All detectable high-molecular-mass penicillin-binding proteins are modified in a high-level β-lactam-resistant clinical isolate of Streptococcus mitis

被引:11
作者
Amoroso, A
Demares, D
Mollerach, M
Gutkind, G
Coyette, J
机构
[1] Univ Buenos Aires, Fac Farm & Bioquim, Dept Microbiol Inmunol & Biotecnol, Lab Resistencia Microbiana,Catedra Microbiol,, RA-1113 Buenos Aires, DF, Argentina
[2] Univ Liege, Inst Chim, Ctr Ingn Prot, Liege, Belgium
关键词
D O I
10.1128/AAC.45.7.2075-2081.2001
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
All detectable high-molecular-mass penicillin-binding proteins (HMM PBPs) are altered in a clinical isolate of Streptococcus mitis for which the beta -lactam MICs are increased from those previously reported in our region (cefotaxime MIG, 64 mug/ml). These proteins were hardly detected at concentrations that saturate all PBPs in clinical isolates and showed, after densitometric analysis, 50-fold-lower radiotracer binding. Resistance was related to mosaic structure in all HMM PBP-coding genes, where critical region replacement was complemented not only by substitutions already reported for the closely related Streptococcus pneumoniae but also by other specific replacements that are presumably close to the active-site serine. Mosaic structure was also presumed in a pbp1a-sensitive strain used far comparison, confirming that these structures do not unambiguously imply, by themselves, detectable critical changes in the kinetic properties of these proteins.
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页码:2075 / 2081
页数:7
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