Revisiting the mechanism of macrolide-antibiotic resistance mediated by ribosomal protein L22
نویسندگان
چکیده
منابع مشابه
Macrolide resistance mediated by a Bifidobacterium breve membrane protein.
A gene coding for a hypothetical membrane protein from Bifidobacterium breve was expressed in Lactococcus lactis. Immunoblotting demonstrated that this protein is located in the membrane. Phenotypical changes in sensitivity towards 21 antibiotics were determined. The membrane protein-expressing cells showed higher levels of resistance to several macrolides.
متن کاملInability of L22 ribosomal protein alteration to increase macrolide MICs in the absence of efflux mechanism in Haemophilus influenzae HMC-S.
BACKGROUND Haemophilus influenzae HMC-C with high-level macrolide resistance after multi-step selection by clarithromycin reverted spontaneously and became hypersusceptible to macrolides. OBJECTIVE Determination of macrolide resistance mechanism(s) in hypersusceptible and hyperresistant strains. METHODS The presence of macrolide efflux in the strains was studied by radioactive erythromycin ...
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Tetracycline resistance protein Tet(O), which protects the bacterial ribosome from binding the antibiotic tetracycline, is a translational GTPase with significant similarity in both sequence and structure to the elongation factor EF-G. Here, we present an atomic model of the Tet(O)-bound 70S ribosome based on our cryo-electron microscopic reconstruction at 9.6-Å resolution. This atomic model al...
متن کاملResistance to quinupristin-dalfopristin due to mutation of L22 ribosomal protein in Staphylococcus aureus.
The mechanism of resistance to the streptogramin antibiotics quinupristin and dalfopristin was studied in a Staphylococcus aureus clinical isolate selected under quinupristin-dalfopristin therapy, in four derivatives of S. aureus RN4220 selected in vitro, and in a mutant selected in a model of rabbit aortic endocarditis. For all strains the MICs of erythromycin, quinupristin, and quinupristin-d...
متن کاملRibosomal Protein L19 and L22 Modulate TLR3 Signaling
BACKGROUND Toll-like receptor 3 (TLR3) recognizes double-stranded RNA (dsRNA) and induces inflammation. In this study we attempted to ascertain if there are endogenous host molecules controlling the production of cytokines and chemokines. Two candidates, ribosomal protein L19 and L22, were analyzed to determine if they influence cytokine production followed by TLR3 activation. In this study we ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2008
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0810357105