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Abstract

The friction and wear properties of 201HT aluminum alloys and the corresponding competitive coupons were tested on an electrohydraulic

servo face friction and wear testing machine (MM-U10G). The microstructures of the competitive coupons were investigated by

scanning electron microscopy (SEM) and consequently the corresponding friction and wear mechanisms were studied. The results

demonstrated that: (1) the best competitive material of friction and wear performance of the 201HT was the 201HTC. (2) the 201HTC

modified by carbon following the initial mill for oil storage of the micro-groove to be produced, increased the corresponding lubrication

performance reduced the friction coefficient and wear rate effectively. (3) the 201HT-201HTC could obtain both better friction and wear

mainly due to the initial process of grinding following the 201HT plastic deformation occurred in the surface and the formation of a series

of re-melting welding points, whereas the 201HT material hardness would be similar to the 201HTC material hardness, which led into the

competitive material friction and wear performance improvement.

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Authors and Affiliations

Y. Liu
R. Li
L.J. Chen
M. Su
Q. Zeng
H. 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

Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to be a major public health concern. Nucleocapsid (N) protein is the most abundant structural protein on SARS-CoV-2 virions and induces the production of antibodies at the early stage of infection. Large-scale preparation of N protein is essential for the development of immunoassays to detect antibodies to SARS-CoV-2 and the control of virus transmission. In this study, expression of water-soluble N protein was achieved through inducing protein expression at 25°C with 0.5 mM IPTG for 12 h. Western blot and ELISA showed that recombinant N protein could be recognized by sera collected from subjects immunized with Sinovac inactivated SARS-CoV-2 vaccine. Four monoclonal antibodies namely 2B1B1, 4D3A3, 5G1F8, and 7C6F5 were produced using hybridoma technology. Titers of all four monoclonal antibodies in ELISA reached more than 1.28×10 6.0. Moreover, all monoclonal antibodies could react specifically with N protein expressed by transfection of pcDNA3.1-N into BHK-21 cells in IPMA and IFA. These results indicated that water-soluble N protein retained high immunogenicity and possessed the same epitopes as that of native N protein on virions. In addition, the preparation of water-soluble N protein and its monoclonal antibodies laid the basis for the development of immunoassays for COVID-19 detection.
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Authors and Affiliations

Y.B. Wang
1
S.W. Wang
2
Q.Y. Jin
3
L.P. Chen
4
F.Q. Zhang
1
J.J. Shi
1
Y. Yin
5
Z.X. Fan
1
X.Y. Liu
6
L.P. Wang
6
P. Li
6

  1. School of Public Health, Xinxiang Medical University, Xinxiang 453003, P.R. China
  2. School of Basic Medical Sciences, Xinxiang Medical University, Xinxiang 453003, P.R. China
  3. Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, P.R. China
  4. Gushi County Center for Animal Disease Control and Prevention, Xinyang 465200, P.R. China
  5. Mingde College of Xinxiang Medical University, Xinxiang 453003, P.R. China
  6. School of Biological Engineering, Xinxiang University, Xinxiang 453003, P.R. China

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