Patrik Mlynarcik1, Jan Bardon1,2, Miroslava Htoutou Sedlakova1, Petra Prochazkova1, Milan Kolar1,3. 1. Department of Microbiology, Faculty of Medicine and Dentistry, Palacky University Olomouc, Czech Republic. 2. State Veterinary Institute Olomouc, Czech Republic Corresponding author: Patrik Mlynarcik, e-mail. 3. Institute of Molecular and Translation Medicine, Faculty of Medicine and Dentistry, Palacky University Olomouc, Czech Republic.
Abstract
BACKGROUND: Various food-producing animals have been recognized in recent years as a potential reservoir for the spread of antibiotic resistant bacteria that may pose a risk to human health and therefore their dissemination in the food production chain needs to be assessed. METHODS: In this study, 450 boot swabs from chicken farms were analyzed for the presence of antimicrobial resistance with a focus on β-lactams resistance in Acinetobacter species. RESULTS: Two β-lactamase-encoding genes were first time identified in Acinetobacter lwoffii and Acinetobacter schindleri isolates. The deduced amino acid sequence of OXA-496 shared 93.8% identity with OXA-363. The second OXA-134-like enzyme, OXA-537, had the highest sequence identity (97.8%) with OXA-235 and OXA-237. CONCLUSIONS: The results of this study illustrate the occurrence of new OXA-134-like β-lactamases, called OXA-496 and OXA-537, carrying strains of Acinetobacter lwoffii and Acinetobacter schindleri in chicken farm litter, and highlight the possible role of Acinetobacter as a reservoir of resistance genes.
BACKGROUND: Various food-producing animals have been recognized in recent years as a potential reservoir for the spread of antibiotic resistant bacteria that may pose a risk to human health and therefore their dissemination in the food production chain needs to be assessed. METHODS: In this study, 450 boot swabs from chicken farms were analyzed for the presence of antimicrobial resistance with a focus on β-lactams resistance in Acinetobacter species. RESULTS: Two β-lactamase-encoding genes were first time identified in Acinetobacter lwoffii and Acinetobacter schindleri isolates. The deduced amino acid sequence of OXA-496 shared 93.8% identity with OXA-363. The second OXA-134-like enzyme, OXA-537, had the highest sequence identity (97.8%) with OXA-235 and OXA-237. CONCLUSIONS: The results of this study illustrate the occurrence of new OXA-134-like β-lactamases, called OXA-496 and OXA-537, carrying strains of Acinetobacter lwoffii and Acinetobacter schindleri in chicken farm litter, and highlight the possible role of Acinetobacter as a reservoir of resistance genes.