Demonstration of a functional variant of chloramphenicol acetyltransferase in Haemophilus influenzae.
Seven clinical isolates of chloramphenicol-resistant Haemophilus influenzae were studied. The products of chloramphenicol inactivation by chloramphenicol acetyltransferase (CAT) were identified by high performance liquid chromatography. The sole product in H. influenzae is a single monoacetyl compound, whereas variants of CAT isolated from other chloramphenicol-resistant bacteria usually produce both monoacetyl and diacetyl chloramphenicol metabolites. The chloramphenicol resistance gene was found to reside on a 65-kb plasmid which, in five of the six cases studied, appeared to be integrated into the host cell chromosome.
Smith
M D
MD
Department of Microbiology, Whittington Hospital, London.
Kelsey
M C
MC
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D015500:Chloramphenicol O-Acetyltransferase / Q000235:genetics* / Q000378:metabolism; D004352:Drug Resistance, Microbial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D014644:Genetic Variation; D006193:Haemophilus influenzae / Q000187:drug effects / Q000201:enzymology / Q000235:genetics*; D008826:Microbial Sensitivity Tests; D011815:R Factors
D000900:Anti-Bacterial Agents; D015500:Chloramphenicol O-Acetyltransferase