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Published on: May 23, 2021
Molecular and biochemical characterization of a novel class A beta-lactamase (HER-1) from Escherichia hermannii
Anne Beauchef-Havard1, Guillaume Arlet, Valerie Gautier
1Service de Bactériologie, Hôpital Cochin, AP-HP, Paris, France.
Abstract:
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).
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