Tello, DanielRodríguez-Rodríguez, MarYélamos, BelénGómez-Gutiérrez, JuliánOrtega, SaraPacheco, BeatrizPeterson, Darrell L.Gavilanes, Francisco2023-06-202023-06-202010-061046-5928; 1096-027910.1016/j.pep.2010.02.012https://hdl.handle.net/20.500.14352/44769Hepatitis C virus encodes two enveloped glycoproteins, E1 and E2, which are involved in viral attachment and entry into target cells. We have obtained in insect cells infected by recombinant baculovirus a chimeric secreted recombinant protein, E1341E2661, containing the ectodomains of E1 and E2. The described procedure allows the purification of approximately 2 mg of protein from 1 L of culture media. Sedimentation velocity experiments and SDS-PAGE in the absence of reducing agents indicate that the protein has a high tendency to self-associate, the dimer being the main species observed. All the oligomeric forms observed maintain a conformation which is recognized by the conformation-dependent monoclonal antibody H53 directed against the E2 ectodomain. The spectroscopic properties of E1341E2661 are those of a three-dimensionally structured protein. Moreover, the chimeric protein is able to bind to human antibodies present in HCV-positive human sera. Accordingly, this chimeric soluble polypeptide chain may be a valuable tool to study the structure-function relationship of HCV envelope proteins.engjournal articlehttp://www.sciencedirect.com/science/article/pii/S1046592810000513open access577.1Hepatitis C Virusenvelope proteinE1E2baculovirusglycosylationBioquímica (Química)