The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
DC-SIGN and L-SIGN Are High Affinity Binding Receptors for Hepatitis C Virus Glycoprotein E2
Open accessAbstract
The hepatitis C virus (HCV) genome codes for highly mannosylated envelope proteins, which are naturally retained in the endoplasmic reticulum. We found that the HCV envelope glycoprotein E2 binds the dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) and the related liver endothelial cell lectin L-SIGN through high-mannose N-glycans. Competing ligands such as mannan and an antibody directed against the carbohydrate recognition domains (CRD) abrogated binding. While no E2 interaction with distant monomeric CRDs on biosensor chips could be detected, binding is observed if CRDs are closely seeded (Kd = 48 nm) and if the CRD is part of the oligomeric-soluble extracellular domain of DC-SIGN (Kd = 30 nm). The highest affinity is seen for plasma membrane-expressed DC-SIGN and L-SIGN (Kd = 3 and 6 nm, respectively). These results indicate that several high-mannose N-glycans in a structurally defined cluster on E2 bind to several subunits of the oligomeric lectin CRD. High affinity interaction of viral glycoproteins with oligomeric lectins might represent a strategy by which HCV targets to and concentrates in the liver and infects dendritic cells.
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Cites
DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
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Binding of Hepatitis C Virus to CD81
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Mycobacteria Target DC-SIGN to Suppress Dendritic Cell Function
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Structural Basis for Selective Recognition of Oligosaccharides by DC-SIGN and DC-SIGNR
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Cited by
Self- and nonself-recognition by C-type lectins on dendritic cells
Geijtenbeek, T. B. H., van Vliet, S. J., Engering, A., 't Hart, B. A., & van Kooyk, Y. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104558 · Cited by 503
How C-type lectins detect pathogens: C-type lectins and pathogens
Cambi, A., Koopman, M., & Figdor, C. G. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00506.x · Cited by 448
Koutsoudakis, G., Kaul, A., Steinmann, E., Kallis, S., Lohmann, V., Pietschmann, T., & Bartenschlager, R. (2006) · Journal of Virology · doi:10.1128/jvi.02460-05 · Cited by 414
Hepatitis C virus infection protein network
de Chassey, B., Navratil, V, Tafforeau, L., Hiet, M. S., Aublin‐Gex, A., Agaugué, S., Meiffren, G., Pradezynski, F., Faria, B. F., Chantier, T., et al. (2008) · Molecular Systems Biology · doi:10.1038/msb.2008.66 · Cited by 384
Marzi, A., Gramberg, T., Simmons, G., Möller, P., Rennekamp, A. J., Krumbiegel, M., Geier, M., Eisemann, J., Turza, N., Saunier, B., et al. (2004) · Journal of Virology · doi:10.1128/jvi.78.21.12090-12095.2004 · Cited by 377
Metadata
- Authors
- Lozach, P.-Y., Lortat-Jacob, H., De Lacroix De Lavalette, A., Staropoli, I., Foung, S., Amara, A., Houlès, C., Fieschi, F., Schwartz, O., Virelizier, J.-L., Arenzana-Seisdedos, F., & Altmeyer, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 278
- Issue
- 22
- Pages
- 20358-20366
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2169601765
- Cited by
- 375
- References
- 45
- FWCI
- 26.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: DC-SIGN and L-SIGN Are High Affinity Binding Receptors for Hepatitis C Virus Glycoprotein E2. https://app.cochat.ai/papers/10.1074/jbc.m301284200
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- Lozach, P.-Y., Lortat-Jacob, H., De Lacroix De Lavalette, A., Staropoli, I., Foung, S., Amara, A., Houlès, C., Fieschi, F., Schwartz, O., Virelizier, J.-L., Arenzana-Seisdedos, F., & Altmeyer, R. (2003). DC-SIGN and L-SIGN Are High Affinity Binding Receptors for Hepatitis C Virus Glycoprotein E2. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m301284200
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
