Cell type specific expression of pre S 1 antigen and secretion of hepatitis B virus surface antigen
- 1 September 1987
- journal article
- research article
- Published by Springer Nature in Archiv für die gesamte Virusforschung
- Vol. 96 (3-4) , 249-256
- https://doi.org/10.1007/bf01320964
Abstract
Production of the three hepatitis B surface (HBs) proteins was studied in a hepatoma cell line (PLC/PRF/5) and two HBs antigen secreting cell lines (HeLa and mouse L-cells), which had been transfected by a viral genome isolated by molecular cloning from PLC/PRF/5 chromosomal DNA. The DNA used for transfection contains the HBs-specific promoters and the enhancer which regulate the expression of HBs genes in the transfected cell lines. All three cell lines expressed well the small and middle HBs protein, but the larger pre S 1 containing protein was barely detectable in the L-cell. In vivo growth of the transfected HeLa cell as nude mouse tumour increased pre S 1 expression and suppressed secretion of HBsAg.This publication has 40 references indexed in Scilit:
- Inhibition of Secretion of Hepatitis B Surface Antigen by a Related Presurface PolypeptideScience, 1986
- Demonstration of pre-S polypeptides of hepatitis B virus in infected liversHepatology, 1986
- Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virusCell, 1986
- The hepatitis B virusNature, 1985
- Expression of Hepatitis B Virus Core Antigen Gene Is Induced in Human Hepatoma Cells by Their Growth in Nude MiceJournal of General Virology, 1984
- Signals regulating hepatitis B surface antigen transcriptionNature, 1983
- Integration of hepatitis B virus DNA: Evidence for integration in the single-stranded gapCell, 1983
- Core and E antigen synthesis in rodent cells transformed with hepatitis B virus DNA is associated with greater than genome length viral messenger RNAsJournal of Molecular Biology, 1983
- A new technique for the assay of infectivity of human adenovirus 5 DNAVirology, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970