Wang Xiong

Publications (3)5.04 Total impact

• Article: A rapid method for detection of PrP by surface plasmon resonance (SPR).

  Wan Jiayu, Wang Xiong, Li Jiping, Liu Wensen, Xu Ming, Liu Linna, Xu Jing, Wang Haiying, Gao Hongwei
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  ABSTRACT: Surface plasmon resonance was used to develop a rapid, label-free and sensitive immunoassay for detection of Prion protein (PrP). Anti-PrP monoclonal antibodies immobilized on the biosensor surface were allowed to bind various concentrations of cellular prion protein (PrP(C)), followed by a pulse with additional soluble anti-PrP polyclonal antibodies to intensify the signal. The interaction of antibody with antigen was monitored in real time. With this method, it was possible to detect PrP(C) with a limit of 31.7 ng/ml in serum and 13.1 ng/ml in HEPES-saline, requiring 1 h for a single sample measurement. The assay also detected misfolded prion protein (PrP(Sc)) in spiked serum and PrP(Sc) in scrapie-infected mouse brains. This is a rapid and sensitive assay for the detection of PrP in serum that could be developed into a platform for a serum-based TSE test.
  Archives of Virology 10/2009; 154(12):1901-8. · 2.11 Impact Factor
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  Available from: beyotime.com

  Article: Mapping the interaction site of prion protein and Sho.

  Wan Jiayu, Hao Zhu, Xu Ming, Wang Xiong, Wu Songbo, Song Bocui, Liu Wensen, Li Jiping, Meng Keying, Li Zhongyi, Gao Hongwei
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  ABSTRACT: The cellular prion protein (PrP(C)) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP(C) remains unclear. Sho (Shadoo, shadow of prion protein) and PrP(C) have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61-77 and PrP(C) 108-126 domains. This indicates that Sho may play a role in the physiological function of PrP(C) and prion pathogenesis.
  Molecular Biology Reports 09/2009; 37(5):2295-300. · 2.93 Impact Factor
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  Available from: beyotime.com

  Article: Mapping the interaction site of prion protein and Sho

  Wan Jiayu, Ae Hao, Zhu Ae Xu, Ming Ae, Wang Xiong, Ae Wu, Songbo Ae, Song Bocui, Ae Liu, Wensen Ae Li, Jiping Ae, Meng Keying, Ae Li, Zhongyi Ae, Gao Hongwei
  [show abstract] [hide abstract]
  ABSTRACT: The cellular prion protein (PrP C) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP C remains unclear. Sho (Shadoo, shadow of prion pro-tein) and PrP C have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61–77 and PrP C 108–126 domains. This indicates that Sho may play a role in the physiological function of PrP C and prion pathogenesis.