Accessibility navigation


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

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item 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

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation