Deletion mutations conferring substrate spectrum extension in the class A β-lactamase

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 f...

Full description

Saved in:

Bibliographic Details
Published in:	Antimicrobial agents and chemotherapy Vol. 58; no. 10; pp. 6265 - 6269
Main Authors:	Hwang, Junghyun, Cho, Kwang-Hwi, Song, Han, Yi, Hyojeong, Kim, Heenam Stanley
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 01-10-2014
Subjects:	beta-Lactamases beta-Lactamases - genetics Burkholderia Burkholderia - enzymology Burkholderia - genetics Burkholderia thailandensis Mechanisms of Resistance Sequence Deletion Sequence Deletion - genetics
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 J.H. and K.-H.C. contributed equally to this work.
ISSN:	0066-4804 1098-6596
DOI:	10.1128/AAC.02648-14