Hepatitis C virus glycoprotein complex localization in the endoplasmic reticulum involves a determinant for retention and not retrieval

Details

Serval ID
serval:BIB_19AFDBA59A3A
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Hepatitis C virus glycoprotein complex localization in the endoplasmic reticulum involves a determinant for retention and not retrieval
Journal
Journal of Biological Chemistry
Author(s)
Duvet  S., Cocquerel  L., Pillez  A., Cacan  R., Verbert  A., Moradpour  D., Wychowski  C., Dubuisson  J.
ISSN
0021-9258 (Print)
Publication state
Published
Issued date
11/1998
Volume
273
Number
48
Pages
32088-95
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Nov 27
Abstract
The hepatitis C virus (HCV) genome encodes two envelope glycoproteins (E1 and E2). These glycoproteins interact to form a noncovalent heterodimeric complex which in the cell accumulates in endoplasmic reticulum (ER)-like structures. The transmembrane domain of E2, at least, is involved in HCV glycoprotein complex localization in this compartment. In principle, ER localization of a protein can be the consequence of actual retention in this organelle or of retrieval from the Golgi. To determine which of these two mechanisms is responsible for HCV glycoprotein complex accumulation in the ER, the precise localization of these proteins was studied by immunofluorescence, and the processing of their glycans was analyzed. Immunolocalization of HCV glycoproteins after nocodazole treatment suggested an ER retention. In addition, HCV glycoprotein glycans were not modified by Golgi enzymes, indicating that the ER localization of these proteins is not because of their retrieval from the cis Golgi. Retention of HCV glycoprotein complexes in the ER without retrieval suggests that this compartment plays an important role for the acquisition of the envelope of HCV particles. A true retention in the ER was also observed for E2 expressed in the absence of E1 or for a chimeric protein containing the ectodomain of CD4 in fusion with the transmembrane domain of E2. These data indicate that, in HCV glycoprotein complex, the transmembrane domain of E2, at least, is responsible for true retention in the ER, without recycling through the Golgi.
Keywords
Animals Carcinoma, Hepatocellular Cell Line Dimerization Endoplasmic Reticulum/*virology Golgi Apparatus/virology Hepacivirus/drug effects/*physiology Humans Liver Neoplasms Nocodazole/pharmacology Polysaccharides/metabolism Tumor Cells, Cultured Viral Envelope Proteins/chemistry/isolation & purification/*metabolism
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 16:06
Last modification date
20/08/2019 12:50
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