T, which is silent.
(ii) blaTEM-13.
Morganella
morganii BM2717 (14) harbored a plasmid that carries
both the blaTEM-2 and the
blaTEM-13 genes (data not shown). The sequence
of blaTEM-13 differs from that of
blaTEM-2 by C990T, resulting in
Thr265Met, as determined by oligotyping (14). Most interestingly, upstream from blaTEM-13 and
blaTEM-2 we found the weak promoter
P3 (C32) instead of the expected strong
promoters Pa and Pb. The presence of the two
genes on the same replicon could therefore result from gene duplication
followed by a point mutation.
Extended-spectrum -lactamases. (i)
blaTEM-8.
The TEM-8 extended-spectrum
-lactamase, later designated CAZ-2 (6), was detected in
Klebsiella pneumoniae HM12, which was isolated in 1987, and
the structural gene for the enzyme was sequenced (6, 17).
The promoter region has a thymine at position 32 (Table 2) which was
not reported for the gene for CAZ-2. The blaTEM-8 gene derives from
blaTEM-2 by three base pair changes and differs
from blaTEM-3 at position 692, where a C-to-A
substitution leads to Arg164Ser.
(ii) blaTEM-11.
The gene for the
extended-spectrum -lactamase TEM-11 harbored by E. coli
1724A (27) was oligotyped (14), with a remaining ambiguity found at position 238, and was characterized by restriction fragment length polymorphism analysis, which revealed an adenine at
position 925 (2). However, sequence determination indicated G925 (Table 2). Thus, the blaTEM-11
gene differs from blaTEM-2 at two positions,
G693A, resulting in Arg164His, and
A925G, which is silent. The strong promoters
Pa and Pb for that gene are identical to those
for blaTEM-2. The
blaTEM-11 gene could therefore result from a
recombination event, in the vicinity of position 692, between
blaTEM-2, which would have provided the 5'
portion of the gene, and blaTEM-6
(11), which would have contributed the 3' part of the gene.
Alternatively, the blaTEM-11 gene could be a
point mutant from a yet uncharacterized TEM-2 progenitor with a
G925 or a double mutant of blaTEM-2.
(iii) blaTEM-15a.
The gene for
extended-spectrum -lactamase TEM-15 from K. pneumoniae
BM2730 was oligotyped (14) and was sequenced without the
promoter (21). We have resequenced the entire region whose sequence differs from that of blaTEM-1a at three
positions: G512A (Glu104Lys),
G914A (Gly238Ser), and
G162T. The last change occurs at position 1 of the 
10
consensus Pribnow box sequence of the P3 promoter and has
been shown to be responsible for the hyperproduction of TEM-1
(22). We suggest the designation P4 for this new
promoter. Since this structural gene was apparently derived from
blaTEM-1a, we propose the nomenclature
blaTEM-15a.
(iv) blaTEM-15b.
The deduced amino
acid sequence of blaTEM-15b is
identical to that of blaTEM-15a. The enzyme,
formerly designated TEM-17 on the basis of oligotyping (14),
was therefore redesignated TEM-15. The TEM-17 sequence that we
originally proposed has subsequently been found in Capnocytophaga
ochracea (EMBL accession no. Y14574). The sequence of
blaTEM-15b differs from that of
blaTEM-1b at two positions:
G512A, which leads to Glu104Lys, and
G914A, which results in Gly238Ser,
whereas the strong Pa and Pb promoters are
present upstream. We thus suggest the designation
blaTEM-15b since this gene is likely to be
derived from blaTEM-1b. The TEM-15 -lactamase
displays the same amino acid substitutions which enlarge the substrate
range of TEM-3, except that TEM-15 has Gln39 instead of Lys.
(v) blaTEM-12c and blaTEM-10b. blaTEM-12c and blaTEM-10b originate from two E. coli strains, F1 and F2, which were isolated from the same patient at a 24-h interval (26). The blaTEM-12c gene is identical to blaTEM-12, which encodes YOU-2 (19), and is located downstream from the Pa and Pb promoters. Since blaTEM-12a refers to the structural gene for TEM-101 (9) and blaTEM-12b is the designation for the gene described by Heritage et al. (12) and also the gene for CAZ-3 (7), we propose the nomenclature blaTEM-12c. We also found a blaTEM-12c gene in E. coli MG32 (28). This gene was chromosomally located and, in an unusual fashion, was preceded by the weak P3 promoter.
The sequence of blaTEM-10b differs from that of blaTEM-12c by a single base pair change, G917A, which results in Glu240Lys. The
blaTEM-10b gene is identical to
blaTEM-10 from plasmids pJPQ100 and pMG223 in
K. pneumoniae and pCLL2302 in E. coli (18,
19). These genes could be designated
blaTEM-10b since they are derived from
blaTEM-1b; blaTEM-10a
would then correspond to the gene carried by pCLL2301 from K. pneumoniae (18), which is derived from
blaTEM-1a. The structural genes for TEM-10 and
TEM-12 have previously been detected in the same clinical isolate
(3).
(vi) blaTEM-24b.
The sequence of
blaTEM-24 encoding TEM-24 (or CAZ-6) has been
published with only part of the promoter region
(6), and we suggest the designation
blaTEM-24a. The sequence of
blaTEM-24b differs by a silent mutation
(T682C) from that of blaTEM-24a and is under the control of the strong promoters Pa and
Pb. It has been proposed that
blaTEM-24a could result from recombination of
blaTEM-3 and blaTEM-5
between positions 604 and 682 (6). Similarly,
blaTEM-24b could originate from a
recombination event between positions 693 and 911 of
blaTEM-8 (6, 17) and
blaTEM-5 (23). Whatever the authentic
origin of the gene may be, our observation documents dissemination of
TEM-24 in Enterobacter aerogenes.
(vii) blaTEM-53.
The sequence of the
new mutant gene blaTEM-53 differs from
that of blaTEM-2 at three loci, with each base
pair change leading to an amino acid substitution: C263T
(Leu21Phe), A317C
(Lys39Gln), and C692A
(Arg164Ser). The gene is expressed from the strong promoters Pa and Pb. It is worth noting that the
corresponding mature protein is identical to TEM-12.
This gene could be secondary to a recombination event, between
positions 436 and 512, of blaTEM-4 (23) or blaTEM-9 (16),
which would provide the 5' third of the gene, and
blaTEM-7 (9), which would correspond
to the 3' two-thirds.
Inhibitor-resistant -lactamases. (i)
blaTEM-33.
The sequence of
blaTEM-33, which we propose be renamed
blaTEM-33a, has been published
(24). We report here the sequence of two genes, designated
blaTEM-33b and
blaTEM-33c, that have been detected in clinical
isolates (Table 1).
(ii) blaTEM-33b.
The structural gene
has the mutation A407C relative to the sequence of
blaTEM-1b, resulting in Met69Leu,
and is under the control of the Pa and Pb promoters.
(iii) blaTEM-33c.
blaTEM-33c is derived from
blaTEM-2 following two changes:
A317C (Lys39Gln) and A407C
(Met69Leu). The promoter region has the
G162T mutation, which is commonly found upstream from the genes for inhibitor-resistant -lactamases. Thus, the
blaTEM-33c gene is derived from that for the
"TEM-2 like" enzyme (5), which consists of TEM-2 with
Lys39Gln and the T32C and
G162T mutations upstream from the gene.
(iv) blaTEM-54.
blaTEM-54 has not yet been described and
originates from E. coli BM2728 (Table 1). It derives from
blaTEM-1a following one mutation,
G930T, which leads to the amino acid change
Arg244Leu, whereas the promoter region corresponds to
Pa and Pb.
-lactamases, and three inhibitor-resistant
-lactamases. The sequence variety found probably reflects the
existence in nature of genes other than
blaTEM-1a, blaTEM-1b,
blaTEM-1c, blaTEM-2, and
blaTEM-13 for penicillinases. With the
exception of chromosomal blaTEM-12, the genes
were located downstream from strong promoters such as Pa and
Pb and the new promoter P4.
Nucleotide sequence accession numbers. The nucleotide sequence data for blaTEM-53 and blaTEM-54 have been submitted to the GenBank nucleotide sequence data library under accession no. AF104441 and AF104442, respectively.
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ACKNOWLEDGMENTS |
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We thank G. Arlet, G. Aubert, R. Bismuth, V. Jarlier, T. Lambert, P. Legrand, D. Lesage, G. Vedel, G. Verschraegen, and D. A. Weber for gifts of strains.
This work was supported in part by a Bristol-Myers Squibb Unrestricted Biomedical Research Grant in Infectious Diseases.
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FOOTNOTES |
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* Corresponding author. Mailing address: Unité des Agents Antibactériens, 28, rue du Docteur Roux, Institut Pasteur, 75724 Paris Cedex 15, France. Phone: (33) (1) 45 68 83 61. Fax: (33) (1) 45 68 83 19. E-mail: sgouss{at}pasteur.fr.
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Antimicrobial Agents and Chemotherapy, February 1999, p. 367-370, Vol. 43, No. 2
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Copyright © 1999, American Society for Microbiology. All rights reserved.
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