Open AccessSubstitution of alanine for aspartate at position 179 in the SHV‐6 extended‐spectrum β‐lactamase
Author(s) -
Arlet Guillaume,
Rouveau Martine,
Philippon Alain
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10423.x
Subject(s) - klebsiella pneumoniae , ceftazidime , amino acid substitution , alanine , point mutation , mutagenesis , biology , nucleotide , gene , nucleic acid sequence , microbiology and biotechnology , klebsiella , substitution (logic) , genetics , amino acid , bacteria , escherichia coli , mutation , pseudomonas aeruginosa , computer science , programming language
SHV‐6 was previously identified by its susceptibility pattern and biochemical criteria in a clinical isolate of Klebsiella pneumoniae which was resistant to ceftazidime. It contains only a single point difference with the βla SHV‐1 gene as determined by PCR amplification and nucleotide sequencing. This is the result of a single amino acid substitution, Ala for Asp, at position 179. Directed mutagenesis experiments have shown this substitution to confer selective resistance to ceftazidime in the TEM family.