RT Journal Article
T1 Expression and structural properties of a chimeric protein based on the ectodomains of E1 and E2 hepatitis C virus envelope glycoproteins
A1 Tello, Daniel
A1 Rodríguez Rodríguez, Mar
A1 Yélamos, Belén
A1 Gómez Gutiérrez, Julián
A1 Ortega, Sara
A1 Pacheco González, Beatriz
A1 Peterson, Darrell L.
A1 Gavilanes, Francisco
AB 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.
PB Academic Press Inc. Elsevier Science
SN 1046-5928; 1096-0279
YR 2010
FD 2010-06
LK https://hdl.handle.net/20.500.14352/44769
UL https://hdl.handle.net/20.500.14352/44769
LA eng
NO 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.
NO Ministerio de Educación, Formación Profesional y Deportes (España)
DS Docta Complutense
RD 5 abr 2025