Molecular and biochemical characterization of a novel class A beta-lactamase (HER-1) from Escherichia hermannii.
Antimicrob Agents Chemother
; 47(8): 2669-73, 2003 Aug.
Article
en En
| MEDLINE
| ID: mdl-12878539
Escherichia hermannii showed a low level of resistance to amoxicillin and ticarcillin, reversed by clavulanate, and a moderate susceptibility to piperacillin but was susceptible to all cephalosporins. A bla gene was cloned and encoded a typical class A beta-lactamase (HER-1, pI 7.5), which shares 45, 44, 41, and 40% amino acid identity with other beta-lactamases, AER-1 from Aeromonas hydrophila, MAL-1/Cko-1 from Citrobacter koseri, and TEM-1 and LEN-1, respectively. No ampR gene was detected. Only penicillins were efficiently hydrolyzed, and no hydrolysis was observed for cefuroxime and broad-spectrum cephalosporins. Sequencing of the bla gene in 12 other strains showed 98 to 100% identity with bla(HER-1).
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Beta-Lactamasas
/
Escherichia
Idioma:
En
Revista:
Antimicrob Agents Chemother
Año:
2003
Tipo del documento:
Article
País de afiliación:
Francia