Abstract
Formation of the viral envelope is an important step in the morphogenesis of enveloped viruses. Our data on the formation of hepatitis C virus (HCV) envelope indicate that endoplasmic reticulum (ER) chaperones play a role in the assembly of HCV envelope proteins (E1 and E2). We have shown that these glycoproteins interact with BiP, calreticulin and calnexin. However, among these chaperones, only calnexin is involved in the productive assembly of E1E2 complex. The other two chaperones interact with misfolded aggregates containing E1 and E2. Folding of HCV glycoproteins occurs in the context of intermediate complexes involving E1, E2 and calnexin. As soon as E1E2 heterodimers are properly folded, they separate from calnexin but don't leave the ER compartment.
MeSH terms
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Calcium-Binding Proteins / physiology
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Calnexin
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Calreticulin
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Carrier Proteins / physiology
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Endoplasmic Reticulum / metabolism
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Endoplasmic Reticulum Chaperone BiP
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Heat-Shock Proteins / physiology
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Hepacivirus / physiology*
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Humans
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Lectins
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Membrane Glycoproteins / physiology
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Membrane Proteins / physiology
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Molecular Chaperones / physiology*
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Morphogenesis / physiology
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Phosphoproteins / physiology
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Protein Folding
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Ribonucleoproteins / physiology
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Viral Envelope Proteins / biosynthesis*
Substances
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Calcium-Binding Proteins
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Calreticulin
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Carrier Proteins
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E1 protein, Hepatitis C virus
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Endoplasmic Reticulum Chaperone BiP
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Heat-Shock Proteins
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Lectins
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Membrane Glycoproteins
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Membrane Proteins
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Molecular Chaperones
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Phosphoproteins
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Ribonucleoproteins
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Viral Envelope Proteins
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Calnexin
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glycoprotein E2, Hepatitis C virus