2026-06-29T07:38:38Zhttps://docta.ucm.es/rest/oai/request

oai:docta.ucm.es:20.500.14352/243822024-09-27T15:18:38Zcom_20.500.14352_14col_20.500.14352_15

The deletion of residues 268-292 of E1 impairs the ability of HCV envelope proteins to induce pore formation Lombana, Laura Ortega Atienza, Sara Gómez Gutiérrez, Julián Yélamos, Belén Peterson, Darrell Gavilanes, Francisco 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 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. Ministerio de Economía y Competitividad (MINECO) Depto. de Bioquímica y Biología Molecular Fac. de Ciencias Químicas TRUE pub 2023-06-18T06:50:45Z 2023-06-18T06:50:45Z 2016-03-06 journal article https://hdl.handle.net/20.500.14352/24382 1872-7492 (Online), 0168-1702 (print) 10.1016/j.virusres.2016.02.009 eng BFU 2010-22014 open access application/pdf Elsevier