The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution
Open accessAbstract
The hemagglutinin-esterases (HEs) are a family of viral envelope glycoproteins that mediate reversible attachment to O -acetylated sialic acids by acting both as lectins and as receptor-destroying enzymes (RDEs). Related HEs occur in influenza C, toro-, and coronaviruses, apparently as a result of relatively recent lateral gene transfer events. Here, we report the crystal structure of a coronavirus (CoV) HE in complex with its receptor. We show that CoV HE arose from an influenza C-like HE fusion protein (HEF). In the process, HE was transformed from a trimer into a dimer, whereas remnants of the fusion domain were adapted to establish novel monomer–monomer contacts. Whereas the structural design of the RDE-acetylesterase domain remained unaltered, the HE receptor-binding domain underwent remodeling to such extent that the ligand is now bound in opposite orientation. This is surprising, because the architecture of the HEF site was preserved in influenza A HA over a much larger evolutionary distance, a switch in receptor specificity and extensive antigenic variation notwithstanding. Apparently, HA and HEF are under more stringent selective constraints than HE, limiting their exploration of alternative binding-site topologies. We attribute the plasticity of the CoV HE receptor-binding site to evolutionary flexibility conferred by functional redundancy between HE and its companion spike protein S. Our findings offer unique insights into the structural and functional consequences of independent protein evolution after interviral gene exchange and open potential avenues to broad-spectrum antiviral drug design.
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Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
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
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Kabsch, W. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889893005588 · Cited by 3,578
Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
Skehel, J. J., & Wiley, D. C. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.531 · Cited by 2,706
Automated protein model building combined with iterative structure refinement.
Anastassis Perrakis, A., Morris, R. J., & Lamzin, V. S. (1999) · Nature Structural Biology · doi:10.1038/8263 · Cited by 2,431
Rational design of potent sialidase-based inhibitors of influenza virus replication
von Itzstein, M., Wu, W.-Y., Kok, G. B., Pegg, M. S., Dyason, J. C., Jin, B., Van Phan, T., Smythe, M. L., White, H. F., Oliver, S. W., et al. (1993) · Nature · doi:10.1038/363418a0 · Cited by 1,862
Use of TLS parameters to model anisotropic displacements in macromolecular refinement
Winn, M. D., Isupov, M. N., & Murshudov, G. N. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900014736 · Cited by 1,696
Cited by
Domingo, E., Sheldon, J., & Perales, C. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05023-11 · Cited by 1,009
Coronavirus Diversity, Phylogeny and Interspecies Jumping
Woo, P. C. Y., Lau, S. K. P., Huang, Y., & Yuen, K.-Y. (2009) · Experimental Biology and Medicine · doi:10.3181/0903-mr-94 · Cited by 758
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
Walls, A. C., Tortorici, M. A., Bosch, B.-J., Frenz, B., Rottier, P. J. M., DiMaio, F., Rey, F. A., & Veesler, D. (2016) · Nature · doi:10.1038/nature16988 · Cited by 538
Accessory proteins of SARS-CoV and other coronaviruses
Liu, D. X., Fung, T. S., Chong, K. K.-L., Shukla, A., & Hilgenfeld, R. (2014) · Antiviral Research · doi:10.1016/j.antiviral.2014.06.013 · Cited by 431
Ecology, evolution and classification of bat coronaviruses in the aftermath of SARS
Drexler, J. F., Corman, V. M., & Drosten, C. (2014) · Antiviral Research · doi:10.1016/j.antiviral.2013.10.013 · Cited by 406
Metadata
- Authors
- Zeng, Q., Langereis, M. A., van Vliet, A. L. W., Huizinga, E. G., & de Groot, R. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-07
- Volume
- 105
- Issue
- 26
- Pages
- 9065-9069
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2141504923
- Cited by
- 288
- References
- 40
- FWCI
- 5.21
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Zeng, Q., Langereis, M. A., van Vliet, A. L. W., Huizinga, E. G., & de Groot, R. J. (2008). Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0800502105
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