J Gen Virol Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 75 (1994), 449-455; DOI 10.1099/0022-1317-75-2-449
© 1994 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 Gallina, A.
Right arrow Articles by Milanesi, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gallina, A.
Right arrow Articles by Milanesi, G.
Agricola
Right arrow Articles by Gallina, A.
Right arrow Articles by Milanesi, G.

Intracellular retention of hepatitis B virus surface protein mutants devoid of amino-terminal pre-S1 sequences

A. Gallina, A. De Koning, F. Rossi and G. Milanesi

Istituto di Genetica Biochimica ed Evoluzionistica, Consiglio Nazionale delle Ricerche, Via Abbiategrasso 207, I-27100 Pavia, Italy

To study the mechanism of L protein-mediated, intracellular (pre-Golgi) retention of hepatitis B virus (HBV) surface proteins, a collection of HBV preS-S open reading frame variants bearing wild-type or modified preS extensions was expressed in human cells. When the secretion phenotype of the corresponding proteins was analysed, all surface proteins with rearranged preS domains were found to be at least partially retained. This held true, in particular, for two variant proteins lacking preS1 amino acids 1 to 19 (ayw), the preS1 myristylated N terminus and a putative retention domain, and for another variant lacking the entire preS1 domain plus the N-terminal portion (amino acids 1 to 12) of the preS2 domain. All the retained variants underwent intracellular dimerization/oligomerization via disulphide bonds to a degree comparable to that observed in well exported natural proteins. Our results show that retention can take place in the absence of L N-terminal sequences and does not imply inhibition of covalent oligomerization.

Received 14 May 1993; accepted 30 August 1993.


This article has been cited by other articles:


Home page
Protein Eng Des SelHome page
J. L. Casey, A. M. Coley, L. M. Tilley, and M. Foley
Green fluorescent antibodies: novel in vitro tools
Protein Eng. Des. Sel., June 1, 2000; 13(6): 445 - 452.
[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 © 1994 by the Society for General Microbiology.