Detection of a Quinolone Resistance Mutation in gyrA in Escherichia albertii

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Antimicrobial resistance is a major hurdle impeding infection control and treatment worldwide.There is limited information on the antimicrobial susceptibility of Escherichia albertii, a recently discovered enteropathogen.E. albertii was first described in 2003 following isolation from human stool samples of Bangladeshi children in the early 1990s (1).E. albertii appears to infect both animals and humans, and it may be subclinically carried by wild and domestic birds (2).In Japan, E. albertii has increasingly been reported to be an enteropathogen infecting humans (2).In the Akita Prefecture of Japan, a number of E. albertii strains have been isolated or reidentified from stocks of laboratory E. coli strains (3,4).The purpose of this study was to investigate antimicrobial susceptibility of E. albertii strains.A total of 28 E. albertii strains were used to investigate antimicrobial susceptibility in this study.These strains were isolated from human stool samples in the Akita Prefecture between 1995 and 2017.The susceptibility of E. albertii strains was determined using the BD-Sensi-Disc kit (Nippon Becton Dickinson, Tokyo, Japan), against 11 antimicrobial agents, namely: 10 μg ampicillin (ABPC), 30 μg ceftazidime (CAZ), 30 μg cefotaxime (CTX), 30 μg cefmetazole (CMZ), 10 μg imipenem (IPM), 30 μg kanamycin (KM), 10 μg streptomycin (SM), 50 μg fosfomycin (FOM), 30 μg tetracycline (TC), 30 μg nalidixic acid (NA), and 10 μg norfloxacin (NFLX), on Mueller Hinton agar (Oxoid, Basingstoke, UK).The results were interpreted according to the manufacturer's instructions, based on the criteria outlined by the Clinical and Laboratory Standards Institute document M100-S23 (5).The minimum inhibitory concentration (MIC) of NFLX for NA-resistant strains was determined using the Etest diagnostic kit (bioMérieux, Tokyo, Japan), according to the manufacturer's instructions.Quality controls were performed using E. coli strain ATCC25922.Resistance against quinolones is primarily due to amino acid substitutions in the topoisomerase enzymes, such as DNA gyrase and topoisomerase IV.