Open AccessInteractions between Glycopeptides and β-Lactams against Isogenic Pairs of Teicoplanin-Susceptible and -Resistant Strains of Staphylococcus haemolyticus
Author(s) -
Carla Vignaroli,
Francesca Biavasco,
Pietro E. Varaldo
Publication year - 2006
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.00260-06
Subject(s) - teicoplanin , glycopeptide , staphylococcus haemolyticus , autolysis (biology) , microbiology and biotechnology , biology , staphylococcus , vancomycin , staphylococcus aureus , micrococcaceae , antibacterial agent , antibiotics , bacteria , genetics , biochemistry , enzyme
Four isogenic derivatives with stably increased glycopeptide MICs (all become resistant to teicoplanin) were obtained from four glycopeptide-susceptible clinical isolates ofStaphylococcus haemolyticus . All strains were extensively analyzed and compared for a number of distinctive features. In particular, the results provided insights into the puzzling issue of antistaphylococcal interactions between glycopeptides and β-lactams, especially the paradox of double zones around β-lactam disks and the relationships between autolysis rate and type of interaction.