| Literature DB >> 11576328 |
S Dueñas-Carrera1, A Viña, H E Garay, O Reyes, L Alvarez-Lajonchere, I Guerra, L J González, J Morales.
Abstract
Two variants of the hepatitis C virus (HCV) E2 envelope protein, lacking the C-terminal domain and comprising amino acids 458-650 (E2A) and 382-605 (E2C), respectively, were efficiently produced in BL21 (DE3) Escherichia coli cells. E2A and E2C were used to immunize mice. The E2C variant induced the maximal mean antibody titer. Anti-E2C mouse sera reacted mainly with E2 synthetic peptides covering the 70 amino acid N-terminal region of the E2 protein. Moreover, a panel of anti-HCV positive human sera recognized only the E2C protein (28.2%) and the synthetic peptide covering the HVR-1 of the E2 protein (23.1%). These data indicate the existence of an immunologically relevant region in the HVR-1 of the HCV E2 protein.Entities:
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Year: 2001 PMID： 11576328 DOI： 10.1034/j.1399-3011.2001.00795.x
Source DB: PubMed Journal: J Pept Res ISSN： 1397-002X