Expression of unmodified hepatitis C virus envelope glycoprotein-coding sequences leads to cryptic intron excision and cell surface expression of E1/E2 heterodimers comprising full-length and partially deleted E1.
Hepatitis C virus (HCV) is a positive-strand RNA virus that replicates exclusively in the cytoplasm of infected cells. The viral envelope glycoproteins, E1 and E2, appear to be retained in the endoplasmic reticulum, where viral budding is thought to occur. Surprisingly, we found that the expression system used to generate HCV envelope glycoproteins influences their subcellular localization and processing. These findings have important implications for optimizing novel HCV fusion and entry assays as well as for budding and virus particle formation.
Dumonceaux
Julie
J
Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Cormier
Emmanuel G
EG
Kajumo
Francis
F
Donovan
Gerald P
GP
Roy-Chowdhury
Jayanta
J
Fox
Ira J
IJ
Gardner
Jason P
JP
Dragic
Tatjana
T
D001483:Base Sequence; D002462:Cell Membrane / Q000378:metabolism*; D019281:Dimerization; D006367:HeLa Cells; D016174:Hepacivirus / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D006801:Humans; D007438:Introns; D008969:Molecular Sequence Data; D017384:Sequence Deletion; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000235:genetics / Q000378:metabolism*
D014759:Viral Envelope Proteins; D015678:Viral Structural Proteins; C107842:protein E1, Classical swine fever virus; C091015:glycoprotein E2, Hepatitis C virus