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Antibiotics That Inhibit the Synthesis of Bacterial Proteins, Page 1 of 2
< Previous page Next page > /docserver/preview/fulltext/10.1128/9781555817602/9781555812980_Chap06-1.gif /docserver/preview/fulltext/10.1128/9781555817602/9781555812980_Chap06-2.gifAbstract:
Bacteria need proteins to perform essential functions and to act as structural components of the cell. Thus, it is not surprising that the process of bacterial protein synthesis has been a major target for antibiotics. Mupirocin was ignored for years because it is too toxic for internal use. It has been used primarily as a topical antibiotic to eliminate antibiotic-resistant Staphylococcus aureus from the noses of hospital workers. Aminoglycosides are among the most widely used antibiotics. Streptomycin was one of the earliest antibiotics to enter the market, and it won its discoverer, Selman Waxman, a Nobel Prize. One way bacteria can become resistant to aminoglycosides is to mutate the ribosomal protein that provides the binding site for the antibiotic. The antibiotic no longer binds to the ribosome and thus no longer inhibits growth of the bacteria. Tetracycline, like streptomycin, binds to the small subunit of the bacterial ribosome. The tetracycline family, which includes such antibiotics as doxycycline, oxytetracycline, and demeclocycline, gets its name from its structure, which consists of four fused cyclic rings. The chapter describes three known mechanisms of resistance to tetracycline. Another widely used class of antibiotics is the macrolides. Erythromycin is an example of a macrolide. Erythromycin and other macrolides have had an excellent safety record, with few side effects. The chapter also talks about clindamycin, synercid, and oxazolidones.