Abstract
During a study to investigate the evolution of ampicillin resistance in Enterococcus faecium, we observed that a number of E. faecium strains, mainly from the recently described subclade A2, showed PBP5 sequences in between PBP5-S and PBP5-R. These hybrid PBP5-S/R patterns reveal a progression of amino acid changes from the S form to the R form of this protein; however, these changes do not strictly correlate with changes in ampicillin MICs.
Copyright © 2014, American Society for Microbiology. All Rights Reserved.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alleles
-
Amino Acid Sequence
-
Ampicillin / pharmacology
-
Ampicillin Resistance / genetics*
-
Anti-Bacterial Agents / pharmacology
-
Enterococcus faecium / drug effects*
-
Enterococcus faecium / enzymology*
-
Enterococcus faecium / genetics
-
Escherichia coli Proteins / genetics*
-
Genetic Variation
-
Microbial Sensitivity Tests
-
Molecular Sequence Data
-
Penicillin-Binding Proteins / genetics*
-
Protein Isoforms / genetics
Substances
-
Anti-Bacterial Agents
-
Escherichia coli Proteins
-
PBP5 protein, E coli
-
Penicillin-Binding Proteins
-
Protein Isoforms
-
Ampicillin
Associated data
-
GENBANK/KJ742831
-
GENBANK/KJ742832
-
GENBANK/KJ742833
-
GENBANK/KJ742834
-
GENBANK/KJ742835