Abstract
Structural and nonstructural regions of the HCV-encoded polyprotein have been expressed in recombinant yeast, bacteria, or insect cells and used to capture and measure reactive antibodies circulating in different individuals. The putative nucleocapsid protein (C) and nonstructural proteins 3-5 (NS3-NS5) were found to contain the most immunodominant epitopes. The NS3, NS4, and C regions were expressed in yeast in the form of a fused, chimeric polyprotein (C25) and a capture assay for reactive antibody was developed. This anti-C25 assay detects all previously identified HCV-seropositive cases and provides a substantially more sensitive diagnostic for both acute and chronic HCV infections than the current anti-C100-3 (NS4) assay. Anti-C25 was detected more frequently than anti-C100-3 in chronic, transfusion-associated non-A, non-B hepatitis patients from the United States (95% vs. 71%) and Japan (98% vs. 82%), in cryptogenic cirrhosis patients from the United States (62% vs. 28%), and in hepatitis B surface antigen-negative cases of hepatocellular carcinoma from Japan (83% vs. 63%). These data indicate that HCV has a greater role in these liver diseases than was previously thought. In volunteer United States blood donors sampled following the introduction of anti-C100-3 screening, the prevalence of anti-C25 and anti-C100-3 was 0.5% and 0.08%, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 10011-10015 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 89 |
| Issue number | 21 |
| State | Published - Dec 1 1992 |
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Keywords
- Blood screening
- Enzyme immunoassay
- Enzyme-linked immunosorbent assay
- Non-A, non-B hepatitis
ASJC Scopus subject areas
- Genetics
- General
Cite this
Diagnosis of hepatitis C virus (HCV) infection using an immunodominant chimeric polyprotein to capture circulating antibodies : Reevaluation of the role of HCV in liver disease. / Chien, D. Y.; Choo, Q. L.; Tabrizi, A.; Kuo, C.; McFarland, J.; Berger, K.; Lee, C.; Shuster, J. R.; Nguyen, Tuan; Moyer, D. L.; Tong, M.; Furuta, S.; Omata, M.; Tegtmeier, G.; Alter, H.; Schiff, Eugene R; Jeffers, Lennox J; Houghton, M.; Kuo, G.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 21, 01.12.1992, p. 10011-10015.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Diagnosis of hepatitis C virus (HCV) infection using an immunodominant chimeric polyprotein to capture circulating antibodies
T2 - Reevaluation of the role of HCV in liver disease
AU - Chien, D. Y.
AU - Choo, Q. L.
AU - Tabrizi, A.
AU - Kuo, C.
AU - McFarland, J.
AU - Berger, K.
AU - Lee, C.
AU - Shuster, J. R.
AU - Nguyen, Tuan
AU - Moyer, D. L.
AU - Tong, M.
AU - Furuta, S.
AU - Omata, M.
AU - Tegtmeier, G.
AU - Alter, H.
AU - Schiff, Eugene R
AU - Jeffers, Lennox J
AU - Houghton, M.
AU - Kuo, G.
PY - 1992/12/1
Y1 - 1992/12/1
N2 - Structural and nonstructural regions of the HCV-encoded polyprotein have been expressed in recombinant yeast, bacteria, or insect cells and used to capture and measure reactive antibodies circulating in different individuals. The putative nucleocapsid protein (C) and nonstructural proteins 3-5 (NS3-NS5) were found to contain the most immunodominant epitopes. The NS3, NS4, and C regions were expressed in yeast in the form of a fused, chimeric polyprotein (C25) and a capture assay for reactive antibody was developed. This anti-C25 assay detects all previously identified HCV-seropositive cases and provides a substantially more sensitive diagnostic for both acute and chronic HCV infections than the current anti-C100-3 (NS4) assay. Anti-C25 was detected more frequently than anti-C100-3 in chronic, transfusion-associated non-A, non-B hepatitis patients from the United States (95% vs. 71%) and Japan (98% vs. 82%), in cryptogenic cirrhosis patients from the United States (62% vs. 28%), and in hepatitis B surface antigen-negative cases of hepatocellular carcinoma from Japan (83% vs. 63%). These data indicate that HCV has a greater role in these liver diseases than was previously thought. In volunteer United States blood donors sampled following the introduction of anti-C100-3 screening, the prevalence of anti-C25 and anti-C100-3 was 0.5% and 0.08%, respectively.
AB - Structural and nonstructural regions of the HCV-encoded polyprotein have been expressed in recombinant yeast, bacteria, or insect cells and used to capture and measure reactive antibodies circulating in different individuals. The putative nucleocapsid protein (C) and nonstructural proteins 3-5 (NS3-NS5) were found to contain the most immunodominant epitopes. The NS3, NS4, and C regions were expressed in yeast in the form of a fused, chimeric polyprotein (C25) and a capture assay for reactive antibody was developed. This anti-C25 assay detects all previously identified HCV-seropositive cases and provides a substantially more sensitive diagnostic for both acute and chronic HCV infections than the current anti-C100-3 (NS4) assay. Anti-C25 was detected more frequently than anti-C100-3 in chronic, transfusion-associated non-A, non-B hepatitis patients from the United States (95% vs. 71%) and Japan (98% vs. 82%), in cryptogenic cirrhosis patients from the United States (62% vs. 28%), and in hepatitis B surface antigen-negative cases of hepatocellular carcinoma from Japan (83% vs. 63%). These data indicate that HCV has a greater role in these liver diseases than was previously thought. In volunteer United States blood donors sampled following the introduction of anti-C100-3 screening, the prevalence of anti-C25 and anti-C100-3 was 0.5% and 0.08%, respectively.
KW - Blood screening
KW - Enzyme immunoassay
KW - Enzyme-linked immunosorbent assay
KW - Non-A, non-B hepatitis
UR - http://www.scopus.com/inward/record.url?scp=0026448768&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026448768&partnerID=8YFLogxK
M3 - Article
VL - 89
SP - 10011
EP - 10015
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 21
ER -