How different is the proteome of the extended spectrum β-lactamase producing Escherichia coli strains from seagulls of the Berlengas natural reserve of Portugal?
β-Lactam antibiotics like cefotaxime are the most commonly used antibacterial agents. Escherichia coli strains 5A, 10A, 12A and 23B isolated from Seagulls feces, are cefotaxime-resistant strains that produces extended-spectrum beta-lactamases. Bacterial resistance to these antibiotics occurs predominantly through structural modification on the penicillin-binding proteins and enzymatic inactivation by extended-spectrum β-lactamases. Using classical proteomic techniques (2D-GE) coupled to mass spectrometry and bioinformatics extended analysis, in this study, we report several significant differences in cytoplasmic proteins expression when the strains were submitted to antibiotic stress and when the resistant strains were compared with a non-resistant strain. A total of 79 differentially expressed spots were collected for protein identification. Significant level of expression was found in antibiotic resistant proteins like β-lactamase CTX-M-1 and TEM and also in proteins related with oxidative stress. This approach might help us understand which pathways form barriers for antibiotics, another possible new pathways involved in antibiotic resistance to devise appropriate strategies for their control already recognized by the World Health Organization and the European Commission.



This study highlights the protein differences when a resistant strain is under antibiotic pressure and how different can be a sensible and resistant strain at the protein level. This survey might help us to understand the specifics barriers for antibiotics and which pathways are involved in its resistance crosswise the wildlife.
Functional Genomics and Proteomics Unit, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal; Department of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal.
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Monteiro
UR454 Microbiology, Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rhône-Alpes, site de Theix, Saint-Genès Champanelle, France; Plate-Forme d'Exploration du Métabolisme composante protéomique, UR370 QuaPA, Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rhône-Alpes, site de Theix, Saint-Genès Champanelle, France.
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Hébraud
UR454 Microbiology, Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rhône-Alpes, site de Theix, Saint-Genès Champanelle, France.
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Chafsey
Veterinary Science Department, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal; UCIBIO-REQUIMTE, Faculty of Science and Technology, University NOVA of Lisbon, Caparica, Portugal.
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Poeta
Functional Genomics and Proteomics Unit, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal; Department of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal; UCIBIO-REQUIMTE, Faculty of Science and Technology, University NOVA of Lisbon, Caparica, Portugal. Electronic address: gigrejas@utad.pt.
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Igrejas
D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D046091:Charadriiformes / Q000382:microbiology*; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000201:enzymology*; D018384:Oxidative Stress / Q000187:drug effects; D011174:Portugal; D020543:Proteome / Q000032:analysis*; D001618:beta-Lactamases
D000900:Anti-Bacterial Agents; D020543:Proteome; D001618:beta-Lactamases
Antibiotic resistance; Cefotaxime; Escherichia coli; Proteomics; Wild life