DNA gyrase mutations in quinolone-resistant clinical isolates of Neisseria gonorrhoeae.
Eight quinolone-resistant clinical isolates of Neisseria gonorrhoeae were shown to carry mutations in their GyrA proteins. Six isolates had a single amino acid change of serine to phenylalanine at the position corresponding to Ser-83 in Escherichia coli. In addition to the change of serine to phenylalanine, two isolates had another change of aspartic acid to asparagine at the position corresponding to Asp-87 in E. coli.
Deguchi
T
T
Department of Urology, Gifu University, Japan.
Yasuda
M
M
Asano
M
M
Tada
K
K
Iwata
H
H
Komeda
H
H
Ezaki
T
T
Saito
I
I
Kawada
Y
Y
D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000494:pharmacology*; D001483:Base Sequence; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II / Q000235:genetics*; D004352:Drug Resistance, Microbial; D024841:Fluoroquinolones; D008969:Molecular Sequence Data; D009154:Mutation; D009344:Neisseria gonorrhoeae / Q000187:drug effects* / Q000201:enzymology*
D000890:Anti-Infective Agents; D024841:Fluoroquinolones; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II