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Trends Microbiol. 2003 Apr;11(4):145-8.

Solving staphylococcal resistance to beta-lactams.

Author information

1
Department of Medicine, Division of Infectious Diseases, San Francisco General Hospital, Box 0811, 3rd and Parnassus Avenues, San Francisco, CA 94110, USA. chipc@itsa.ucsf.edu

Abstract

Class resistance to beta-lactam antibiotics in Gram-positive bacteria is mediated by structural changes in transpeptidase penicillin-binding proteins. These structural changes render a complex series of interactions between antibiotic and protein that are energetically unfavorable, such that the active site is inactivated not at all or too slowly to prevent cell-wall synthesis and bacterial growth. Determination of the crystal structure of the low-affinity penicillin-binding protein PBP2a, which mediates beta-lactam antibiotic resistance in staphylococci, has identified the molecular structures and interactions that are responsible for resistance. This information could be useful for designing beta-lactams to overcome these structural impediments, as well as resistance.

PMID:
12706985
DOI:
10.1016/s0966-842x(03)00046-5
[Indexed for MEDLINE]

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