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• W1557805105 abstract "The preS domain at the N-terminus of the large envelope protein (LHBs) of the hepatitis B virus is involved in (i) envelopment of viral nucleocapsids and (ii) binding to the host cell. While the first function suggests a cytosolic location of the preS domain during virion assembly, the function as an attachment site requires its translocation across the lipid bilayer and final exposure on the virion surface. We compared the transmembrane topology of newly synthesized LHBs in the endoplasmic reticulum (ER) membrane with its topology in the envelope of secreted virions. Protease sensitivity and the absence of glycosylation suggest that the entire preS domain of newly synthesized LHBs remains at the cytosolic side of ER vesicles. However, virions secreted from transfected cell cultures or isolated from the blood of persistent virus carriers expose antibody binding sites and proteolytic cleavage sites of the preS domain at their surface in approximately half of the LHBs molecules. Thus, preS domains appear to be transported across the viral lipid barrier by a novel post-translational translocation mechanism to fulfil a dual function in virion assembly and attachment to the host cell." @default.
• W1557805105 created "2016-06-24" @default.
• W1557805105 creator A5043096075 @default.
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• W1557805105 date "1994-05-01" @default.
• W1557805105 modified "2023-10-05" @default.
• W1557805105 title "Post-translational alterations in transmembrane topology of the hepatitis B virus large envelope protein." @default.
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• W1557805105 doi "https://doi.org/10.1002/j.1460-2075.1994.tb06509.x" @default.
• W1557805105 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/395089" @default.
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• W1557805105 hasPublicationYear "1994" @default.
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