Antibiotics: Actions, Origins, Resistance by Christopher Walsh

By Christopher Walsh

A entire account of the structural periods of antibiotics that experience impacted human infectious ailment. • presents an creation to antibiotics and examines how antibiotics block particular proteins appearing in crucial bacterial strategies and the way the molecular constitution of the small-molecule medicines permits their antibiotic task. • Explores the advance of bacterial resistance to antibiotics, together with the molecular common sense that microbial manufacturers of antibiotics use for self-protection. • Addresses the molecular common sense of antibiotic biosynthesis, beginning with regulatory networks that keep watch over gene transcription of secondary metabolites in streptomycetes, and examines the clients for broadening the bottom of bacterial ambitions and in addition the place new antibiotics are inclined to emerge, together with either artificial chemical efforts and traditional items.

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The space-filling model shows the optimized tightness of fit of antibiotic for its target. There are two kinds of PG units that have the intact pentapeptide strand, the lipid II molecules at the periplasmic face of the membrane, and also strands as yet un-cross-linked in polymerized PG (Fig. 21). The steric blockade of the transpeptidation can also have effects on transglycosylases, especially in the bifunctional, high-molecularweight PBPs. Different members of the vancomycin glycopeptide antibiotic family have different tendencies to dimerize, and this may enable an enhanced avidity for complexation with PG termini (Williams, 1996).

Once facing outside and presumably anchored at the membrane surface by the C55 lipid tail, the disaccharyl pentapeptide unit is substrate for transglycosylases and transpeptidases that are also membrane bound (Fig. 3). There are multiple transglycosylases (four known in the E. coli genome and two in the Staphylococcus aureus and Streptococcus pneumoniae genomes) and multiple transpeptidases. Some of them are bifunctional with discrete transglycosylase and transpeptidase domains (Spratt, 1994), and members of this subset are of particular importance as killing targets of ␤-lactam antibiotics, as will be noted below.

8 (A) Sequential action of alanine racemase and D-Ala-D-Ala ligase (Ddl) to generate D-Ala-D-Ala. (B) D-Ala-P intermediate in Ddl catalysis. creating toxicity. These examples suggest that all eight enzymes noted above are in principle good targets for new antibiotic development. We will return to the D,D-ligase story when we discuss vancomycin resistance in chapter 10 and observe that glycopeptide antibiotic resistance centers around D,D-ligase specificity. Enzymes that provide D-glutamate and meso-DAP for MurD and MurE The pathways to D-glutamate have been reviewed recently (van Heijenoort, 2001b) and involve either a glutamate racemase encoded by the murI gene or a D-amino acid transaminase pathway.

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