Glycosylation of the hepatitis C virus envelope protein E1 occurs posttranslationally in a mannosylphosphoryldolichol-deficient CHO mutant cell line
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چکیده
منابع مشابه
Development of Preventive Vaccines for Hepatitis C Virus E1/E2 Protein
Hepatitis C virus (HCV) is responsible for a vast majority of liver failure cases. HCV is a kind of blood disease appraised to chronically infect 3% of the worlds’ population causing significant morbidity and mortality. Therefore, a complete knowledge of humoral responses against HCV, resulting antibodies, and virus-receptor and virus-antibody interactions, are essential to design a vaccine. HC...
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We searched for novel Chinese hamster ovary (CHO) cell mutants defective in peroxisome biogenesis by an improved method using peroxisome targeting sequence (PTS) of Pex3p (amino acid residues 1–40)-fused enhanced green fluorescent protein (EGFP). From mutagenized TKaEG3(1–40) cells, the wild-type CHO-K1 stably expressing rat Pex2p and of rat Pex3p(1–40)-EGFP, numerous cell colonies resistant to...
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Unfolded protein response (UPR) is a cellular adaptive response which functions to reduce stress caused by misfolded proteins in the endoplasmic reticulum (ER). We and others have previously shown that infection with hepatitis C virus (HCV) or expression of the viral proteins can trigger the UPR. HCV is a single-stranded positive-sense RNA virus causing chronic diseases in humans. Its genome en...
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The study of hepatitis C virus (HCV), a major cause of chronic liver disease, has been hampered by the lack of a cell culture system supporting its replication. Here, we have successfully generated infectious pseudo-particles that were assembled by displaying unmodified and functional HCV glycoproteins onto retroviral and lentiviral core particles. The presence of a green fluorescent protein ma...
متن کاملOligomerization of hepatitis C virus core protein is crucial for interaction with the cytoplasmic domain of E1 envelope protein.
Hepatitis C virus (HCV) contains two membrane-associated envelope glycoproteins, E1 and E2, which assemble as a heterodimer in the endoplasmic reticulum (ER). In this study, predictive algorithms and genetic analyses of deletion mutants and glycosylation site variants of the E1 glycoprotein were used to suggest that the glycoprotein can adopt two topologies in the ER membrane: the conventional ...
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ژورنال
عنوان ژورنال: Glycobiology
سال: 2002
ISSN: 0959-6658,1460-2423
DOI: 10.1093/glycob/12.2.95