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Title: Enzymatic treatment of duck hepatitis B virus: Topology of the surface proteins for virions and noninfectious subviral particles

Abstract

The large surface antigen L of duck hepatitis B virus exhibits a mixed topology with the preS domains of the protein alternatively exposed to the particles' interior or exterior. After separating virions from subviral particles (SVPs), we compared their L topologies and showed that both particle types exhibit the same amount of L with the following differences: 1-preS of intact virions was enzymatically digested with chymotrypsin, whereas in SVPs only half of preS was accessible, 2-phosphorylation of L at S118 was completely removed by phosphatase treatment only in virions, 3-iodine-125 labeling disclosed a higher ratio of exposed preS to S domains in virions compared to SVPs. These data point towards different surface architectures of virions and SVPs. Because the preS domain acts in binding to a cellular receptor of hepatocytes, our findings implicate the exclusion of SVPs as competitors for the receptor binding and entry of virions.

Authors:
 [1];  [1];  [2]
  1. Heinrich-Pette-Institut fuer Experimentelle Virologie und Immunologie an der Universitaet Hamburg, Martinistrasse 52, D-20251 Hamburg (Germany)
  2. Heinrich-Pette-Institut fuer Experimentelle Virologie und Immunologie an der Universitaet Hamburg, Martinistrasse 52, D-20251 Hamburg (Germany). E-mail: mbruns@hpi.uni-hamburg.de
Publication Date:
OSTI Identifier:
20976995
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 359; Journal Issue: 1; Other Information: DOI: 10.1016/j.virol.2006.09.006; PII: S0042-6822(06)00651-9; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ANTIGENS; CHYMOTRYPSIN; DUCKS; HEPATITIS; IODINE 125; LABELLING; LIVER CELLS; PHOSPHORYLATION; RECEPTORS; TOPOLOGY; VIRUSES

Citation Formats

Franke, Claudia, Matschl, Urte, and Bruns, Michael. Enzymatic treatment of duck hepatitis B virus: Topology of the surface proteins for virions and noninfectious subviral particles. United States: N. p., 2007. Web. doi:10.1016/j.virol.2006.09.006.
Franke, Claudia, Matschl, Urte, & Bruns, Michael. Enzymatic treatment of duck hepatitis B virus: Topology of the surface proteins for virions and noninfectious subviral particles. United States. doi:10.1016/j.virol.2006.09.006.
Franke, Claudia, Matschl, Urte, and Bruns, Michael. Thu . "Enzymatic treatment of duck hepatitis B virus: Topology of the surface proteins for virions and noninfectious subviral particles". United States. doi:10.1016/j.virol.2006.09.006.
@article{osti_20976995,
title = {Enzymatic treatment of duck hepatitis B virus: Topology of the surface proteins for virions and noninfectious subviral particles},
author = {Franke, Claudia and Matschl, Urte and Bruns, Michael},
abstractNote = {The large surface antigen L of duck hepatitis B virus exhibits a mixed topology with the preS domains of the protein alternatively exposed to the particles' interior or exterior. After separating virions from subviral particles (SVPs), we compared their L topologies and showed that both particle types exhibit the same amount of L with the following differences: 1-preS of intact virions was enzymatically digested with chymotrypsin, whereas in SVPs only half of preS was accessible, 2-phosphorylation of L at S118 was completely removed by phosphatase treatment only in virions, 3-iodine-125 labeling disclosed a higher ratio of exposed preS to S domains in virions compared to SVPs. These data point towards different surface architectures of virions and SVPs. Because the preS domain acts in binding to a cellular receptor of hepatocytes, our findings implicate the exclusion of SVPs as competitors for the receptor binding and entry of virions.},
doi = {10.1016/j.virol.2006.09.006},
journal = {Virology},
number = 1,
volume = 359,
place = {United States},
year = {Thu Mar 01 00:00:00 EST 2007},
month = {Thu Mar 01 00:00:00 EST 2007}
}