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Antimicrobial Agents and Chemotherapy, January 2000, p. 39-42, Vol. 44, No. 1
0066-4804/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Aminoglycoside Resistance in Mycobacterium kansasii, Mycobacterium avium-M. intracellulare, and Mycobacterium fortuitum: Are Aminoglycoside-Modifying Enzymes Responsible?

I. I. Y. Ho, C. Y. Chan,* and A. F. B. Cheng

Department of Microbiology, The Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, N.T., Hong Kong, China

Received 14 May 1999/Returned for modification 11 August 1999/Accepted 14 October 1999

Aminoglycoside acetyltransferase was detected in Mycobacterium 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. kansasii and M. fortuitum displayed relatively high Kms, all at the millimolar level, for substrates including tobramycin, neomycin, and kanamycin A. The Km 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.

* Corresponding author. Mailing address: Department of Microbiology, The Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, N.T., Hong Kong, China. Phone: (852)-26322875. Fax: (852)-26473227. E-mail: chiuychan{at}cuhk.edu.hk.

Antimicrobial Agents and Chemotherapy, January 2000, p. 39-42, Vol. 44, No. 1
0066-4804/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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