The deletion of residues 268-292 of E1 impairs the ability of HCV envelope proteins to induce pore formation
We have obtained a chimeric protein containing the ectodomains of hepatitis C virus (HCV) envelope proteins but lacking the region 268-292 of E1. All its structural properties are coincident with those of the corresponding full length chimera. The deleted and entire chimeras were compared in terms o...
| Authors: | , , , , , |
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| Format: | article |
| Publication Date: | 2016 |
| Country: | España |
| Institution: | Universidad Complutense de Madrid (UCM) |
| Repository: | Docta Complutense |
| Language: | English |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/24382 |
| Online Access: | https://hdl.handle.net/20.500.14352/24382 |
| Access Level: | Open access |
| Keyword: | 577.1 hepatitis C virus viral envelope proteins lipid-protein interaction membrane fusion protein spectroscopic properties. Biología molecular (Biología) Bioquímica (Biología) 2415 Biología Molecular 2302 Bioquímica |
| Summary: | We have obtained a chimeric protein containing the ectodomains of hepatitis C virus (HCV) envelope proteins but lacking the region 268-292 of E1. All its structural properties are coincident with those of the corresponding full length chimera. The deleted and entire chimeras were compared in terms of their membrane destabilizing properties. No differences were found in their ability to induce vesicle aggregation and lipid mixing but the deleted chimera showed a reduced capacity to promote leakage. The role of the deletion was also studied by obtaining HCV pseudoparticles (HCVpp). Both E1 and E2, and also the E1 deleted mutant, were incorporated into HCVpp to a similar level. However, HCVpp containing the E1 deleted protein are almost unable to infect Huh7 cells. These results point to the involvement of the region 268-292 in the formation of pores in the membrane necessary for the complete fusion of the membranes. |
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