DNA Polymerase in the Core of the Human Hepatitis B Virus Candidate

Author:

Robinson William S.1,Greenman Richard L.1

Affiliation:

1. Department of Medicine, Stanford University, Stanford, California 94305

Abstract

Experiments were done to show that the human hepatitis B antigen (HBAg)-associated DNA polymerase is a component of Dane particles and their antigenically distinct cores prepared by Nonidet P-40 detergent treatment of Dane particles. Before detergent treatment, the DNA polymerase was precipitated by serum containing anti-HB surface antigen (anti-HB s ) but not with serum containing anti-HB core antigen (anti-HB c ). After detergent treatment, the enzyme was precipitated by anti-HB c - and not by anti-HB s -containing serum. Highly purified 16- to 25-nm HBAg particles blocked only the precipitation of DNA polymerase in untreated HBAg preparations. The 110 S structure with which the DNA reaction product remains associated in Nonidet P-40-treated preparations was identified as Dane particle core by immunoprecipitation with serum containing anti-HB c . The DNA polymerase and the radioactive DNA reaction product were used as markers for core in immunoprecipitation tests for anticore. In such assays, 8 of 11 human sera with anti-HB s activity and all of 10 sera from chronic HBAg carriers were found to contain anti-HB c activity.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference11 articles.

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