J Gen Virol Tips for Better Browsing
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 72 (1991), 421-425; DOI 10.1099/0022-1317-72-2-421
© 1991 Society for General Microbiology

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shamoon, B.-M.
Right arrow Articles by Mandart, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shamoon, B.-M.
Right arrow Articles by Mandart, E.
Agricola
Right arrow Articles by Shamoon, B.-M.
Right arrow Articles by Mandart, E.

Production of polyclonal antibodies against the S and preS2 regions of woodchuck hepatitis virus: lack of detectable low glycosylated preS2 protein (GP33) in sera from infected animals

Blanche-Marie Shamoon, Alan Kay, Stéphane Dupont de Dinechin, Francis Galibert and Elisabeth Mandart{dagger}

UPR 41 CNRS Recombinaisons Génétiques, Centre Hayem, Hôpital Saint-Louis, 75475 Paris Cedex 10, France

Polyclonal antibodies directed against the preS2 and S domains of the woodchuck hepatitis virus (WHV) envelope proteins were prepared using synthetic peptides and fusion polypeptides as immunogens. They were tested by immunoblotting and immunoprecipitation of infected woodchuck sera and lysates of a eukaryotic cell line expressing WHV envelope proteins. Only one anti-peptide serum directed against the preS2 domain was reactive with WHV envelope proteins, recognizing the preS2 and preS1 proteins by their preS2 epitopes. With recombinant fusion proteins we generated several anti-S sera, which recognized all envelope proteins, and anti-preS2 antisera, which recognized the preS proteins. Results obtained with our antisera showed that sera of infected woodchucks lack the low glycosylated form (GP33) of the preS2 protein, unlike human hepatitis B virus.

{dagger} Present address: UPR 2420 CNRS, Centre de Génétique Moléculaire, avenue de la Terrasse, 91198 Gif-sur-Yvette, France

Received 4 July 1990; accepted 22 October 1990.


This article has been cited by other articles:


Home page
J. Virol.Home page
T. K. Tolle, D. Glebe, M. Linder, D. Linder, S. Schmitt, R. Geyer, and W. H. Gerlich
Structure and Glycosylation Patterns of Surface Proteins from Woodchuck Hepatitis Virus
J. Virol., December 1, 1998; 72(12): 9978 - 9985.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1991 by the Society for General Microbiology.