Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy

Brazilian Journal of Microbiology

Lunbiao Cui¹  Yiyue Ge¹  Yuhua Qi¹  Zhiyang Shi¹  Yongjun Jiao¹  Xian Qi¹  Xiangjun Zhai¹  Hua Wang¹ 

[1] ,Institute of Microbiology Jiangsu Provincial Center for Diseases Prevention and Control Nanjing,China

关键词: HBV;    PreS1;    Proteomics;    GRP75;   

DOI  :  10.1590/S1517-83822010000200036

来源: SciELO

【 摘 要 】

The PreS1 region of the L protein is important in cell attachment and consequently in hepatitis B virus (HBV) infectivity. To identify novel PreS1 interacting protein, we performed Glutathione-S-transferase (GST) pull-down, two-dimensional gel electrophoresis (2-DE) and mass spectrometry assays. Glucose-regulated proteins (GRP) 78 and 75 were found to bind PreS1. The interactions between PreS1 and GRP75 were confirmed by a co-immunoprecipitation experiment. GRP78 and GRP75 may play important roles in mediating HBV virion entering into hepatocyte and regulating proper folding of the L protein due to their critical functions in protein folding and trafficking. The finding of novel PreS1 binding protein enriches our knowledge about molecular mechanism of HBV infection.

【 授权许可】

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