Abstract
We describe four new deletion mutations in a class A β-lactamase PenA in Burkholderia thailandensis, each conferring an extended substrate spectrum. Single-amino-acid deletions T171del, I173del, and P174del and a two-amino-acid deletion, R165-T167delinsP, occurred in the omega loop, increasing the flexibility of the binding cavity. This rare collection of mutations has significance, allowing exploration of the diverse evolutionary trajectories of β-lactamases and as potential future mutations conferring high-level ceftazidime resistance on isolates from clinical settings, compared with amino acid substitution mutations.
Original language | English |
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Pages (from-to) | 6265-6269 |
Number of pages | 5 |
Journal | Antimicrobial Agents and Chemotherapy |
Volume | 58 |
Issue number | 10 |
DOIs | |
Publication status | Published - 2014 Oct 1 |
Bibliographical note
Publisher Copyright:© 2014, American Society for Microbiology. All Rights Reserved.
ASJC Scopus subject areas
- Pharmacology
- Pharmacology (medical)
- Infectious Diseases