title: [Resistance to antimicrobiotics and mutation of PBPs in Streptococcus pneumoniae isolated from Kinki region of Japan].
abstract: We studied the susceptibility to penicillin G (PCG) and other antimicrobiotics in 235 clinical isolates of Streptococcus pneumoniae. Samples were collected between April 1 and June 30, 2000 from nine medical institutions of the Kinki Region of Japan. We classified the minimum inhibitory concentration (MIC) of PCG according to the National Committee for Clinical Laboratory Standards (NCCLS) criteria. The overall rate of all types of S. pneumoniae resistance was 53.2% (penicillin-susceptible S. pneumoniae (PSSP): 46.8%, penicillin-intermediate S. pneumoniae (PISP): 42.6%, penicillin-resistant S. pneumoniae (PRSP): 10.6%). In other antimicrobiotics, the resistance (R)/intermediate susceptibility (I) rates (R/I%) were as follows: ceftriaxone, 28.9%; cefotaxime, 7.7%; imipenem, 8.9%; meropenem, 9.8%; clarithromycin, 82.6%; clindamycin, 42.1%; levofloxacin, 0.4%; vancomycin, 0%. We used the polymerase chain reaction to study the mutations of the penicillin-binding proteins pbp1 a, pbp2b, and pbp2x in 140 strains of S. pneumoniae in the MIC for PCG was < 0.5 microgram/ml. Among the 109 strains of PSSP, 32 (29.4%) had no mutation and 77 (70.6%) showed mutation of more than one of the pbp mutations. Among the 31 strains of PISP, only 1 strain (3.2%) was not mutated. Since 70.6% of the strains classified as PSSP had pbp mutations, S. pneumoniae clearly can acquire resistance to anti-microbiotics. In the future, a comprehensive surveillance of S. pneumoniae is necessary.
authors.affiliation: Department of Clinical Laboratory, Kinki University Hospital.
authors.forename: Kaori
authors.initials: K
authors.lastname: Satoh
authors.forename: Masaru
authors.initials: M
authors.lastname: Komatsu
authors.forename: Koichi
authors.initials: K
authors.lastname: Shimakawa
authors.forename: Toshiro
authors.initials: T
authors.lastname: Ura
authors.forename: Shohiro
authors.initials: S
authors.lastname: Kinoshita
authors.forename: Katsutoshi
authors.initials: K
authors.lastname: Yamasaki
authors.forename: Hisaaki
authors.initials: H
authors.lastname: Nishio
authors.forename: Ryodo
authors.initials: R
authors.lastname: Washizu
authors.forename: Tomonari
authors.initials: T
authors.lastname: Yamashita
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Nakamura
authors.forename: Yasunao
authors.initials: Y
authors.lastname: Wada
authors.forename: Masahiro
authors.initials: M
authors.lastname: Toyokawa
authors.forename: Tomomi
authors.initials: T
authors.lastname: Koufuku
authors.forename: Masanori
authors.initials: M
authors.lastname: Aihara
mesh_terms: D019881:Aminoacyltransferases; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000235:genetics*; D006602:Hexosyltransferases; D007769:Lactams; D002267:Muramoylpentapeptide Carboxypeptidase / Q000235:genetics*; D009154:Mutation; D010403:Penicillin Resistance / Q000235:genetics; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D013296:Streptococcus pneumoniae / Q000187:drug effects / Q000235:genetics* / Q000302:isolation & purification; D018440:beta-Lactam Resistance / Q000235:genetics
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; D019881:Aminoacyltransferases; C478701:penicillin-binding protein 2b, Streptococcus; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase