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

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. Glu...

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Detalles Bibliográficos
Autores principales: Cui, Lunbiao, Ge, Yiyue, Qi, Yuhua, Shi, Zhiyang, Jiao, Yongjun, Qi, Xian, Zhai, Xiangjun, Wang, Hua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Sociedade Brasileira de Microbiologia 2010
Materias:
General Microbiology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3768686/
https://www.ncbi.nlm.nih.gov/pubmed/24031525
http://dx.doi.org/10.1590/S1517-838220100002000036
Descripción
Sumario: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.

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