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
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author Cui, Lunbiao
Ge, Yiyue
Qi, Yuhua
Shi, Zhiyang
Jiao, Yongjun
Qi, Xian
Zhai, Xiangjun
Wang, Hua
author_facet Cui, Lunbiao
Ge, Yiyue
Qi, Yuhua
Shi, Zhiyang
Jiao, Yongjun
Qi, Xian
Zhai, Xiangjun
Wang, Hua
author_sort Cui, Lunbiao
collection PubMed
description 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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spelling pubmed-37686862013-09-12 Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy Cui, Lunbiao Ge, Yiyue Qi, Yuhua Shi, Zhiyang Jiao, Yongjun Qi, Xian Zhai, Xiangjun Wang, Hua Braz J Microbiol General Microbiology 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. Sociedade Brasileira de Microbiologia 2010 2010-06-01 /pmc/articles/PMC3768686/ /pubmed/24031525 http://dx.doi.org/10.1590/S1517-838220100002000036 Text en © Sociedade Brasileira de Microbiologia http://creativecommons.org/licenses/by-nc/3.0/ All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License
spellingShingle General Microbiology
Cui, Lunbiao
Ge, Yiyue
Qi, Yuhua
Shi, Zhiyang
Jiao, Yongjun
Qi, Xian
Zhai, Xiangjun
Wang, Hua
Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy
title Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy
title_full Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy
title_fullStr Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy
title_full_unstemmed Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy
title_short Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy
title_sort identification of grp75 as a novel pres1 binding protein using a proteomics strategy
topic General Microbiology
url 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
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