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


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hourioux, C.
Right arrow Articles by Roingeard, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hourioux, C.
Right arrow Articles by Roingeard, P.
Agricola
Right arrow Articles by Hourioux, C.
Right arrow Articles by Roingeard, P.
Journal of General Virology (2000), 81, 1099-1101.
© 2000 Society for General Microbiology


Animal: DNA Viruses

DNA-containing and empty hepatitis B virus core particles bind similarly to envelope protein domains

Christophe Hourioux1, Antoine Touzé2, Pierre Coursaget2 and Philippe Roingeard1

Laboratoires de Biologie Cellulaire et Virologie, EA 2639 Analyse Structurale des Antigènes, Faculté de Médecine, Institut Fédératif de Recherche Transposons et Virus, Université François Rabelais, 2 bis Boulevard Tonnellé, F-37032 Tours Cedex, France1
Laboratoire de Virologie Moléculaire, EA 2637 Processus Infectieux et Tumoraux, Faculté des Sciences Pharmaceutiques ‘Philippe Maupas’, Institut Fédératif de Recherche Transposons et Virus, Université François Rabelais, Tours, France2

Author for correspondence: Philippe Roingeard. Fax +33 2 47 36 60 90. e-mail roingeard{at}med.univ-tours.fr

DNA synthesis within the hepatitis B virus (HBV) nucleocapsid appears to be coupled to nucleocapsid envelopment. The nature of the envelopment signal is unknown, but is thought to involve a conformational change at the surface of the capsid that facilitates interaction with HBV envelope proteins. In binding assays in vitro, it was found that empty HBV core particles bound synthetic peptides corresponding to HBV envelope protein domains with the same affinity as did HBV DNA-containing core particles. This suggests that the selection of replication-competent nucleocapsids for envelopment is not related to the capacity of DNA-containing core particles to bind specifically to HBV envelope proteins, and that there must be an alternative mechanism.







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 © 2000 by the Society for General Microbiology.