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Number of results: 6
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Abstract

Highly immunogenic nucleotide fragments from 3 genes of Mycoplasma hyopneumoniae strain 232 were selected using information software technology. After repeating each fragment three times, a total of 9 nucleotide fragments were joined together to form a new nucleotide sequence called Mhp2321092bp. Mhp2321092bp was directly synthesized and cloned into a pET100 vector and expressed in Escherichia coli. After purification, the proteins were successfully validated by SDS-PAGE and Western blotting using mouse His-tag antibody and pig anti-Mhp serum. BALB/c mice were intraperitoneally injected with purified proteins in the high-dose (100 μg), medium-dose group (50 μg) and low-dose (10 μg) groups. Mice in each group were injected on day 1, day 8 and day 15 of feeding, respectively. Serum samples were collected from all mice on the day before immunization and on day 22 after immunization. The antibody level in the mouse serum was detected using western blotting using purified expressed proteins as antigens. IL-2, TNF-α and IFN-γ were simultaneously detected in the mouse serum by ELISA. The results showed that the 60 kDa protein was successfully expressed and reacted specifically with the specific serum Mhp His-Tag mouse monoclonal antibody and pig anti-Mhp serum. From day 0 to day 22 of immunization, IFN-γ increased from 269.52 to 467.74 pg/mL, IL-2 increased from 14.03 to 145.16 pg/mL, and TNF-α increased from 6.86 to 12.37 pg/mL. The IgG antibody in mice increased significantly from 0 day to day 22 after immunization. This study suggests that the expressed recombinant protein may serve as one of the novel vaccine candidates for Mhp.
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Authors and Affiliations

J. Li
1
G. Wang
1

  1. College of Veterinary Medicine, Hunan Agricultural University, Nongda road 1#, Changsha, Hunan, 410128, China
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Abstract

A “rock bridge”, defined as the closest distance between two joints in a rock mass, is an important feature affecting the jointed rock mass strength. Artificial jointed rock specimens with two parallel joint fractures were tested under uniaxial compression and numerical simulations were carried out to study the effects of the inclination of the rock bridge, the dip angle of the joint, rock bridge length, and the length of joints on the strength of the jointed rock mass. Research results show: (1) When the length of the joint fracture, the length of the rock bridge, and the inclination of the rock bridge stay unchanged, the uniaxial compressive strength of the specimen gradually increases as the inclination of the joint fracture increases from 0° to 90°. (2) When the length of the joint fracture, the length of the rock bridge, and the inclination of the joint fracture stay unchanged, the uniaxial compressive strength of the specimen shows variations in trends with the inclination of the rock bridge increasing from 30° to 150° (3). In the case when the joint is angled from the vertical loading direction, when the dip angle of the joint fracture, the inclination of the rock bridge, and the length of the rock bridge stay unchanged, the uniaxial compressive strength of the specimen gradually decreases with an increasing length of joint fracture. When the dip angle of the joint fracture, the inclination of the rock bridge, and the length of the joint fracture stay unchanged, the uniaxial compressive strength of the specimen does not show a clear trend with an increase of the length of the rock bridge.

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Authors and Affiliations

L.X. Xiong
H.Y. Yuan
Y. Zhang
K.F. Zhang
J.B. Li
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Abstract

Sapelovirus A (SV-A) is a positive-sense single-stranded RNA virus which is associated with acute diarrhea, pneumonia and reproductive disorders. The virus capsid is composed of four proteins, and the functions of the structural proteins are unclear. In this study, we expressed SV-A structural protein VP1 and studied its antigenicity and immunogenicity. SDS-PAGE analysis revealed that the target gene was expressed at high levels at 0.6 mM concentration of IPTG for 24 h. The mouse polyclonal antibody against SV-A VP1 protein was produced and reached a high antiserum titer (1: 2,048,000). Immunized mice sera with the recombinant SV-A VP1 protein showed specific recognition of purified VP1 protein by western blot assay and could recognize native SV-A VP1 protein in PK-15 cells infected with SV-A by indirect immunofluorescence assay. The successfully purified recombinant protein was able to preserve its antigenic determinants and the generated mouse anti-SV-A VP1 antibodies could recognize native SV-A, which may have the potential to be used to detect SV-A infection in pigs.

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Authors and Affiliations

T.T. Zhao
L. Cui
L. Chen
J.J. Li
Q.L. Liang
P.J. Wu
X.Q. Yu
Z.H. Zhang
X.G. Hua
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Abstract

Emerging researches in humans, pigs and mice, highlighted that estrogen plays a pivotal role in self-renewal and differentiation of bone marrow mesenchymal stem cells (BMSCs). The present study aimed at evaluating effects of 17 beta-estradiol (E2) on proliferation and apoptosis of canine-derived bone marrow mesenchymal stem cells (cBMSCs) in vitro. The results showed that E2 supplementation at the concentration of 10-11 M promoted the proliferation of cBMSCs by CCK-8 assay and RT-qPCR analysis for the proliferation-related genes, with proliferating cell nuclear antigen (PCNA), cyclin-D1 (CCND1) being up-regulated and cyclin-dependent kinase inhibitor 1B (CDKN1B) being down-regulated. Contrarily, analysis of fluorescence-activated cell sorting (FACS) and RT-qPCR demonstrated that E2 supplementation above 10-11 M had inhibitory effects on the proliferation of cBMSCs and induced apoptosis. Intriguingly, cBMSCs still possessed the capability to differentiate into osteoblasts and adipocytes with 10-11 M E2 addition. Taken together, this study determined the optimal culture condition of cBMSCs in vitro, and has important implications for further understanding the regulatory effect of E2 on the self-renewal of cBMSCs, which are helpful for the clinical application of BMSCs.

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Authors and Affiliations

Z.-H. Zhou
C.-W. Gu
J. Li
X.-Y. Huang
J.-Q. Deng
L.-H. Shen
S.-Z. Cao
J.-L. Deng
Z.-C. Zuo
Y. Wang
ORCID: ORCID
X.-P. Ma
Z.-H. Ren
S.-M. Yu

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