Abstract
Hepatitis B virus surface protein variants are described, capable of translocating to the lumenal side of the endoplasmic reticulum membrane their myristylated N-termini, as revealed by the contestual modification of N-terminal, N-linked glycosylation sites. To our knowledge, this is the first example of transmembrane translocation of a preformed protein acyl adduct. The possible significance of this event for hepatitis B virus biology is discussed.
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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Base Sequence
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Cell Line
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Codon / genetics
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Endoplasmic Reticulum / metabolism*
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Hepatitis B Surface Antigens / biosynthesis
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Hepatitis B Surface Antigens / isolation & purification
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Hepatitis B Surface Antigens / metabolism*
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Hepatitis B virus / metabolism
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Humans
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Intracellular Membranes / metabolism
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Lipid Bilayers / metabolism
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Myristic Acid
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Myristic Acids / metabolism*
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Oligodeoxyribonucleotides
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Plasmids
Substances
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Codon
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Hepatitis B Surface Antigens
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Lipid Bilayers
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Myristic Acids
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Oligodeoxyribonucleotides
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Myristic Acid