Nan Bao

Nan Bao


Research Focus & Metrics

Academic Career Length

16Years (2011-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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Verified
Journal Article
Open access
PDF file
YZYuan Zhao
Yuan Zhao
GQGuixin Qin
Guixin Qin
ZSZewei Sun
Zewei Sun
Dongsheng CheDongsheng Che
Dongsheng Che
NBNan Bao
Nan Bao
XZXiaodong Zhang
Xiaodong Zhang
This study was developed to provide further information on the intestinal barrier permeability and the tight junction protein expression in weaned piglets fed with different levels of soybean agglutinin (SBA). Twenty-five weaned crossbred barrows (Duroc × Landrace × Yorkshire) were selected and randomly allotted to five groups, each group with five replicates. The piglets in the control group were not fed with leguminous products. 0.05, 0.1, 0.15 and 0.2% SBA was added to the control diet to form four experimental diets, respectively. After the experimental period of 7 days (for each group), all the piglets were anesthetized with excess procaine and slaughtered. The D-lactic acid in plasma and the Ileal mucosa diamine oxidase (DAO) was analyzed to observe the change in the intestinal permeability. The tight junction proteins occludin and ZO-1 in the jejunum tissue distribution and relative expression were detected by immunohistochemistry and Western Blot. The results illustrated that a high dose of SBA (0.1–0.2%) could increase the intestinal permeability and reduce piglet intestinal epithelial tight junction protein occludin or ZO-1 expression, while low dose of SBA (0.05% of total diet) had no significant affects. The contents of DAO, D-lactic acid, occludin or ZO-1, had a linear relationship with the SBA levels (0–0.2%) in diets. The high dose SBA (0.1–0.2%) could increase the intestinal permeability and reduce piglet intestinal epithelial tight junction protein occludin or ZO-1 expression, while low dose of SBA (0.05% of total diet) had no affects.

Verified
Journal Article
Open access
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LPLi Pan
Li Pan
Mohammed Hamdy FaroukMohammed Hamdy Farouk
Mohammed Hamdy Farouk
GQGuixin Qin
Guixin Qin
YZYuan Zhao
Yuan Zhao
NBNan Bao
Nan Bao
Soybean agglutinin (SBA) is a non-fiber carbohydrate-related protein and the main anti-nutritional factor that exists in soybean or soybean products. SBA possesses a specific binding affinity for N-glyphthalide-d-galactosamine or galactose and has a covalently linked oligosaccharide chain. SBA mediates negative effects on animal intestinal health by influencing the intestinal structure, barrier function, mucosal immune system, and the balance of the intestinal flora. Functional oligosaccharides are non-digestible dietary oligosaccharides that are commonly applied as prebiotics since the biological effects of the functional oligosaccharides are to increase the host health by improving mucosal structure and function, protecting the integrity of the intestinal structure, modulating immunity, and balancing the gastrointestinal microbiota. The purpose of this review is to describe the structure and anti-nutritional functions of SBA, summarize the influence of SBA and functional oligosaccharides on the intestinal tract of monogastric animals, and emphasize the relationship between SBA and oligosaccharides. This review provides perspectives on applying functional oligosaccharides for alleviating the anti-nutritional effects of SBA on the intestinal tract.

8 January 2021 in Frontiers in Veterinary Science
Verified
Journal Article
Open access
YZYuan Zhao
Yuan Zhao
GNGaowa Naren
Gaowa Naren
JQJianan Qiang
Jianan Qiang
GQGuixin Qin
Guixin Qin
NBNan Bao
Nan Bao
Mohammed Hamdy FaroukMohammed Hamdy Farouk
Mohammed Hamdy Farouk
Soybean can cause allergy in both humans and animals. The herein study aims to identify the antigenic determinants (epitopes) of β-conglycinin that lead to allergy in different animal species (swine, bovine, and rats). The epitopes of β-conglycinin were identified through co-immunoprecipitation and mass spectrometry. The binding abilities of seven identified epitope peptides to allergic sera of three animal species were compared by ELISA and dot-blot techniques. Some epitope peptides could be recognized by the three animal allergic sera, while most epitopes showed some differences in binding abilities to the different animal sera. The strongest reaction using swine sera was detected with peptides α2, β2, and β3, but the biggest sensitive regions for bovine and rats were peptides α2, β1, and β4. Most epitopes of β-conglycinin exhibited different binding abilities to the three animal sera, in which the biggest sensitive regions were peptides α2, β2, and β3 for swine, but peptides α2, β1, and β4 were detected for bovine and rats.

Verified
Journal Article
Open access
PDF file
LPLi Pan
Li Pan
YZYuan Zhao
Yuan Zhao
Mohammed Hamdy FaroukMohammed Hamdy Farouk
Mohammed Hamdy Farouk
NBNan Bao
Nan Bao
Tao WangTao Wang
Tao Wang
GQGuixin Qin
Guixin Qin
Soybean agglutinin (SBA), is a non-fiber carbohydrate related protein and a major anti-nutritional factor. Integrins, transmembrane glycoproteins, are involved in many biological processes. Although recent work suggested that integrins are involved in SBA-induced cell-cycle alterations, no comprehensive study has reported whether integrins are involved in SBA-induced cell apoptosis (SCA) in IPEC-J2. The relationship between SBA and integrins are still unclear. We aimed to elucidate the effects of SBA on IPEC-J2 cell proliferation and cell apoptosis; to study the roles of integrins in IPEC-J2 normal cell apoptosis (NCA) and SCA; and to illustrate the relationship and connection type between SBA and integrins. Thus, IPEC-J2 cells were treated with SBA at the levels of 0, 0.125, 0.25, 0.5, 1.0 or 2.0 mg/mL to determine cell proliferation and cell apoptosis. The cells were divided into control, SBA treated groups, integrin inhibitor groups, and SBA + integrin inhibitor groups to determine the integrin function in SCA. The results showed that SBA significantly (p < 0.05) lowered cell proliferation and induced cell apoptosis in IPEC-J2 (p < 0.05). Inhibition of any integrin type induced the cell apoptosis (p < 0.05) and these integrins were involved in SCA (p < 0.05). Even SBA had no physical connection with integrins, an association was detected between SBA and α-actinin-2 ACTN2 (integrin-binding protein). Additionally, SBA reduced the mRNA expression of integrins by down regulating the gene expression level of ACTN2. We concluded an evidence for the anti-nutritional mechanism of SBA by ACTN2 with integrins. Further trials are needed to prove whether ACTN2 is the only protein for connecting SBA with integrin.

14 March 2022 in Italian Journal of Animal Science
Verified
Journal Article
Open access
YZYuan Zhao
Yuan Zhao
YZYaru Zhu
Yaru Zhu
GQGuixin Qin
Guixin Qin
LPLi Pan
Li Pan
HSHui Sun
Hui Sun
Mohammed Hamdy FaroukMohammed Hamdy Farouk
Mohammed Hamdy Farouk
The nutritional values of the protein are related to its amino acid content, and its physicochemical properties. We aimed to determine the relationship between the variation of protein digestibility or the releasing coefficient of amino acids with the physicochemical properties of different feedstuffs. We analysed the secondary protein structure and solubility of 10 protein-rich feed ingredients, including soybean, soybean meal, dehulled soybean meal, fermented soybean meal, distiller’s dried grains with solubles (DDGS), feather meal, fish meal, rapeseed meal, corn gluten meal, and corn germ meal. The results showed that the soybeans and their products had greater protein solubility than the other dietary protein (p < .001). Fish meal, rapeseed meal and all soybean sources had the higher protein digestibility and releasing coefficient of amino acids, also reached different peaks in shorter times. But corn germ meal, corn gluten meal, and feather meal exhibited lower releasing coefficient of amino acids and weaker solubility (p < .001). The in-vitro protein digestibility or releasing coefficient of total amino acid had positive regression coefficients with α-helix, α-helix/β-sheet, and solubility; and a negative regression coefficient with β-sheet. Feedstuffs with faster amino acid releasing rate had higher α-helix, α-helix/β-sheet and solubility and lower β-sheet. Therefore, the physicochemical properties of the dietary protein could be used as predictors for the amino acids’ digestibility and amino acid bioavailability.

1 February 2022 in Animal Bioscience
Verified
Journal Article
Open access
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NHNianzhi Hu
Nianzhi Hu
ZSZhiwen Shen
Zhiwen Shen
LPLi Pan
Li Pan
GQGuixin Qin
Guixin Qin
YZYuan Zhao
Yuan Zhao
NBNan Bao
Nan Bao
Objective: We aimed to investigate the effect of the differing amino acid (AA) release dynamics of two protein sources on the growth performance, nitrogen deposition, plasma biochemical parameters, and muscle synthesis and degradation of piglets when included in their diets at normal and low concentrations.Methods: Forty-eight piglets (Duroc×Landrace×Large White) with initial body weight of 7.45±0.58 kg were assigned to six groups and fed one of 6 diets. The 6 dietary treatments were arranged by 3×2 factorial with 3 protein sources and 2 dietary protein levels. They are NCAS (a normal protein content with casein), NBlend (a normal protein content with blend of casein and corn gluten meal), NCGM (a normal protein content with corn gluten meal), LCAS (a low protein content with casein), LBlend (a low protein content with blend of casein and corn gluten meal), LCGM (a low protein content with corn gluten meal). The release dynamics of AA in these diets were determined by in vitro digestion. The digestibility, utilization and biological value of nitrogen in piglets were determined by micro Kjeldahl method. Plasma insulin was measured by enzyme-linked immunosorbent assay kits. The protein expression of mediators of muscle synthesis and degradation was determined by western blotting.Results: Although the consumption of a low-protein diet supplemented with crystalline AA was associated with greater nitrogen digestion and utilization (p<0.05), the final body weight, growth performance, nitrogen deposition, and phosphorylation of ribosomal protein S6 kinase 1 and eIF4E binding protein 1 in the muscle of pigs in the low-protein diet-fed groups were lower than those of the normal-protein diet-fed groups (p<0.05) because of the absence of non-essential AA. Because of the more balanced release of AA, the casein (CAS) and Blend-fed groups showed superior growth performance, final body weight and nitrogen deposition, and lower expression of muscle ring finger 1 and muscle atrophy F-box than the CGM-fed groups (p<0.05).Conclusion: We conclude that the balanced release of AA from CAS containing diets and mixed diets could reduce muscle degradation, favor nitrogen retention, % intake and improve growth performance in pigs consuming either a normal- or low-protein diet.