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Correlation between Substitutions in Penicillin‐Binding Protein 1 and Amoxicillin Resistance in Helicobacter pylori
Author(s) -
Rimbara Emiko,
Noguchi Norihisa,
Kawai Takashi,
Sasatsu Masanori
Publication year - 2007
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2007.tb03990.x
Subject(s) - amoxicillin , helicobacter pylori , penicillin binding proteins , biology , microbiology and biotechnology , amino acid substitution , amino acid , gene , penicillin , genetics , antibiotic resistance , transformation (genetics) , antibiotics , mutation
The correlation between the substitutions of penicillin‐binding protein 1 (PBP1) and amoxicillin resistance was studied for the determination of the substitutions in PBP1 which confer amoxicillin resistance in Helicobacter pylori . By the comparison of the amino acid sequences of PBP1 in the amoxicillin‐resistant ( n =3), low‐susceptible ( n =3), and susceptible ( n = 13) H. pylori isolates, the substitution Asn 562 →Tyr, which is adjacent to KTG motif (555–557), was common and specific to amoxicillin‐resistant H. pylori . Additionally, all amoxicillin‐resistant isolates had multiple substitutions such as Ser 414 →Arg in the transpeptidase region of PBP1 of H. pylori . Furthermore all transformants obtained by the natural transformation using the pbp1 genes of amoxicillin‐resistant H. pylori isolates had multiple substitutions including Asn 562 →Tyr. These results suggest that multiple amino acid substitutions in the transpeptidase region of PBP1 are closely related to amoxicillin resistance in H. pylori .