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Antimicrobial Agents and Chemotherapy, August 2001, p. 2393-2396, Vol. 45, No. 8
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.8.2393-2396.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Alterations in MurM, a Cell Wall Muropeptide Branching Enzyme, Increase High-Level Penicillin and Cephalosporin Resistance in Streptococcus pneumoniae

Anthony M. Smith1,* and Keith P. Klugman1,2

Pneumococcal Diseases Research Unit, Department of Clinical Microbiology and Infectious Diseases, South African Institute for Medical Research, Johannesburg, South Africa,1 and Departments of International Health and Infectious Diseases, Emory University, Atlanta, Georgia2

Received 1 December 2000/Returned for modification 23 March 2001/Accepted 5 May 2001

We report that alteration in MurM, an enzyme involved in the biosynthesis of branched-stem cell wall muropeptides, is required for maximal expression of penicillin and cefotaxime resistance in the pneumococcus. Hungarian isolate 3191 (penicillin MIC, 16 µg/ml; cefotaxime MIC, 4 µg/ml) was a source of donor DNA in transformation experiments. Penicillin-binding protein DNA was insufficient to transform recipient strain R6 to full resistance. Further transformation with altered murM DNA was required for full expression of donor penicillin and cefotaxime resistance.

* Corresponding author. Mailing address: MRC/SAIMR/WITS Pneumococcal Diseases Research Unit, Department of Clinical Microbiology and Infectious Diseases, South African Institute for Medical Research, P.O. Box 1038, Johannesburg, 2000, South Africa. Phone: 27-011-4899335. Fax: 27-011-4899332. E-mail: anthonys{at}mail.saimr.wits.ac.za.

Antimicrobial Agents and Chemotherapy, August 2001, p. 2393-2396, Vol. 45, No. 8
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.8.2393-2396.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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