Background: The growing number of macrolide-resistant strains of Streptococcus pyogenes represents an increasing worldwide problem. Macrolide resistance in S. pyogenes is mediated by several different genes, which determine different levels of resistance to macrolides, lincosamides and streptogramin B (MLS).
Methods: This study compared the in vitro antimicrobial activity of azithromycin, clarithromycin, erythromycin, ceftibuten, cefaclor, and telithromycin against 287 strains of S. pyogenes by the broth microdilution method. All strains were characterized both phenotypically and genotypically for erythromycin resistance and most of them have been M-typed by means of PCR.
Results: Ceftibuten and cefaclor showed the best antimicrobial activity, while MIC values for telithromycin were higher against constitutively MLS (cMLS)-resistant strains rather than against the other phenotypes.
Conclusion: Oral cephalosporins retain the best activity against S. pyogenes; showing good activity except for cMLS-resistant strains, telithromycin is a valid alternative to these antimicrobials.
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http://dx.doi.org/10.1159/000087254 | DOI Listing |
Jpn J Infect Dis
July 2024
Department of Bacteriology, Nagoya University Graduate School of Medicine, Japan.
All clinical isolates of Streptococcus dysgalactiae subsp. equisimilis (SDSE) are considered susceptible to β-lactams, the first-line drugs used to treat SDSE infections. However, given that penicillin-non-susceptible SDSE strains have been isolated in Denmark, in this study, we aimed to identify β-lactam-non-susceptible clinical isolates of SDSE in Japan.
View Article and Find Full Text PDFPharmacotherapy
July 2020
Pharmacy Practice Department, Faculty of Pharmacy, King Abdulaziz University, Jeddah, Saudi Arabia.
Biliary tract infections (BTIs), including cholangitis and cholecystitis, are common causes of bacteremia. Bacteremic BTIs are associated with a mortality rate of 9-12%. The extent to which antibiotics are excreted in the bile and the ratio of their exposure to the minimum inhibitory concentration of the infecting organism are among the important factors for the treatment of BTIs.
View Article and Find Full Text PDFMicrob Drug Resist
December 2017
Institute of Microbiology, Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy .
The emergence of group B Streptococcus (GBS) isolates with reduced penicillin susceptibility (PRGBS) and their tendency to be nonsusceptible to fluoroquinolones prompted us to analyze the possible presence of amino acid mutations in penicillin-binding proteins (PBPs) (PBP2X, PBP1A, and PBP2B) from a collection of fluoroquinolone-resistant GBS isolates. We analyzed 21 GBS isolates resistant to levofloxacin. Sequence analysis of genes for PBPs was performed.
View Article and Find Full Text PDFJ Allergy Clin Immunol
September 2015
Ambulatorio di Allergologia, IDI-IRCCS, Capranica, Italy.
Background: Studies regarding the cross-reactivity and tolerability of alternative cephalosporins in large samples of subjects with an IgE-mediated hypersensitivity to cephalosporins are lacking.
Objective: We sought to evaluate the possibility of using alternative cephalosporins in subjects with cephalosporin allergy who especially require them.
Methods: One hundred two subjects with immediate reactions to cephalosporins and positive skin test results to the responsible drugs underwent serum specific IgE assays with cefaclor and skin tests with different cephalosporins.
J Clin Microbiol
September 2014
Department of Bacteriology, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya, Aichi, Japan
We characterized penicillin-susceptible group B streptococcal (PSGBS) clinical isolates exhibiting no growth inhibition zone around a ceftibuten disk (CTB(r) PSGBS). The CTB(r) PSGBS isolates, for which augmented MICs of cefaclor and ceftizoxime were found, shared a T394A substitution in penicillin-binding protein 2X (PBP 2X) and a T567I substitution in PBP 2B, together with an additional G429S substitution in PBP 2X or a T145A substitution in PBP 1A, although the T145A substitution in the transglycosidase domain of PBP 1A would have no effect on the level of resistance to ceftibuten.
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