NDLI: Identification of a structural determinant for resistance to beta-lactam antibiotics in Gram-positive bacteria.

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Identification of a structural determinant for resistance to beta-lactam antibiotics in Gram-positive bacteria.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Petit, I. Dupont, Y. Di Guilmi, A. M. Hakenbeck, R. Vernet, T. Pétillot, Y. Gordon, E. Mouz, N. Dideberg, O.
Description	Author Affiliation: Mouz N ( Laboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale Jean-Pierre Ebel (Commissariat à l'Energie Atomique-Centre National de la Recherche Scientifique), 41, avenue des Martyrs, F-38027 Grenoble Cedex 1, France.);
Abstract	Streptococcus pneumoniae is the main causal agent of pathologies that are increasingly resistant to antibiotic treatment. Clinical resistance of S. pneumoniae to beta-lactam antibiotics is linked to multiple mutations of high molecular mass penicillin-binding proteins (H-PBPs), essential enzymes involved in the final steps of bacterial cell wall synthesis. H-PBPs from resistant bacteria have a reduced affinity for beta-lactam and a decreased hydrolytic activity on substrate analogues. In S. pneumoniae, the gene coding for one of these H-PBPs, PBP2x, is located in the cell division cluster (DCW). We present here structural evidence linking multiple beta-lactam resistance to amino acid substitutions in PBP2x within a buried cavity near the catalytic site that contains a structural water molecule. Site-directed mutation of amino acids in contact with this water molecule in the 'sensitive' form of PBP2x produces mutants similar, in terms of beta-lactam affinity and substrate hydrolysis, to altered PBP2x produced in resistant clinical isolates. A reverse mutation in a PBP2x variant from a clinically important resistant clone increases the acylation efficiency for beta-lactams and substrate analogues. Furthermore, amino acid residues in contact with the structural water molecule are conserved in the equivalent H-PBPs of pathogenic Gram-positive cocci. We suggest that, probably via a local structural modification, the partial or complete loss of this water molecule reduces the acylation efficiency of PBP2x substrates to a point at which cell wall synthesis still occurs, but the sensitivity to therapeutic concentrations of beta-lactam antibiotics is lost.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Carrier Proteins Chemistry Genetics Hexosyltransferases Muramoylpentapeptide Carboxypeptidase Peptidyl Transferases Streptococcus Pneumoniae Beta-Lactam Resistance Amino Acid Substitution Mutagenesis, Site-Directed Penicillin-Binding Proteins Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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