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Intrahepatic expression of HBcAg in chronic HBV hepatitis: Lessons from molecular biology
Author(s) -
Chu ChiaMing,
Liaw YunFan
Publication year - 1990
Publication title -
hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.488
H-Index - 361
eISSN - 1527-3350
pISSN - 0270-9139
DOI - 10.1002/hep.1840120630
Subject(s) - hbcag , signal peptide , hepatitis b virus , endoplasmic reticulum , cytosol , virology , peptide sequence , biology , cleavage (geology) , amino acid , microbiology and biotechnology , chemistry , virus , biochemistry , hbsag , gene , enzyme , paleontology , fracture (geology)
The precore and core proteins of hepatitis B virus have identical deduced amino acid sequences other than a 29‐residue amino‐terminal extension (precore region) on the precore protein. The first 19 of these residues serve as a signal sequence to direct the precore protein to the endoplasmic reticulum, where they are cleaved off with formation of precore protein derivative P22 for secretion. In this report, we show that P22 can alternatively be transported into the nucleus following signal peptide cleavage. Experiments with deletion mutants indicated that this nuclear transport proceeds via the cytosol and is dependent on the amino‐terminal portion of P22. Thus, the hepatitis B virus precore protein is a secreted, cytosolic, and nuclear protein.