The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Crystal Structure of the West Nile Virus Envelope Glycoprotein
Open accessAbstract
The envelope glycoprotein (E) of West Nile virus (WNV) undergoes a conformational rearrangement triggered by low pH that results in a class II fusion event required for viral entry. Herein we present the 3.0-Å crystal structure of the ectodomain of WNV E, which reveals insights into the flavivirus life cycle. We found that WNV E adopts a three-domain architecture that is shared by the E proteins from dengue and tick-borne encephalitis viruses and forms a rod-shaped configuration similar to that observed in immature flavivirus particles. Interestingly, the single N-linked glycosylation site on WNV E is displaced by a novel α-helix, which could potentially alter lectin-mediated attachment. The localization of histidines within the hinge regions of E implicates these residues in pH-induced conformational transitions. Most strikingly, the WNV E ectodomain crystallized as a monomer, in contrast to other flavivirus E proteins, which have crystallized as antiparallel dimers. WNV E assembles in a crystalline lattice of perpendicular molecules, with the fusion loop of one E protein buried in a hydrophobic pocket at the DI-DIII interface of another. Dimeric E proteins pack their fusion loops into analogous pockets at the dimer interface. We speculate that E proteins could pivot around the fusion loop-pocket junction, allowing virion conformational transitions while minimizing fusion loop exposure.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
Kuhn, R. J., Zhang, W., Rossmann, M. G., Pletnev, S. V., Corver, J., Lenches, E., Jones, C. T., Mukhopadhyay, S., Chipman, P. R., Strauss, E. G., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00660-8 · Cited by 1,563
The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C., & Harrison, S. C. (1995) · Nature · doi:10.1038/375291a0 · Cited by 1,437
Structure of the dengue virus envelope protein after membrane fusion
Modis, Y., Ogata, S., Clements, D., & Harrison, S. C. (2004) · Nature · doi:10.1038/nature02165 · Cited by 1,203
A ligand-binding pocket in the dengue virus envelope glycoprotein
Modis, Y., Ogata, S., Clements, D., & Harrison, S. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0832193100 · Cited by 1,061
DC-SIGN (CD209) Mediates Dengue Virus Infection of Human Dendritic Cells
Tassaneetrithep, B., Burgess, T. H., Granelli-Piperno, A., Trumpfheller, C., Finke, J., Sun, W., Eller, M. A., Pattanapanyasat, K., Sarasombath, S., Birx, D. L., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021840 · Cited by 890
Guo, Y., Feinberg, H., Conroy, E., Mitchell, D. A., Alvarez, R., Blixt, O., Taylor, M. E., Weis, W. I., & Drickamer, K. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb784 · Cited by 602
Cited by
Dengue virus life cycle: viral and host factors modulating infectivity
Rodenhuis-Zybert, I. A., Wilschut, J., & Smit, J. M. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0357-z · Cited by 499
Zlatkovic, J., Tsouchnikas, G., Jarmer, J., Koessl, C., Stiasny, K., & Heinz, F. X. (2013) · Journal of Virology · doi:10.1128/jvi.01690-13 · Cited by 23
Metadata
- Authors
- Nybakken, G. E., Nelson, C. A., Chen, B. R., Diamond, M. S., & Fremont, D. H.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2006-12
- Volume
- 80
- Issue
- 23
- Pages
- 11467-11474
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2102575242
- Cited by
- 264
- References
- 42
- FWCI
- 18.02
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Crystal Structure of the West Nile Virus Envelope Glycoprotein. https://app.cochat.ai/papers/10.1128/jvi.01125-06
- The paper
- Nybakken, G. E., Nelson, C. A., Chen, B. R., Diamond, M. S., & Fremont, D. H. (2006). Crystal Structure of the West Nile Virus Envelope Glycoprotein. Journal of Virology. https://doi.org/10.1128/jvi.01125-06
Data sources
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.
