Genetic and biochemical properties of AER-1, a novel carbenicillin-hydrolyzing beta-lactamase from Aeromonas hydrophila
Author(s) -
R. W. Hedges,
Antone A. Medeiros,
Menashi A. Cohenford,
George A. Jacoby
Publication year - 1985
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.27.4.479
Subject(s) - aeromonas hydrophila , carbenicillin , biology , plasmid , microbiology and biotechnology , escherichia coli , transposable element , gene cluster , aeromonas , genetics , gene , ampicillin , bacteria , antibiotics , mutant
A novel carbenicillin-hydrolyzing beta-lactamase has been discovered in a blood isolate of Aeromonas hydrophila. The enzyme resembles plasmid-determined carbenicillinases in substrate profile but differs in isoelectric point (pI 5.9) and molecular weight (22,000) and has been termed AER-1. No evidence for a plasmid location could be obtained in A. hydrophila, but the AER-1 gene and resistance to chloramphenicol, streptomycin, and sulfonamide could be transferred by mobilization with IncP plasmids to Escherichia coli, where the gene cluster inserted at a unique chromosomal site. The linked resistances are similar to those found on multiresistance beta-lactamase transposons, but since insertion of the A. hydrophila gene cluster was site specific and recA+ dependent, the cluster is not a functional transposon.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom