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Staphylococcal methicillin resistance: Fine focus on folds and functions

AuthorsMallorquí-Fernández, Goretti; Marrero, Aniebrys ; García-Piqué, Sonia; García-Castellanos, Raquel; Gomis-Rüth, F. Xavier ; Gomis-Rüth, F. Xavier
KeywordsDD, Dimerisation domain
DBD, DNA-binding domain
BLA, β-lactam antibiotic
X-ray crystal structure
Staphylococcus aureus
Three-dimensional structure
Bacterial antibiotic resistance
MRSA, Methicillin-resistant Staphylococcus aureus
MSSA, Methicillin-susceptible Staphylococcus aureus
NPBD, Non-penicillin-binding domain
PBP, Penicillin-binding protein
Issue Date28-Apr-2004
PublisherBlackwell Publishing
CitationFEMS Microbiology Letters 235(1): 1-8 (2004)
AbstractGlobalisation has entailed a massive increase in trade and human mobility facilitating the rapid spread of infectious agents, including those that are drug resistant. A particularly serious threat to human health is posed by methicillin-resistant staphylococcal strains which have acquired molecular mechanisms to evade the action of β-lactam antibiotics (BLAs). Full expression of high-level methicillin resistance involves a complex network of molecules and depends primarily on sufficient expression of a penicillin-binding protein with low sensitivity towards BLAs. Other factors include the fine-tuned regulation of autolytic activity of cell-wall components, as well as an optimal rate of peptidoglycan precursor formation and a highly specific peptidoglycan precursor structure. Three-dimensional structural data are available on several of the pieces involved in the jigsaw puzzle and provide a molecular basis for the understanding of methicillin resistance and for the design of new therapeutic strategies. © 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
Publisher version (URL)http://dx.doi.org/10.1016/j.femsle.2004.04.035
Identifiersdoi: 10.1016/j.femsle.2004.04.035
issn: 0378-1097
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