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Tang Z.R.,Southwest University | Tang Z.R.,Chongqing Engineering Research Center for Herbivores Resource Protection and Utilization | Deng H.,Southwest University | Zhang X.L.,Southwest University | And 4 more authors.
Animal Feed Science and Technology | Year: 2013

The antimicrobial peptide buforin II contains residues Thr16 to Lys36 of buforin I and exhibits antimicrobial activity that is twice as potent as that of its parent peptide. Buforin II was expressed in Pichia pastoris FZM2009 as a fusion peptide linked to porcine interferon-α and tested as an alternative to antimicrobial growth-promoters in pig production. Fifteen Landrace×Yorkshire barrows (5.55±0.49kg), weaned at 21 days of age, were challenged with three enterotoxigenic Escherichia coli strains. The animals were randomly divided into 3 groups with 5 barrows in each, fed a maize-soybean meal diet, and orally dosed with 5mL sterile water (CON), 5mL buforin II (BF; 0.05mg/mL in sterile water), or 5mL colistin sulphate (CS; 0.5mg/mL in sterile water) twice daily for 21 days. Compared with CS and CON, oral administration of BF increased (P<0.05) daily weight gain, feed intake gain, and feed conversion. The expression of tight junction proteins and protective factors in the small intestine also increased in BF-treated piglets. Compared with the CON group, oral administration of BF and CS decreased (P<0.05) for the abundance of hemolytic E. coli in rectal swabs. Collectively, our results indicate that oral administration of buforin II protects small intestinal mucosal membrane integrity by increasing the abundance of tight junction proteins and enhancing the expression of protective factors, and can reduce hemolytic E. coli concentrations in the intestines of piglets. © 2013 Elsevier B.V.

Chu H.,CAS Northwest Institute of Plateau Biology | Chu H.,University of Chinese Academy of Sciences | Guo X.,CAS Northwest Institute of Plateau Biology | Guo X.,University of Chinese Academy of Sciences | And 5 more authors.
Conservation Genetics Resources | Year: 2014

Chromobox-helicase DNA-binding gene (CHD1) is the most reliable gene for sex identification in birds. However, the CHD1 fragments of some species are difficult to amplify. In this study, we designed a new primer set (IntP2/IntP8) that targets a conserved region of CHD1 gene. Firstly, we tested this protocol in Oriental skylark (Alauda gulgula). PCR amplification produced a single band (259 bp) for males and two bands (259 and 297 bp) for females. We then successfully conducted sex identification in other bird species including Tibetan lark (Melanocorypha maxima), Horned lark (Eremophila alpestris), Mongolian skylark (Melanocorypha mongolica), Asian short-toed lark (Calandrella cheleensis), Humes short-toed lark (Calandrella acutirostris), Crested lark (Galerida cristata), Yellow-headed wagtail (Motacilla citreola), White wagtail (Motacilla alba) and Ground tit (Pseudopodoces humilis Hume). Collectively, these findings support that IntP2/IntP8 primer set can be used to accurately determine sex identity in birds. © 2014, Springer Science+Business Media Dordrecht.

Sun Y.,Hunan Normal University | Fu Z.,Hunan Normal University | Fu Z.,Hunan Institute of Microbiology | He X.,Hunan Normal University | And 3 more authors.
Journal of Invertebrate Pathology | Year: 2016

In order to assess the potency of bi-functional HWTX-XI toxin from spider Ornithoctonus huwena in improving the insecticidal activity of Bacillus thuringiensis, a fusion gene of cry1Ac and hwtx-XI was constructed and expressed in an acrystalliferous B. thuringiensis strain Cry-B. Western blot analysis and microscopic observation revealed that the recombinant strain could express 140-kDa Cry1Ac-HWTX-XI fusion protein and produce parasporal inclusions during sporulation. Bioassay using the larvae of Helicoverpa armigera and Spodoptera exigua showed that the Cry1Ac-HWTX-XI fusion was more toxic than the control Cry1Ac protoxin, as revealed by 95% lethal concentration. Our study indicated that the HWTX-XI from spider might be a candidate for enhancing the toxicity of B. thuringiensis products. © 2015 Elsevier Inc.

Hu Q.,Hunan Normal University | Wang J.,Hunan Normal University | Fu Z.,Hunan Normal University | Fu Z.,Hunan Institute of Microbiology | And 5 more authors.
Applied Microbiology and Biotechnology | Year: 2015

It was reported that the parasporal crystal from Bacillus thuringiensis contained DNA fragments. To investigate the distribution of protoxin and DNA in B. thuringiensis cells at different growth stages, a cry1Ac-gfp fusion gene was constructed and expressed in an acrystalliferous B. thuringiensis strain, in which the localization of DNA and protoxin were indicated by DNA-specific dye and green fluorescent protein, respectively. When the recombinant cells were at the vegetative growth stage, the Cry1Ac-GFP fusion protein was not expressed and the DNA fluorescent signal was evenly distributed throughout the cell. At the initial stage of sporulation, the Cry1Ac-GFP fusion protein was expressed and accumulated as inclusion body, while two condensed DNA signals existed at each pole of the cell. With the extension of culture time, it seemed that the DNA fluorescence from the region of spore development gradually became faint or vanishing, while the DNA signal was still present in the other pole or the remaining area of the mother cell. Interestingly and unexpectedly, there was no DNA fluorescence signal in the region of the growing and mature inclusion body of Cry1Ac-GFP in B. thuringiensis cell, which might indicate that the DNA embodied in the inclusion body was not accessible to the DNA-specific dye. This was the first investigation devoted exclusively to the in vivo distribution of protoxin and DNA in B. thuringiensis at different growth stages. These data shed light on deeply understanding the process of sporulation and parasporal crystal formation as well as further exploring the interaction of DNA and protoxin in B. thuringiensis. © 2015, Springer-Verlag Berlin Heidelberg.

Wang S.-P.,CAS Institute of Subtropical Agriculture | Wang S.-P.,Hunan Institute of Microbiology | Gao Y.-L.,CAS Institute of Subtropical Agriculture | Liu G.,CAS Institute of Subtropical Agriculture | And 8 more authors.
Journal of Zhejiang University: Science B | Year: 2015

The energy homeostasis-associated (Enho) gene encodes a secreted protein, adropin, which regulates the expression of hepatic lipogenic genes and adipose tissue peroxisome proliferator-activated receptor γ, a major regulator of lipogenesis. In the present study, the porcine (Sus scrofa) homologue of the Enho gene, which was named pEnho, was amplified by reverse transcriptase polymerase chain reaction (RT-PCR) using oligonucleotide primers derived from in silico sequences. The gene sequence was submitted into the GenBank of NCBI, and the access number is GQ414763. The pEnho encodes a protein of 76 amino acids which shows 75% similarity to Homo sapiens adropin. The expression profile of pEnho in tissues (liver, muscle, anterior jejunum, posterior jejunum, and ileum) was determined by quantitative real-time RT-PCR. pEnho was localized on porcine chromosome 10 and no introns were found. In conclusion, pEnho was cloned and analysed with the aim of increasing knowledge about glucose and lipid metabolism in piglets and helping to promote the health and growth of piglets through adropin regulation. © 2015, Zhejiang University and Springer-Verlag Berlin Heidelberg.

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