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A replication-defective herpes simplex virus type 1 (HSV-1) recombinant lacking the glycoprotein H (gH)-encoding gene and expressing a truncated form of the hepatitis C (HCV) E2 glycoprotein (E2-661) was constructed and characterized. We show here that cells infected with the HSV/HCV recombinant virus efficiently express the HCV E2-661 protein. Most importantly, cellular and secreted E2-661 protein were both readily detected by the E2-conformational mAb H53 and despite the high expression levels, only limited amounts of misfolded aggregates were detected in either the cellular or secreted fractions. Furthermore, cell-associated and secreted E2-661 protein bound to the major extracellular loop (MEL) of CD81 in a concentration-dependent manner and both were highly reactive with sera from HCV-infected patients. Finally, BALB/c mice immunized intraperitoneally with the recombinant HSV/HCV virus induced high levels of anti-E2 antibodies. Analysis of the induced immunoglobulin G (IgG) isotypes showed high levels of IgG2a while the levels of the IgG1 isotype were significantly lower, suggesting a Th1-type of response. We conclude that the HSV-1 recombinant virus represents a promising tool for production of non-aggregated, immunologically active forms of the E2-661 protein and might have potential applications in vaccine development.

Original publication

DOI

10.1099/vir.0.18775-0

Type

Journal article

Journal

J Gen Virol

Publication Date

03/2003

Volume

84

Pages

545 - 554

Keywords

Adolescent, Adult, Aged, Animals, Cell Line, Female, Hepatitis C Antibodies, Hepatitis C Antigens, Hepatitis C, Chronic, Humans, Immunoenzyme Techniques, Immunoglobulin G, Male, Mice, Mice, Inbred BALB C, Middle Aged, Protein Engineering, Recombinant Proteins, Simplexvirus, Transfection, Vaccination, Viral Envelope Proteins