PMID- 16195228
OWN - NLM
STAT- MEDLINE
DCOM- 20060228
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 281
IP  - 1
DP  - 2006 Jan 6
TI  - Intracellular versus cell surface assembly of retroviral pseudotypes is 
      determined by the cellular localization of the viral glycoprotein, its capacity 
      to interact with Gag, and the expression of the Nef protein.
PG  - 528-42
AB  - Retroviral Gag and Env glycoproteins (GPs) are expressed from distinct cellular 
      areas and need to encounter to interact and assemble infectious particles. 
      Retroviral particles may also incorporate GPs derived from other enveloped 
      viruses via active or passive mechanisms, a process known as "pseudotyping." To 
      further understand the mechanisms of pseudotyping, we have investigated the 
      capacity of murine leukemia virus (MLV) or lentivirus core particles to recruit 
      GPs derived from different virus families: the G protein of vesicular stomatitis 
      virus (VSV-G), the hemagglutinin from an influenza virus, the E1E2 glycoproteins 
      of hepatitis C virus (HCV-E1E2), and the retroviral Env glycoproteins of MLV and 
      RD114 cat endogenous virus. The parameters that influenced the incorporation of 
      viral GPs onto retroviral core particles were (i) the intrinsic cell localization 
      properties of both viral GP and retroviral core proteins, (ii) the ability of the 
      viral GP to interact with the retroviral core, and (iii) the expression of the 
      lentiviral Nef protein. Whereas the hemagglutinin and VSV-G glycoproteins were 
      recruited by MLV and lentivirus core proteins at the cell surface, the HCV and 
      MLV GPs were most likely recruited in late endosomes. In addition, whereas these 
      glycoproteins could be passively incorporated on either retrovirus type, the MLV 
      GP was also actively recruited by MLV core proteins, which, through interactions 
      with the cytoplasmic tail of the latter GP, induced its localization to late 
      endosomal vesicles. Finally, the expression of Nef proteins specifically enhanced 
      the incorporation of the retroviral GPs by increasing their localization in late 
      endosomes.
FAU - Sandrin, Virginie
AU  - Sandrin V
AD  - INSERM U412, Lyon Ecole Normale Superieure de Lyon, and IFR128 BioSciences 
      Lyon-Gerland, Lyon, F-69007 France.
FAU - Cosset, Francois-Loic
AU  - Cosset FL
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20050928
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (E1 protein, Hepatitis C virus)
RN  - 0 (G protein, vesicular stomatitis virus)
RN  - 0 (Gene Products, env)
RN  - 0 (Gene Products, gag)
RN  - 0 (Gene Products, nef)
RN  - 0 (Hemagglutinins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Viral Envelope Proteins)
RN  - 157184-61-7 (glycoprotein E2, Hepatitis C virus)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Carcinoma, Hepatocellular
MH  - Cell Line, Tumor
MH  - Cell Membrane/virology
MH  - Chlorocebus aethiops
MH  - Endosomes/virology
MH  - Gene Products, env/metabolism
MH  - Gene Products, gag/*metabolism
MH  - Gene Products, nef/*metabolism
MH  - Hemagglutinins/metabolism
MH  - Humans
MH  - Kidney/cytology
MH  - Lentivirus/growth & development/physiology
MH  - Lentivirus Infections/metabolism/virology
MH  - Leukemia Virus, Murine/growth & development/*physiology
MH  - Liver Neoplasms
MH  - Membrane Glycoproteins/metabolism
MH  - Retroviridae Infections/metabolism/*virology
MH  - Rhabdomyosarcoma
MH  - Tumor Virus Infections/metabolism/*virology
MH  - Viral Envelope Proteins/metabolism
EDAT- 2005/10/01 09:00
MHDA- 2006/03/01 09:00
CRDT- 2005/10/01 09:00
PHST- 2005/10/01 09:00 [pubmed]
PHST- 2006/03/01 09:00 [medline]
PHST- 2005/10/01 09:00 [entrez]
AID - S0021-9258(19)47831-9 [pii]
AID - 10.1074/jbc.M506070200 [doi]
PST - ppublish
SO  - J Biol Chem. 2006 Jan 6;281(1):528-42. doi: 10.1074/jbc.M506070200. Epub 2005 Sep 
      28.