THE FUNCTIONAL E1–E2 HETERODIMER HCV GLYCOPROTEINS
| Autor: | Ammara Waqar, Sir Syed, Hashim Riaz, Hamid Mahmood, Irfan Farooqi, Nasir Zulfiqar, Naeem Shahzad, Ghazia Irfan |
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| Rok vydání: | 2018 |
| Předmět: | |
| Zdroj: | The Professional Medical Journal. 21:829-840 |
| ISSN: | 2071-7733 1024-8919 |
| DOI: | 10.29309/tpmj/2014.21.05.2501 |
| Popis: | Introduction: The two HCV envelope glycoproteins E1 and E2 are released fromHCV polyprotein by signal peptidase cleavages. These glycoproteins are type I transmembraneproteins with a highly glycosylated N-terminal ectodomain and a C-terminal hydrophobicanchor. Methods and pathways: After their synthesis, HCV glycoproteins E1 and E2 associateas a non covalent heterodimer. The transmembrane domains of HCV envelope glycoproteinsplay a major role in E1–E2 heterodimer assembly and subcellular localization. The envelopeglycoprotein complex E1–E2 has been proposed to be essential for HCV entry. Results andconclusions: However, for a long time, HCV entry studies have been limited by the lack of arobust cell culture system for HCV replication and viral particle production. Recently, a modelmimicking the entry process of HCV lifecycle has been developed by pseudo typing retroviralparticles with native HCV envelope glycoproteins, allowing the characterization of functionalE1–E2 envelope glycoproteins., we review our understanding to date on the assembly of thefunctional HCV glycoprotein heterodimer. |
| Databáze: | OpenAIRE |
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