JAC Advance Access published online on November 1, 2002
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkf140
© 2002 by The British Society for Antimicrobial Chemotherapy
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Original Paper
1 Department of Microbiology, Yamaguchi University School of Medicine, Minamikogushi
1-1-1, Ube, Yamaguchi 755-8505, Japan; Department of Gastroenterology
and Hepatology, Yamaguchi University School of Medicine, Minamikogushi
1-1-1, Ube, Yamaguchi 755-8505, Japan
* Corresponding author. E-mail: mshirai{at}po.cc.yamaguchi-u.ac.jp.
Received 14 January 2002
; revised 23 May 2002
; accepted 6 June 2002
Reports on the isolation of amoxicillin-resistant Helicobacter pylori are increasing worldwide, which
may cause serious problems in eradication therapy. To elucidate
the mechanism of amoxicillin resistance of H. pylori,
penicillin-binding proteins (PBPs) of amoxicillin-resistant strains isolated
in Korea were analysed. Three PBPs (66, 63 and 60 kDa) were identified
in both amoxicillin-resistant and -susceptible strains using biotinylated
ampicillin, and the PBP profiles were very similar irrespective
of the difference in amoxicillin susceptibility. We obtained clones
with moderate resistance from an amoxicillin-susceptible strain,
HPK5, by transformation with genomic DNA from an amoxicillin-resistant
strain, HPA116. In a resistance-induced clone, HPO1, the affinity
of PBP1 for amoxicillin was reduced. The pbp1 genes
from HPA116, HPO1 and HPK5 were cloned and sequenced. The nucleotide
sequences of pbp1 from HPA116 and HPO1 were almost
identical, whereas that of HPK5 was quite different. Both the ORFs
of HPA116 and HPO1 pbp1 have four substitutions
and one insertion of amino acid residues compared with those of
HPK5 and other sensitive strains. All the mutations, except one,
are in the C-terminal half of the 659-amino-acid sequence containing
the penicillin-binding modules. DNA fragments containing either
full-length or a C-terminal half of pbp1 could
transform HPK5 to have resistance, indicating that changes in the
penicillin-binding core of PBP1 are involved in the amoxicillin
resistance of H. pylori isolated in Korea.
A change in PBP1 is involved in amoxicillin resistance
of clinical isolates of Helicobacter pylori
2 Department of Microbiology, Yamaguchi University School of Medicine, Minamikogushi
1-1-1, Ube, Yamaguchi 755-8505, Japan; Center
for Virus Vector Development, Institute for Genetic Medicine, Hokkaido
University, Kita-15, Nishi-7, Kita-Ku, Sapporo, 060-0815, Japan;
3 Department of Microbiology, Yamaguchi University School of Medicine, Minamikogushi
1-1-1, Ube, Yamaguchi 755-8505, Japan
4 Department of Microbiology, Kosin
Medical College, 34 Amnam-Dong, Seo-Gu, Busan 602-702, Korea
5 Department of Gastroenterology
and Hepatology, Yamaguchi University School of Medicine, Minamikogushi
1-1-1, Ube, Yamaguchi 755-8505, Japan
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