Structure and Function of the Hepatitis C Virus Envelope Glycoproteins E1 and E2: Antiviral and Vaccine Targets
| Autor: | Holly Freedman, Michael Logan, John Lok Man Law, Michael Houghton |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Hepatitis C virus 030106 microbiology Hepacivirus Biology medicine.disease_cause Antiviral Agents 03 medical and health sciences Protein Domains Viral Envelope Proteins Viral entry medicine Animals Humans chemistry.chemical_classification Cell fusion Viral Vaccines Hepatitis C Virology Herpesvirus glycoprotein B Hypervariable region Heptad repeat Transmembrane domain 030104 developmental biology Infectious Diseases chemistry Glycoprotein |
| Zdroj: | ACS Infectious Diseases. 2:749-762 |
| ISSN: | 2373-8227 |
| DOI: | 10.1021/acsinfecdis.6b00110 |
| Popis: | The hepatitis C virus (HCV) envelope glycoproteins E1 and E2 are critical in viral attachment and cell fusion, and studies of these proteins may provide valuable insights into their potential uses in vaccines and antiviral strategies. Progress has included elucidating the crystal structures of portions of their ectodomains, as well as many other studies of hypervariable regions, stem regions, glycosylation sites, and the participation of E1/E2 in viral fusion with the endosomal membrane. The available structural data have shed light on the binding sites of cross-neutralizing antibodies. A large amount of information has been discovered concerning heterodimerization, including the roles of transmembrane domains, disulfide bonding, and heptad repeat regions. The possible organization of higher order oligomers within the HCV virion has also been evaluated on the basis of experimental data. In this review, E1/E2 structure and function is discussed, and some important issues requiring further study are highlighted. |
| Databáze: | OpenAIRE |
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