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.; Gutkind, G.; Coyette, Jacques

doi:10.1128/AAC.45.7.2075-2081.2001

Article (Scientific journals)

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

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https://hdl.handle.net/2268/194272

DOI
10.1128/AAC.45.7.2075-2081.2001

PubMed
11408226

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Keywords :

Amino Acid Substitution; Anti-Bacterial Agents/pharmacology; Bacterial Proteins/genetics; Carrier Proteins/genetics/metabolism; DNA, Bacterial/analysis; Gene Amplification; Hexosyltransferases/genetics/metabolism; Humans; Microbial Sensitivity Tests; Molecular Weight; Multienzyme Complexes/genetics/metabolism; Muramoylpentapeptide Carboxypeptidase/genetics/metabolism; Penicillin-Binding Proteins; Peptidyl Transferases/genetics/metabolism; RNA, Ribosomal, 16S/genetics; Sequence Analysis, DNA; Streptococcus/drug effects/genetics/metabolism; Superoxide Dismutase/genetics; beta-Lactam Resistance/physiology; beta-Lactams

Abstract :

[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

Volume :

Issue :

Pages :

2075-81

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 04 March 2016

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