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Expression of hepatitis B virus large envelope polypeptide inhibits hepatitis B surface antigen secretion in transgenic mice

Academic Article
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Overview

authors

  • Chisari, Francis
  • Filippi, P.
  • McLachlan, A.
  • Milich, D. R.
  • Riggs, M.
  • Lee, S.
  • Palmiter, R. D.
  • Pinkert, C. A.
  • Brinster, R. L.

publication date

  • December 1986

journal

  • Journal of Virology  Journal

abstract

  • The outer membrane of the hepatitis B virus consists of host lipid and the hepatitis B virus major (p25, gp28), middle (gp33, gp36), and large (p39, gp42) envelope polypeptides. These polypeptides are encoded by a large open reading frame that contains three in-phase translation start codons and a shared termination signal. The influence of the large envelope polypeptide on the secretion of hepatitis B surface antigen (HBsAg) subviral particles in transgenic mice was examined. The major polypeptide is the dominant structural component of the HBsAg particles, which are readily secreted into the blood. A relative increase in production of the large envelope polypeptide compared with that of the major envelope polypeptide led to profound reduction of the HBsAg concentration in serum as a result of accumulation of both envelope polypeptides in a relatively insoluble compartment within the cell. We conclude that inhibition of HBsAg secretion is related to a hitherto unknown property of the pre-S-containing domain of the large envelope polypeptide.

subject areas

  • Animals
  • Gene Expression Regulation
  • Hepatitis B Surface Antigens
  • Hepatitis B virus
  • Liver
  • Metallothionein
  • Mice
  • Molecular Weight
  • Secretory Rate
  • Tissue Distribution
  • Transcription, Genetic
  • Transfection
  • Viral Envelope Proteins
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Identity

PubMed Central ID

  • PMC253312

International Standard Serial Number (ISSN)

  • 0022-538X

PubMed ID

  • 3783819
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Additional Document Info

start page

  • 880

end page

  • 887

volume

  • 60

issue

  • 3

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