JAC Advance Access published online on October 29, 2003
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkg474
© 2003 by The British Society for Antimicrobial Chemotherapy
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Brief report
1 Department of Pathology,
Hershey Medical Center, 500 University Drive, Hershey, PA 17033;
* Corresponding author. E-mail: bozdogan-b{at}psu.edu.
Received 9 July 2003
; revised 2 September 2003
; accepted 15 September 2003
The roles of
Keywords: H. influenzae, penicillin-binding
proteins, Contribution of
-lactamase
and PBP amino acid substitutions to amoxicillin/clavulanate resistance
in -lactamase-positive,
amoxicillin/clavulanate-resistant Haemophilus influenzae
2 Case Western Reserve University,
Cleveland, OH, USA;
3 Kitasato
University, Tokyo, Japan
-lactamase
and alterations in penicillin-binding protein in the development
of amoxicillin and amoxicillin/clavulanate resistance in two -lactamase-positive, amoxicillin/clavulanate-resistant
(BLPACR) strains of Haemophilus influenzae were
investigated. Seven -lactamase-negative,
ampicillin-resistant (BLNAR) strains were also studied for comparison
of their resistance mechanisms. All strains had been recovered from
patients in Japan. The TEM type -lactamase
of the two BLPACR strains had 100% homology with the amino
acid sequences of published TEM-1 -lactamase,
showing that amoxicillin/clavulanate resistance was not associated
with mutations in this -lactamase.
However, these strains, as well as the seven BLNAR strains, had
multiple mutations in ftsI, which encodes penicillin
binding protein 3 (PBP3). The transformation of H. influenzae Rd
strain with amplified ftsI genes from two BLPACR
and two BLNAR strains enabled the selection of amoxicillin/clavulanate-resistant
transformants with the same mutations as their parent strains. We
concluded that amoxicillin/clavulanate resistance in the two BLPACR
strains was due to changes in PBP3. The possibility of the presence
of an extended spectrum -lactamase
was excluded in the BLPACR strains studied.-lactamases, mutations
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