Fosmid cloning, nucleotide sequence, and characterization of a beta-lactamase gene from subsurface isolates

2012 ◽  
Vol 50 (4) ◽  
pp. 680-683
Author(s):  
Nurcan Vardar ◽  
Gölnül Vardar-Schara
1999 ◽  
Vol 13 (2) ◽  
pp. 82-88 ◽  
Author(s):  
Hiroshi Ogawara ◽  
Youko Katashiro ◽  
Kyoichiro Higashi ◽  
Hiroaki Urabe

1990 ◽  
Vol 34 (7) ◽  
pp. 1444-1446 ◽  
Author(s):  
A Garbarg-Chenon ◽  
V Godard ◽  
R Labia ◽  
J C Nicolas

1996 ◽  
Vol 40 (9) ◽  
pp. 2080-2086 ◽  
Author(s):  
B A Rasmussen ◽  
K Bush ◽  
D Keeney ◽  
Y Yang ◽  
R Hare ◽  
...  

In 1984, a year prior to the U.S. approval of imipenem for clinical use, a wound isolate and a bile isolate of Enterobacter cloacae were obtained from two patients in a California hospital. These isolates were resistant to imipenem, penicillins, and inhibitor combinations; early cephalosporins such as cephalothin, cefamandole, and cefoxitin; and cefoperazone. However, they were susceptible (MICs, < 4 micrograms/ml) to cefotaxime, ceftriaxone, ceftazidime, and moxalactam. Both strains produced an apparent TEM-1 beta-lactamase; an inducible NmcA-type imipenem-hydrolyzing beta-lactamase, IMI-1, with a pl of 7.05; and an inducible beta-lactamase with a pI of 8.1, typical of an E. cloacae AmpC beta-lactamase. Purified IMI-1 hydrolyzed imipenem and benzylpenicillin at modest rates, but more slowly than cephaloridine. The enzyme was inhibited by clavulanic acid and tazobactam. EDTA did not inhibit the cephaloridine-hydrolyzing activity. The beta-lactamase gene encoding IMI-1, imiA1, was cloned from E. cloacae 1413B. Sequence analysis identified the imiA1 gene as encoding a class A serine beta-lactamase. Both the imiA1 DNA and encoded amino acid sequences shared greater than 95% identity with the NmcA gene and its encoded protein. DNA sequence analysis also identified a gene upstream of imiA1 that shares > 95% identity with nmcR and that may encode a regulatory protein. In conclusion, IMI-1, a carbapenem-hydrolyzing beta-lactamase inhibited by clavulanic acid, was identified as a group 2f, class A, carbapenem-hydrolyzing cephalosporinase.


1995 ◽  
Vol 39 (6) ◽  
pp. 1379-1382 ◽  
Author(s):  
E. Scoulica ◽  
A. Aransay ◽  
Y. Tselentis

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