Abstract
The proper folding and assembly of viral envelope proteins are mediated by host chaperones. In this study, we demonstrated that an endoplasmic reticulum luminal chaperone GRP78/BiP bound specifically to the pre-S1 domain of the L protein in vitro and in vivo where complete viral particles were secreted, suggesting that GRP78/BiP plays an essential role in the proper folding of the L protein and/or assembly of viral envelope proteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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COS Cells
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Carrier Proteins / metabolism*
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Endoplasmic Reticulum / metabolism
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Endoplasmic Reticulum Chaperone BiP
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Heat-Shock Proteins*
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Hepatitis B virus / genetics
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Hepatitis B virus / metabolism*
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Hepatitis B virus / pathogenicity
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Humans
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Molecular Chaperones / metabolism*
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Molecular Sequence Data
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Rabbits
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Tumor Cells, Cultured
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Viral Envelope Proteins / metabolism*
Substances
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Carrier Proteins
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Endoplasmic Reticulum Chaperone BiP
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HSPA5 protein, human
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Heat-Shock Proteins
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L protein, hepatitis B virus
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Molecular Chaperones
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Viral Envelope Proteins