Fusion Expression, Immunogenicity and
Applications of
C-terminally Truncated HCV Core Proteins
YANG Li, ZHU Li-Xin, WANG Yuan and LI Guang-Di*
( Shanghai Institute of Biochemistry, Chinese Academy of Sciences, Shanghai
200031, China )
Abstract¡¡¡¡Clones expressing
full-length(aa 1-191) or C-terminally truncated forms (aa 1-69 and aa 1-40) of
hepatitis C virus core(HCc) protein fused to the C-terminal of glutathione
S-transferase(GST) were constructed and their expressions in different strains
of Escherichia coli were compared. The expressed proteins were
soluble. ELISA and Western blot analyses showed that GSTC191 was poorly
expressed and had poor stability, whereas GSTC69 and GSTC40 were stable and
could be purified to 90% purity in a single step on glutathione-Sepharose 4B.
Mice immunized with these purified proteins produced high-titre antibodies. As
an application, purified GSTC69 and GSTC40 were used in a preliminary assay of
anti-HCc antibodies in patients' sera, and results showed that they had high
specificity in the assay.
Key Words¡¡¡¡Viral core protein; C-terminally
truncated; GST fusion expression; immunogenicity
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