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Antimicrobial Agents and Chemotherapy, July 2001, p. 2075-2081, Vol. 45, No. 7
Laboratorio de resistencia microbiana,
Cátedra de Microbiología. Departamento de
Microbiología, Inmunología y Biotecnología,
Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires,
Buenos Aires, Argentina,1 and Centre
d'ingenierie des Protéines, Institut de Chimie, Université
de Liège, Sart Tilman, Liege, Belgium2
Received 9 October 2000/Returned for modification 29 January
2001/Accepted 6 April 2001
All detectable high-molecular-mass penicillin-binding proteins (HMM
PBPs) are altered in a clinical isolate of Streptococcus mitis for which the
0066-4804/01/$04.00+0 DOI: 10.1128/AAC.45.7.2075-2081.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
All Detectable High-Molecular-Mass
Penicillin-Binding Proteins Are Modified in a High-Level
-Lactam-Resistant Clinical Isolate of Streptococcus
mitis
-lactam MICs are increased from those
previously reported in our region (cefotaxime MIC, 64 µg/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 for comparison, confirming
that these structures do not unambiguously imply, by themselves,
detectable critical changes in the kinetic properties of these proteins.
*
Corresponding author. Mailing address: Laboratorio de
resistencia microbiana, Cátedra de Microbiología.
Departamento de Microbiología, Inmunología y
Biotecnología, Facultad de Farmacia y Bioquímica,
Universidad de Buenos Aires, Junin 956 (1113) Buenos Aires, Argentina.
Phone: 54 11 4964 8285. Fax: 54 11 4962. 5341. E-mail:
ggutkind{at}huemul.ffyb.uba.ar.
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