The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus
Open accessAbstract
Hepatitis C virus (HCV) infects ∼2% of the world's population. It is estimated that there are more than 500,000 new infections annually in Egypt, the country with the highest HCV prevalence. An effective vaccine would help control this expanding global health burden. HCV is highly variable, and an effective vaccine should target conserved T- and B-cell epitopes of the virus. Conserved B-cell epitopes overlapping the CD81 receptor-binding site (CD81bs) on the E2 viral envelope glycoprotein have been reported previously and provide promising vaccine targets. In this study, we isolated 73 human mAbs recognizing five distinct antigenic regions on the virus envelope glycoprotein complex E1E2 from an HCV-immune phage-display antibody library by using an exhaustive-panning strategy. Many of these mAbs were broadly neutralizing. In particular, the mAb AR4A, recognizing a discontinuous epitope outside the CD81bs on the E1E2 complex, has an exceptionally broad neutralizing activity toward diverse HCV genotypes and protects against heterologous HCV challenge in a small animal model. The mAb panel will be useful for the design and development of vaccine candidates to elicit broadly neutralizing antibodies to HCV.
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Cites
Safran, M., Kim, W. Y., Kung, A. L., Horner, J. W., Depinho, R. A., & Kaelin, W. G. (2003) · Molecular Imaging · doi:10.1162/153535003322750637 · Cited by 134
Cited by
The HCV Life Cycle: In vitro Tissue Culture Systems and Therapeutic Targets
Gerold, G., & Pietschmann, T. (2014) · Digestive Diseases · doi:10.1159/000360830 · Cited by 4,854
Understanding the hepatitis C virus life cycle paves the way for highly effective therapies
Scheel, T. K. H., & Rice, C. M. (2013) · Nature Medicine · doi:10.1038/nm.3248 · Cited by 554
Self-citationHepatitis C Virus E2 Envelope Glycoprotein Core Structure
Kong, L., Giang, E., Nieusma, T., Kadam, R. U., Cogburn, K. E., Hua, Y., Dai, X., Stanfield, R. L., Burton, D. R., Ward, A. B., et al. (2013) · Science · doi:10.1126/science.1243876 · Cited by 398
Self-citationKoh, C., Li, Q., & Liang, J. (2016) · Clinical Virology · doi:10.1128/9781555819439.ch54 · Cited by 321
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00972-2 · Cited by 285
Metadata
- Authors
- Giang, E., Dorner, M., Prentoe, J. C., Dreux, M., Evans, M. J., Bukh, J., Rice, C. M., Ploss, A., Burton, D. R., & Law, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2012-04-04
- Volume
- 109
- Issue
- 16
- Pages
- 6205-6210
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2102253058
- Cited by
- 346
- References
- 1
- FWCI
- 18.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Giang, E., Dorner, M., Prentoe, J. C., Dreux, M., Evans, M. J., Bukh, J., Rice, C. M., Ploss, A., Burton, D. R., & Law, M. (2012). Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1114927109
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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