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00925njm 22002777a 4500 dc Tello, Daniel author Rodríguez Rodríguez, Mar author Yélamos, Belén author Gómez Gutiérrez, Julián author Ortega, Sara author Pacheco González, Beatriz author Peterson, Darrell L. author Gavilanes, Francisco author 2010-06 Hepatitis 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. Tello, D., Rodríguez Rodríguez, M., Yélamos, B. et al. «Expression and Structural Properties of a Chimeric Protein Based on the Ectodomains of E1 and E2 Hepatitis C Virus Envelope Glycoproteins». Protein Expression and Purification, vol. 71, n.o 2, junio de 2010, pp. 123-31. DOI.org (Crossref), https://doi.org/10.1016/j.pep.2010.02.012. 1046-5928; 1096-0279 10.1016/j.pep.2010.02.012 https://hdl.handle.net/20.500.14352/44769 https//doi.org/10.1016/j.pep.2010.02.012 http://www.sciencedirect.com/science/article/pii/S1046592810000513 Expression and structural properties of a chimeric protein based on the ectodomains of E1 and E2 hepatitis C virus envelope glycoproteins