The deletion of residues 268-292 of E1 impairs the ability of HCV envelope proteins to induce pore formation

By Laura Lombana, Sara Ortega-Atienza, Julián Gómez-Gutiérrez, Belén Yélamos, Darrell L. Peterson, Francisco Gavilanes

July 28, 2017

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Title

The deletion of residues 268-292 of E1 impairs the ability of HCV envelope proteins to induce pore formation

Author

Laura Lombana, Sara Ortega-Atienza, Julián Gómez-Gutiérrez, Belén Yélamos, Darrell L. Peterson, Francisco Gavilanes

Year

2016

Journal

Virus Research

Abstract

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.

Full Article

http://www.sciencedirect.com/science/article/pii/S0168170215301660

Instrument

J-715

Keywords

Circular dichroism, Secondary structure, Biochemistry