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Impact of Probiotics on Animal Health
Published in Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani, Lactic Acid Bacteria, 2020
Sabrina da Silva Sabo, Elías Figueroa Villalobos, Anna Carolina Meireles Piazentin, André Moreni Lopes, Ricardo Pinheiro de Souza Oliveira
Increasing evidences led the World Health Organization (WHO) to become aware of the importance of this subject, suggesting periodically over the last few years the phase out or even the complete banishment of using AGPs (WHO 1997, 2004, 2017). The European Commission (EC) banned the marketing and use of AGPs in feed nutrition since January 1st 2006 (EC Regulation No. 1831/2003), although ionophores continue to be administered (Economou and Gousia 2015). In the United States, the use of fluoroquinolones in poultry was banned in 2005. After that, the rise of fluoroquinolone-resistant Campylobacter infections in humans has significantly decreased (FDA 2018). However, other than this action, little has been effectively done by regulatory authorities to reduce inappropriate and unnecessary use of antibiotics on livestock. In South America, Brazil, known as the second largest poultry producer (Ferreira et al. 2018), following the recommendations of the international agencies such as Food and Agriculture Organization of the United States (FAO), OIE World Organization for Animal Health, and the EC, and based on scientific evidence for the analysis of risks associated with veterinary drug residues in foods, has restricted since 1998 the use of antibiotics avoparcin, amphiphilic, tetracyclines, penicillins, cephalosporins, quinolones, sulfonamides, erythromycin, spiramycin, and recently colistin (Bezerra et al. 2017).
Use of Critically Important Antimicrobials in Food Production
Published in M. Lindsay Grayson, Sara E. Cosgrove, Suzanne M. Crowe, M. Lindsay Grayson, William Hope, James S. McCarthy, John Mills, Johan W. Mouton, David L. Paterson, Kucers’ The Use of Antibiotics, 2017
Many classes of antibiotics used in food animals are the same as used in people. This includes groups classified as “critically important” for human use by the WHO (WHO, 2011; WHO, 2013; Collignon et al., 2009). Although many antibiotics can be the same as those used in humans (e.g. ampicillin), others are in the same class but are not used in people. These agents often have unfamiliar names to medical workers but nevertheless are from similar drug classes as agents used in human health. For example, ceftiofur is a commonly used third-generation cephalosporin in animal production but in fact is very similar to ceftriaxone (see Chapter 27, Ceftriaxone). Similarly, tylosin is a high-volume usage macrolide administered only in animals, and avoparcin is a glycopeptide similar to vancomycin (see Chapter 43, Vancomycin), which was used as an animal growth promoter.
Improving the attrition rate of Lanthipeptide discovery for commercial applications
Published in Expert Opinion on Drug Discovery, 2018
Finding a suitable heterologous organism to produce new lanthipeptides can be a good alternative. Lactococcus lactis, the producing strain of nisin, has been developed into the NIsin Controlled gene Expression system for more than 20 years [39]. Briefly, when a gene of interest, usually the structural gene of a lanthipeptide, is placed downstream of the promotor of nisA, expression of that gene can be induced by adding subinhibitory amounts of nisin (0.1–5 ng/ml) to the culture. Subsequently, the product is expected to be modified by dehydratase NisB [40] and cyclase NisC [41]. With leader peptide gene sequence of nisin attached, a novel type II two-component lanthipeptide pneumococcins A1 and A2 with no homology to nisin was expressed and modified [31], as was demonstrated by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and 1-cyano-4-dimethylaminopyridinium tetrafluoroborate (CDAP) modification of the products. Together with the fact that the produced lanthipeptide is active against Micrococcus flavus, the correct PTM modifications are likely to have formed. In a more recent study, nisin expression system was used to produce at least five novel bioactive lanthipeptides [34]. Out of 54 novel putative lanthipeptides that were identified by genome mining using BAGEL3, 5 novel lanthipeptides were successfully expressed with activity against selected pathogenic bacteria using the nisin producing strain. Flavucin, one of the most active lanthipeptides, was twofold more active than nisin against a vancomycin and avoparcin-resistant Enterococcus faecium strain.