PMID- 16298963
OWN - NLM
STAT- MEDLINE
DCOM- 20051220
LR  - 20200306
IS  - 0022-1317 (Print)
IS  - 0022-1317 (Linking)
VI  - 86
IP  - Pt 12
DP  - 2005 Dec
TI  - Assembly of functional hepatitis C virus glycoproteins on infectious 
      pseudoparticles occurs intracellularly and requires concomitant incorporation of 
      E1 and E2 glycoproteins.
PG  - 3189-3199
LID - 10.1099/vir.0.81428-0 [doi]
AB  - Hepatitis C virus (HCV) E1 and E2 envelope glycoproteins (GPs) displayed on 
      retroviral cores (HCVpp) are a powerful and highly versatile model system to 
      investigate wild-type HCV entry. To further characterize this model system, the 
      cellular site of HCVpp assembly and the respective roles of the HCV GPs in this 
      process were investigated. By using a combination of biochemical methods with 
      confocal and electron microscopic techniques, it was shown that, in cells 
      producing HCVpp, both E1 and E2 colocalized with retroviral core proteins 
      intracellularly, presumably in multivesicular bodies, but not at the cell 
      surface. When E1 and E2 were expressed individually with retroviral core 
      proteins, only E2 colocalized with and was incorporated on retroviral cores. 
      Conversely, the colocalization of E1 with retroviral core proteins and its 
      efficient incorporation occurred only upon co-expression of E2. Moreover, HCVpp 
      infectivity correlated strictly with the presence of both E1 and E2 on retroviral 
      cores. Altogether, these results confirm that the E1E2 heterodimer constitutes 
      the prebudding form of functional HCV GPs and, more specifically, show that 
      dimerization with E2 is a prerequisite for efficient E1 incorporation onto 
      particles.
FAU - Sandrin, Virginie
AU  - Sandrin V
AD  - IFR128 BioSciences Lyon-Gerland, Lyon, F-69007 France.
AD  - Ecole Normale Superieure de Lyon, Lyon, F-69007 France.
AD  - INSERM, U412, Lyon, F-69007 France.
FAU - Boulanger, Pierre
AU  - Boulanger P
AD  - Laboratoire de Virologie et Pathogenese Virale, CNRS UMR-5537, Faculte de 
      Medecine de Lyon and Institut Federatif de Recherche RTH Laennec, Lyon, France.
FAU - Penin, Francois
AU  - Penin F
AD  - Institut de Biologie et Chimie des Proteines, CNRS-UMR 5086, Universite Claude 
      Bernard Lyon 1, Lyon, France.
FAU - Granier, Christelle
AU  - Granier C
AD  - IFR128 BioSciences Lyon-Gerland, Lyon, F-69007 France.
AD  - Ecole Normale Superieure de Lyon, Lyon, F-69007 France.
AD  - INSERM, U412, Lyon, F-69007 France.
FAU - Cosset, Francois-Loic
AU  - Cosset FL
AD  - IFR128 BioSciences Lyon-Gerland, Lyon, F-69007 France.
AD  - Ecole Normale Superieure de Lyon, Lyon, F-69007 France.
AD  - INSERM, U412, Lyon, F-69007 France.
FAU - Bartosch, Birke
AU  - Bartosch B
AD  - IFR128 BioSciences Lyon-Gerland, Lyon, F-69007 France.
AD  - Ecole Normale Superieure de Lyon, Lyon, F-69007 France.
AD  - INSERM, U412, Lyon, F-69007 France.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Gen Virol
JT  - The Journal of general virology
JID - 0077340
RN  - 0 (E1 protein, Hepatitis C virus)
RN  - 0 (Viral Envelope Proteins)
RN  - 157184-61-7 (glycoprotein E2, Hepatitis C virus)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Cell Membrane/chemistry
MH  - Chlorocebus aethiops
MH  - Cytoplasm/chemistry
MH  - Hepacivirus/*physiology
MH  - Humans
MH  - Microscopy, Confocal
MH  - Microscopy, Electron
MH  - Viral Envelope Proteins/*metabolism
MH  - *Virus Assembly
EDAT- 2005/11/22 09:00
MHDA- 2005/12/21 09:00
CRDT- 2005/11/22 09:00
PHST- 2005/11/22 09:00 [pubmed]
PHST- 2005/12/21 09:00 [medline]
PHST- 2005/11/22 09:00 [entrez]
AID - 10.1099/vir.0.81428-0 [doi]
PST - ppublish
SO  - J Gen Virol. 2005 Dec;86(Pt 12):3189-3199. doi: 10.1099/vir.0.81428-0.