Aminoglycoside Resistance in Mycobacterium kansasii,Mycobacterium avium-M. intracellulare, andMycobacterium fortuitum: Are Aminoglycoside-Modifying Enzymes Responsible?
ABSTRACT Aminoglycoside acetyltransferase was detected inMycobacterium kansasii and M. fortuitum but not in M. avium-M. intracellulare when they were screened by a radioassay. Aminoglycoside phosphotransferase and nucleotidyltransferase activities were absent from all three species tested. Acetyltransferases from both M. kansasiiand M. fortuitum displayed relatively highKm s, all at the millimolar level, for substrates including tobramycin, neomycin, and kanamycin A. TheKm of each substrate was well above the corresponding maximum achievable level in serum. The low affinities of these enzymes for their substrates suggested that drug modification in vivo was very unlikely. Among the various substrates tested, no apparent positive correlation was found between substrate affinity and resistance level. The presence of aminoglycoside-modifying enzymes in these mycobacterial species was therefore not shown to confer resistance to aminoglycosides.