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Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2

Mathewson, A. C., Bishop, A., Yao, Y., Kemp, F., Ren, J., Chen, H., Xu, X., Berkhout, B., van der Hoek, L. and Jones, I. M. (2008) Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2. Journal of General Virology, 89. pp. 2741-2745. ISSN 0022-1317

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To link to this article DOI: 10.1099/vir.0.2008/003962-0

Abstract/Summary

Although in different groups, the coronaviruses severe acute respiratory syndrome-coronavirus (SARS-CoV) and NL63 use the same receptor, angiotensin converting enzyme (ACE)-2, for entry into the host cell. Despite this common receptor, the consequence of entry is very different; severe respiratory distress in the case of SARS-CoV but frequently only a mild respiratory infection for NL63. Using a wholly recombinant system, we have investigated the ability of each virus receptor-binding protein, spike or S protein, to bind to ACE-2 in solution and on the cell surface. In both assays, we find that the NL63 S protein has a weaker interaction with ACE-2 than the SARS-CoV S protein, particularly in solution binding, but the residues required for contact are similar. We also confirm that the ACE-2-binding site of NL63 S lies between residues 190 and 739. A lower-affinity interaction with ACE-2 might partly explain the different pathological consequences of infection by SARS-CoV and NL63.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences
Faculty of Life Sciences > School of Biological Sciences
ID Code:9846
Uncontrolled Keywords:SARS-CORONAVIRUS, RECEPTOR, ACE2, IDENTIFICATION, BINDING, DOMAIN, RESIDUES, REGIONS, VIRUS

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