Liver Antioxidant Capacity and Steatosis in Laying Hens Exposed to Various Quantities of Lupin (Lupinus angustifolius) Seeds in the Diet.

Despite the many beneficial properties of legume plants, their use in diets for poultry is limited by the presence of antinutritional factors. The aim of the study was to determine the activity of DT-diaphorase, ethoxycoumarin O-deethylase, and catalase, and the concentration of malondialdehyde in liver tissue, as well as the activity of SOD and CAT in the serum of Hy-line Brown hens fed a diet supplemented with various doses of Lupinus angustifolius seeds. The results indicate that the use of large amounts of lupin in the diet resulted in an increase in MDA concentration in the liver and the lipid vacuolization of hepatocytes. A significant increase in DTD activity was observed in chickens receiving 15% lupin. Regardless of lupin dose, no increase in SOD activity was observed in chicken serum after 33 days of the experiment. From the 66th day of the experiment, an increase in catalase activity in the serum of laying hens was observed, while low activity of this enzyme was found in the liver. It can be concluded that the short-term use of lupin in the diet of laying hens does not affect the activity of antioxidant enzymes and, therefore, does not affect the oxidative-antioxidant balance of their body.

Applying Bipartite Network Analysis and Ordination Technique to Evaluate Long-Term Data from Veterinary-Sanitary Examination of Slaughtered Pigs.

Animal and meat inspections in abattoirs are important in the surveillance of zoonotic diseases. Veterinary inspections in abattoirs can provide useful data for the management of health and welfare issues of humans and animals. Using the network analysis and ordination technique, in this study, we analyzed the data from 11 years of veterinary inspections in pig slaughterhouses from 16 regions in Poland. Based on the huge data set of 80,187,639 cases of diseases and welfare issues of pigs, the most frequent livestock diseases were identified to be abscesses, soiling, faecal or other contaminations, and congestions, which together accounted for 77.6% of the total condemnations. Spatial and temporal differences in swine diseases between the Polish regions were recognized using the above-mentioned statistical approaches. Moreover, with the use of a quite novel method, not used yet in preventive veterinary medicine, called a heatmap, the most problematic disease and welfare issues in each region in Poland were identified. The use of statistical approaches such as network analysis and ordination technique allow for identification of the health and welfare issues in slaughterhouses when dealing with long-term inspection data based on a very large number of cases, and then have to be adopted in current veterinary medicine.

The cross-reactivity of Shewanella fidelis lipopolysaccharide with anti-Proteus antibodies.

The serological cross-reactivity between lipopolysaccharides (LPS) of S. fidelis KMM3582(T) and rabbit anti-O P. mirabilis antibodies was tested. Using ELISA and Western blot cross-reactivity between S. fidelis LPS and antisera against P. mirabilis O14, O3 LPSs was found. The observed cross-reaction may suggest that anti-P. mirabilis S1959 (O3) antibodies may bind to the internal part of S. fidelis O-polysaccharides. A weak interaction between S. fidelis LPS and antiserum against P. mirabilis O13 in Western blot suggests that the absolute configuration of non-sugar "AlaLys" component (N(epsilon)-[(S)-l-carboxyethyl]-N(alpha)-(D-galacturonoyl)-L-lysine) may influence the affinity of antibodies for S. fidelis LPS.

Serotyping of clinical isolates belonging to Proteus mirabilis serogroup O36 and structural elucidation of the O36-antigen polysaccharide.

The O-specific polysaccharide (OPS) isolated from the lipopolysaccharide of Proteus mirabilis O36 was found to have a pentasaccharide repeating unit of the following structure: -->2)-beta-D-Ribf-(1-->4)-beta-D-Galp-(1-->4)-alpha-D-GlcpNAc6Ac-(1-->4)-beta-D-Galp-(1-->3)-alpha-D-GlcpNAc-(1-->. The structure is unique among Proteus OPS, which is in agreement with the classification of this strain into a separate Proteus O-serogroup. Remarkably, the P. mirabilis O36-polysaccharide has the same structure as the OPS of Escherichia coli O153, except that the latter is devoid of O-acetyl groups. The cross-reaction of anti-O36 antibodies with the O-part of E. coli O153 lipopolysaccharide is observed. In the present study, two steps of serotyping Proteus strains are proposed: screening of dry mass with enzyme-linked immunosorbent assay and immunoblot with the crude lipopolysaccharides. This method allowed serotyping of 99 P. mirabilis strains infecting the human urinary tract. Three strains were classified into serogroup O36. The migration pattern of these lipopolysaccharides fraction with long O-specific PSs was similar to the standard laboratory P. mirabilis O36 (Prk 62/57) lipopolysaccharide. The relatively low number of clinical strains belonging to serogroup O36 did not correspond to the presence of anti-P. mirabilis O36 antibodies in the blood donors' sera. Twenty-five percent of tested sera contained a statistically significant elevated level of antibodies reacting with thermostable surface antigens of P. mirabilis O36. The presence and amount of antibodies correlated with Thr399Ile TLR4 polymorphism types (P=0.044).

Structures and serology of the O-antigens of Proteus strains classified into serogroup O17 and former serogroup O35.

INTRODUCTION: Bacteria of the genus Proteus are facultative pathogens which commonly cause urinary tract infections. Based on the serological specificity of the O-chain polysaccharide of the lipopolysaccharide (O-polysaccharide, O-antigen), strains of P. mirabilis and P. vulgaris have been classified into 60 serogroups. Studies on the chemical structure and serological specificity of the O-antigens aim at the elucidation of the molecular basis and improvement of the serological classification of these bacteria. MATERIALS AND METHODS: The O-polysaccharide was prepared by acetic acid degradation of the lipopolysaccharide isolated from dried bacterial mass of each strain by hot phenol/water extraction. (1)H- and (13)C-NMR spectroscopy was used for structural studies. Serological studies were performed with rabbit O-antisera using enzyme immunosorbent assay, passive hemolysis test, and the inhibition of reactions in these assays as well DOC-PAGE and Western blot. RESULTS: Four Proteus strains belonging to serogroups O17 and O35 were found to possess similar O-polysaccharide structures, in particular having the same carbohydrate backbone built up of tetrasaccharide repeating units. However, they differ in the presence or absence of additional substituents, such as phosphoethanolamine in P. mirabilis O17 and glucose in P. penneri O17, as well as in the pattern and degree of O-acetylation of various monosaccharide residues. Serological studies also showed close relationships between the O-antigens studied. CONCLUSIONS: Based on these data it is proposed to reclassify strain P. mirabilis PrK 61/57, formerly representing the O35 serogroup, into the serogroup O17 in the Kauffman-Perch classification system of Proteus.

Synthetic peptides mimicking antigenic epitope of Helicobacter pylori urease.

Short peptides resembling the Helicobacter pylori urease antigen (UreB F8 Ser-Ile-Lys-Glu-Asp-Val-Gln-Phe) with deleted aspartic acid and glutamic acid residues, anchored through a triazine linker via the N-terminal moiety to cellulose plate were prepared. The peptides were used for binding of antibodies from sera of patients with medically confirmed atherosclerosis. Recognition of the peptides was also tested with anti-Jack beans urease antibodies. The important role of a Gly-Gly spacer separating the peptides from the cellulose support was shown. Different patterns of binding of antibodies from H. pylori infected patients and anti-Jack bean urease antibodies were observed only in the case of pentapeptides. The peptide Gly-Gly-Leu-Val-Phe-Lys-Thr was recognized by most of the tested sera.

Synthesis and serological interactions of H. pylori urease fragment 321-339 n-terminally immobilized on the cellulose.

Antigenic epitopes F8 (SIKEDVQF) and UB-33 (UreB fragment with residues 321-339: CHHLDKSIKEDVQFADSRI) in H. pylori urease that induces neutralizing antibody production were prepared on the cellulose plate from N- to C-terminus using CDMT as a coupling reagent. Reaction of both epitopes with sera of patients with medically confirmed atherosclerosis was studied. Strong, selective reactions of both peptides with some patients sera were observed.