Protein Synthesis as a Basis for Chloramphenicol-Resistance in Staphylococcus aureus

Abstract

IT has been established that chloramphenicol is a specific inhibitor of inducible enzyme formation and of protein synthesis in general¹. The antibiotic does not exert its effect on protein synthesis by inhibition of amino-acid activation, by inhibition of peptide bond formation, or by inhibition of incorporation of amino-acids into cell-wall². Pardee, Paigen and Prestidge³ reported that ribonucleic acid synthesized in the presence of chloramphenicol possessed an electrophoretic mobility which differed from that of normal ribonucleic acid synthesized in the absence of the antibiotic. It was later found by Neidhardt and Gros⁴ that this altered ribonucleic acid was unstable and was rapidly degraded in the absence of chloramphenicol. These observations have prompted the suggestion by Gale⁵ that “chloramphenicol alters, or in some way interferes with the function of the ribonucleic acid component concerned in amino-acid incorporation”.