There is an increasing demand for non-antibiotics solutions to control infectious disease in intensive pig production. Here, one such alternative, namely pig antibodies purified from slaughterhouse blood was investigated in order to elucidate its potential usability to control post-weaning diarrhoea (PWD), which is one of the top indications for antibiotics usage in the pig production. A very cost-efficient and rapid one-step expanded bed adsorption (EBA) chromatography procedure was used to purify pig immunoglobulin G from slaughterhouse pig plasma (more than 100 litres), resulting in >85% pure pig IgG (ppIgG). The ppIgG thus comprised natural pig immunoglobulins and was subsequently shown to contain activity towards four pig-relevant bacterial strains (three different types of Escherichia coli and one type of Salmonella enterica) but not towards a fish pathogen (Yersinia ruckeri), and was demonstrated to inhibit the binding of the four pig relevant bacteria to a pig intestinal cell line (IPEC-J2). Finally it was demonstrated in an in vivo weaning piglet model for intestinal colonization with an E. coli F4+ challenge strain that ppIgG given in the feed significantly reduced shedding of the challenge strain, reduced the proportion of the bacterial family Enterobacteriaceae, increased the proportion of families Enterococcoceae and Streptococcaceae and generally increased ileal microbiota diversity. Conclusively, our data support the idea that natural IgG directly purified from pig plasma and given as a feed supplement can be used in modern swine production as an efficient and cost-effective means for reducing both occurrence of PWD and antibiotics usage and with a potential for the prevention and treatment of other intestinal infectious diseases even if the causative agent might not be known.
The microheterogeneity components of orosomucoid and the dissociation constants and mobilities of concanavalin A/orosomucoid complexes in crossed afinoirnmunoelectrophoresis with free concanavalin AIn crossed afinoimmunoelectrophoresis with free concanavalin A (Con A) in the first dimension, four orosomucoid components are normally found in human serum. In this study an optimal range of Con A concentration in the first-dimension gel was defined. The most retarded, fourth component of orosomucoid was shown to be a result of entrapment of Con A-binding molecules in the affinity precipitate. The affinities of the second, weakly retarded, component and of the third, strongly retarded, component to a Con A binding site were found to be identical. The mobilities in the first-dimension electrophoresis of the orosomucoid/Con A complexes were found to be significantly different from each other. Compared to the mobility ofthe nonretarded, first, component of orosomucoid, the second component had a mobility of 40 % and the third component had a mobility of 10 %. Differences in the antennary carbohydrate structures on the glycosylation sites of orosomucoid are suggested as an explanation for these observations.
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