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Mechanisms of methicillin resistance in Staphylococcus aureus

Peacock, Sharon J.; Paterson, Gavin K.

Authors

Sharon J. Peacock

Gavin K. Paterson

Abstract

Staphylococcus aureus is a major human and veterinary pathogen worldwide. Methicillin-resistant S. aureus (MRSA) poses a significant and enduring problem to the treatment of infection by such strains. Resistance is usually conferred by the acquisition of a nonnative gene encoding a penicillin-binding protein (PBP2a), with significantly lower affinity for β-lactams. This resistance allows cell-wall biosynthesis, the target of β-lactams, to continue even in the presence of typically inhibitory concentrations of antibiotic. PBP2a is encoded by the mecA gene, which is carried on a distinct mobile genetic element (SCCmec), the expression of which is controlled through a proteolytic signal transduction pathway comprising a sensor protein (MecR1) and a repressor (MecI). Many of the molecular and biochemical mechanisms underlying methicillin resistance in S. aureus have been elucidated, including regulatory events and the structure of key proteins. Here we review recent advances in this area.

Journal Article Type Review
Publication Date Jun 2, 2015
Journal Annual review of biochemistry
Print ISSN 0066-4154
Electronic ISSN 1545-4509
Publisher Annual Reviews
Peer Reviewed Peer Reviewed
Volume 84
Issue 1
Pages 577-601
Institution Citation Peacock, S. J., & Paterson, G. K. (2015). Mechanisms of methicillin resistance in Staphylococcus aureus. Annual review of biochemistry, 84(1), 577-601. doi:10.1146/annurev-biochem-060614-034516
DOI https://doi.org/10.1146/annurev-biochem-060614-034516
Keywords Methicillin resistance; Staphylococcus aureus; Antibiotic resistance; Penicillin-binding protein; β-lactam antibiotics; MRSA
Publisher URL http://arjournals.annualreviews.org/eprint/NE4Ir8fN2bgbSsINVY2S/full/10.1146/annurev-biochem-060614-034516
Copyright Statement ©2016 University of Hull
Additional Information This is a description of an article publised in Annual review of biochemistry, 2015, v.84. The weblink provides complimentary access to the review from Annual Reviews.