Dietary Se deficiency dysregulates metabolic and cell death signaling in aggravating the AFB1 hepatotoxicity of chicks.

The objective of this study was to use isobaric tags for relative and absolute quantitation (iTRAQ) proteomic technology to systematically analyze the hepatotoxic mechanism of aflatoxin B1 (AFB1) and its prevention by Se in broilers. Four groups of day-old broilers were allocated into a 2 × 2 factorial design trial that fed a Se-deficient based diet (BD) or the BD + 1.0 mg AFB1/kg, 0.3 mg Se/kg, or 1.0 mg AFB1/kg plus 0.3 mg Se/kg for 3 wk. Dietary AFB1 increased serum ALT and decreased total protein and albumin concentrations, and induced hepatic histopathological lesions in Se adequate groups. Notably, Se deficiency exacerbated these AFB1-induced changes. Furthermore, Se deficiency reduced hepatic glutathione peroxidase but increased thioredoxin reductase and glutathione S-transferase activities and 8-hydroxydeoxyguanosine concentration in AFB1 administrated groups. Moreover, AFB1 dysregulated 261 co-differentially expressed proteins (DEPs) in both Se adequate and deficiency diets, and Se deficiency dysregulated 64 DEPs in AFB1 administrated diets. These DEPs are mainly related to phase I and II metabolizing enzymes, heat shock proteins, DNA repair, fatty acid metabolism and apoptosis. The in vitro study has verified that aldo-keto reductase family1, member10 plays an important role in AFB1-induced hepatotoxicity and Se-mediated detoxification of AFB1 in a chicken leghorn male hepatoma cells. Conclusively, this study has analyzed the hepatic proteome response to dietary AFB1 and Se, and thus shed new light on the mechanisms of hepatotoxicity of AFB1 and its detoxification by Se in broilers.

Increased Consumption of Sulfur Amino Acids by Both Sows and Piglets Enhances the Ability of the Progeny to Adverse Effects Induced by Lipopolysaccharide.

This study determined the effects of increased consumption of sulfur amino acids (SAA), as either DL-Met or Hydroxy-Met (OH-Met), by sows and piglets on their performance and the ability of the progeny to resist a lipopolysaccharide (LPS) challenge. Thirty primiparous sows were fed a diet adequate in SAA (CON) or CON + 25% SAA, either as DL-Met or OH-Met from gestation day 85 to postnatal day 21. At 35 d old, 20 male piglets from each treatment were selected and divided into 2 groups (n = 10/treatment) for a 3 × 2 factorial design [diets (CON, DL-Met or OH-Met) and challenge (saline or LPS)]. OH-Met and/or DL-Met supplementation increased (p ≤ 0.05) piglets' body weight gain during day 0-7 and day 7-14. Sow's milk quality was improved in the supplemented treatments compared to the CON. The LPS challenge decreased (p ≤ 0.05) piglets' performance from 35 to 63 d and increased (p ≤ 0.05) the levels of aspartate aminotransferase, total bilirubin, IL-1ß, IL-6, TNF-a, and malondialdehyde. Plasma albumin, total protein, total antioxidant capacity and glutathione peroxidase decreased post-challenge. The results were better with OH-Met than DL-Met. The increase of Met consumption, particularly as OH-Met increased piglets' growth performance during the lactation phase and the challenging period.

Efficacy of 2-hydroxy-4-methylthiobutanoic acid compared to DL-Methionine on growth performance, carcass traits, feather growth, and redox status of Cherry Valley ducks.

The objective of this study was to compare the bio-efficacy of 2-hydroxy-4-methylthiobutanoic acid (DL-HMTBA) with that of DL-methionine (DLM) as sources of methionine in terms of the growth performance, carcass traits, feather growth, and redox statuses of Cherry Valley ducks. Six hundred and thirty male ducks were randomly allotted to 9 dietary treatment groups with 7 replicates of 10 birds each. The first group received a basal diet (BD) without methionine addition that was deficient in the total number of sulfur amino acids. In Groups 2 to 5 and Groups 6 to 9, the BD was supplemented with 4 increasing doses of methionine as either DLM or DL-HMTBA. The trial was run from ages 1 to 42 d. Dietary supplementation with DLM and DL-HMTBA improved body weight gain and feed intake as well as weights of carcasses, breast meat, and feathers compared with the BD. No significant difference was observed between the 2 methionine sources on growth performance, carcass traits, and feather growth. Concentrations of some redox markers in the pectoralis major muscle were improved by addition of methionine to the BD. However, a significant difference was observed between DLM and DL-HMTBA in this respect, as the supplementation of DL-HMTBA significantly increased the total antioxidant capacity, the activities of glutathione peroxidase, and the concentration of reduced glutathione in the pectoralis major muscle, compared with DLM. No significant difference between methionine sources was found with regard to the concentrations of oxidized glutathione and malondialdehyde in the pectoralis major muscle. Both DLM and DL-HMTBA increased malondialdehyde concentrations in the pectoralis major muscle compared with the BD. In conclusion, these results indicated that DLM and DL-HMTBA have equal biological value for the growth performance, carcass traits, and feather growth of Cherry Valley duck. Moreover, the improved antioxidant capacity observed with DL-HMTBA makes this a better candidate than DLM for lowering the oxidation process in the meat during post-mortem storage and thereby contributes to a better duck meat quality.

Effects of recombinant Agrocybe aegerita lectin as an immunoadjuvant on immune responses.

CONTEXT: Accumulated evidence has indicated that recombinant Agrocybe aegerita lectin (AAL) possesses immunoadjuvant activity to enhance antigen-specific immune responses. However, the mechanism of how AAL regulates immune response remains poorly defined. AIM: This study is aimed to reveal the mechanism of AAL's immunoadjuvant activity. METHODS: In this study, AAL alone or combined with inactivated avian influenza virus H9N2 was immunized to mice and the transcriptome profile of immunized mice was analyzed. RESULTS: In line with previous studies, our results showed that H9N2-specific IgG level was significantly increased in AAL-treated mice, suggesting the immunoadjuvant activity of AAL. More importantly, transcriptome data revealed that genes participating in the primary adherence, lymphocyte activation, secondary adherence and transmembrane migration of leukocyte migration, were up-regulated by AAL. CONCLUSION: These findings suggest that AAL exerts immunoadjuvant effects by promoting chemotaxis and phagotrophy activity of neutrophil leucocyte and macrophage to improve innate immunity and antigen presentation.

Adjuvant effects mediated by the carbohydrate recognition domain of Agrocybe aegerita lectin interacting with avian influenza H9N2 viral surface glycosylated proteins.

OBJECTIVE: To evaluate the potential adjuvant effect of Agrocybe aegerita lectin (AAL), which was isolated from mushroom, against a virulent H9N2 strain in vivo and in vitro. METHODS: In trial 1, 50 BALB/c male mice (8 weeks old) were divided into five groups (n=10 each group) which received a subcutaneous injection of inactivated H9N2 (control), inactivated H9N2+0.2% (w/w) alum, inactivated H9N2+0.5 mg recombinant AAL/kg body weight (BW), inactivated H9N2+1.0 mg AAL/kg BW, and inactivated H9N2+2.5 mg AAL/kg BW, respectively, four times at 7-d intervals. In trial 2, 30 BALB/c male mice (8 weeks old) were divided into three groups (n=10 each group) which received a subcutaneous injection of inactivated H9N2 (control), inactivated H9N2+2.5 mg recombinant wild-type AAL (AAL-wt)/kg BW, and inactivated H9N2+2.5 mg carbohydrate recognition domain (CRD) mutant AAL (AAL-mutR63H)/kg BW, respectively, four times at 7-d intervals. Seven days after the final immunization, serum samples were collected from each group for analysis. Hemagglutination assay, immunogold electron microscope, lectin blotting, and co-immunoprecipitation were used to study the interaction between AAL and H9N2 in vitro. RESULTS: IgG, IgG1, and IgG2a antibody levels were significantly increased in the sera of mice co-immunized with inactivated H9N2 and AAL when compared to mice immunized with inactivated H9N2 alone. No significant increase of the IgG antibody level was detected in the sera of the mice co-immunized with inactivated H9N2 and AAL-mutR63H. Moreover, AAL-wt, but not mutant AAL-mutR63H, adhered to the surface of H9N2 virus. The interaction between AAL and the H9N2 virus was further demonstrated to be associated with the CRD of AAL binding to the surface glycosylated proteins, hemagglutinin and neuraminidase. CONCLUSIONS: Our findings indicated that AAL could be a safe and effective adjuvant capable of boosting humoral immunity against H9N2 viruses in mice through its interaction with the viral surface glycosylated proteins, hemagglutinin and neuraminidase.