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Synthesis, assembly, and processing of the Env ERVWE1/syncytin human endogenous retroviral envelope.

Authors :
Cheynet V
Ruggieri A
Oriol G
Blond JL
Boson B
Vachot L
Verrier B
Cosset FL
Mallet F
Source :
Journal of virology [J Virol] 2005 May; Vol. 79 (9), pp. 5585-93.
Publication Year :
2005

Abstract

Syncytin is a fusogenic protein involved in the formation of the placental syncytiotrophoblast layer. This protein is encoded by the envelope gene of the ERVWE1 proviral locus belonging to the human endogenous retrovirus W (HERV-W) family. The HERV-W infectious ancestor entered the primate lineage 25 to 40 million years ago. Although the syncytin fusion property has been clearly demonstrated, little is known about this cellular protein maturation process with respect to classical infectious retrovirus envelope proteins. Here we show that the cellular syncytin protein is synthesized as a glycosylated gPr73 precursor cleaved into two mature proteins, a gp50 surface subunit (SU) and a gp24 transmembrane subunit (TM). These SU and TM subunits are found associated as homotrimers. The intracytoplasmic tail is critical to the fusogenic phenotype, although its cleavage requirements seem to have diverged from those of classical retroviral maturation.

Details

Language :
English
ISSN :
0022-538X
Volume :
79
Issue :
9
Database :
MEDLINE
Journal :
Journal of virology
Publication Type :
Academic Journal
Accession number :
15827173
Full Text :
https://doi.org/10.1128/JVI.79.9.5585-5593.2005