Peptide immunogen mimicry of putative E1 glycoprotein-specific epitopes in hepatitis C virus
نویسندگان
چکیده
منابع مشابه
Identification of Aptamer-Binding Sites in Hepatitis C Virus Envelope Glycoprotein E2
Hepatitis C Virus (HCV) encodes two envelope glycoproteins, E1 and E2. Our previous work selected a specific aptamer ZE2, which could bind to E2 with high affinity, with a great potential for developing new molecular probes as an early diagnostic reagents or therapeutic drugs targeting HCV. In this study, the binding sites between E2 and aptamer ZE2 were further explored. E2 was truncated to 15...
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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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Currently, there is no effective vaccine to prevent hepatitis C virus (HCV) infection, partly due to our insufficient understanding of the virus glycoprotein immunology. Most neutralizing antibodies (nAbs) were identified using glycoprotein immunogens, such as recombinant E1E2, HCV pseudoparticles or cell culture derived HCV. However, the fact that in the HCV acute infection phase, only a small...
متن کاملFolding of hepatitis C virus E1 glycoprotein in a cell-free system.
The hepatitis C virus (HCV) envelope proteins, E1 and E2, form noncovalent heterodimers and are leading candidate antigens for a vaccine against HCV. Studies in mammalian cell expression systems have focused primarily on E2 and its folding, whereas knowledge of E1 folding remains fragmentary. We used a cell-free in vitro translation system to study E1 folding and asked whether the flanking prot...
متن کاملHepatitis C Virus Envelope Glycoprotein E1 Forms Trimers at the Surface of the Virion.
UNLABELLED In hepatitis C virus (HCV)-infected cells, the envelope glycoproteins E1 and E2 assemble as a heterodimer. To investigate potential changes in the oligomerization of virion-associated envelope proteins, we performed SDS-PAGE under reducing conditions but without thermal denaturation. This revealed the presence of SDS-resistant trimers of E1 in the context of cell-cultured HCV (HCVcc)...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1994
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.68.7.4420-4426.1994