All detectable high-molecular-mass penicillin-binding proteins are modified in a high-level beta-lactam-resistant clinical isolate of Streptococcus mitis.
Amoroso, Ana Maria; Demares, D.; Mollerach, M.et al.
2001 • In Antimicrobial Agents and Chemotherapy, 45 (7), p. 2075-81
[en] 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 MIC, 64 microg/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.
Disciplines :
Microbiology
Author, co-author :
Amoroso, Ana Maria ; Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Demares, D.
Mollerach, M.
Gutkind, G.
Coyette, Jacques ; Université de Liège > Relations académiques et scientifiques (Sciences)
Language :
English
Title :
All detectable high-molecular-mass penicillin-binding proteins are modified in a high-level beta-lactam-resistant clinical isolate of Streptococcus mitis.
Publication date :
2001
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
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