S. Duenas-carrera et al., Immunological evaluation of Escherichia coli-derived hepatitis C virus second envelope protein (E2) variants, J PEPT RES, 58(3), 2001, pp. 221-228
Two variants of the hepatitis C virus (HCV) E2 envelope protein, lacking th
e C-terminal domain and comprising amino acids 458-650 (E2A) and 382-605 (E
2C), 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 sy
nthetic peptides covering the 70 amino acid N-terminal region of the E2 pro
tein. Moreover, a panel of anti-HCV positive human sera recognized only the
E2C protein (28.2%) and the synthetic peptides covering the HVR-1 of the E
2 protein (23.1%). These data indicate the existence of an immunologically
relevant region in the HVR-1 of the HCV E2 protein.