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Antimicrobial Agents and Chemotherapy, May 1998, p. 1281-1283, Vol. 42, No. 5
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Properties of Mutant SHV-5 beta -Lactamases Constructed by Substitution of Isoleucine or Valine for Methionine at Position 69

Panagiota Giakkoupi,1 Vivi Miriagou,2 Maria Gazouli,1 Eva Tzelepi,1 Nicholas J. Legakis,3 and Leonidas S. Tzouvelekis1,3,*

Department of Bacteriology1 and Quality Control Laboratory,2 Hellenic Pasteur Institute, and Department of Microbiology, Medical School, Athens University,3 Athens, Greece

Received 8 October 1997/Returned for modification 9 January 1998/Accepted 17 February 1998

The effect of replacement of Met-69 by Ile or Val on the properties of the extended-spectrum beta -lactamase SHV-5 was studied. Mutant enzymes were constructed by site-specific mutagenesis and expressed under isogenic conditions in Escherichia coli DH5alpha cells. Compared with SHV-5, the mutant beta -lactamases conferred lower levels of beta -lactam resistance and were less efficient in hydrolyzing ampicillin, cephalothin, and cefotaxime. The substitutions rendered SHV-5 less susceptible to inhibition by clavulanate, sulbactam, and tazobactam; however, the MICs of penicillin-inhibitor combinations remained similar, suggesting an attenuation of penicillinase activity.

* Corresponding author. Mailing address: Department of Bacteriology, Hellenic Pasteur Institute, Vass. Sofias 127, Athens 11521, Greece. Phone: 30 (1) 6462281. Fax: 30 (1) 6423498. E-mail: Lstbact{at}hotmail.com.

Antimicrobial Agents and Chemotherapy, May 1998, p. 1281-1283, Vol. 42, No. 5
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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