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Título:
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Expression and structural properties of a chimeric protein based on the ectodomains of E1 and E2 hepatitis C virus envelope glycoproteins
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Autores:
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Tello, Daniel ;
Rodríguez-Rodríguez, Mar ;
Yélamos, Belén ;
Gómez-Gutiérrez, Julián ;
Ortega, Sara ;
Pacheco, Beatriz ;
Peterson, Darrell L. ;
Gavilanes, Francisco
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Tipo de documento:
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texto impreso
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Editorial:
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Academic Press Inc. Elsevier Science, 2010-06
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Dimensiones:
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application/pdf
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Nota general:
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info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias: Química: Bioquímica
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Tipo = Artículo
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Resumen:
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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.
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En línea:
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https://eprints.ucm.es/33661/1/Prot.%20Expres%20Purif.%2071%2C%201123-131%20%282010%29.pdf
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