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

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 d...

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Autores principales: Mathewson, Alison C., Bishop, Alexandra, Yao, Yongxiu, Kemp, Fred, Ren, Junyuan, Chen, Hongying, Xu, Xiaodong, Berkhout, Ben, van der Hoek, Lia, Jones, Ian M.
Formato: Texto
Lenguaje:English
Publicado: Society for General Microbiology 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886958/
https://www.ncbi.nlm.nih.gov/pubmed/18931070
http://dx.doi.org/10.1099/vir.0.2008/003962-0
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author Mathewson, Alison C.
Bishop, Alexandra
Yao, Yongxiu
Kemp, Fred
Ren, Junyuan
Chen, Hongying
Xu, Xiaodong
Berkhout, Ben
van der Hoek, Lia
Jones, Ian M.
author_facet Mathewson, Alison C.
Bishop, Alexandra
Yao, Yongxiu
Kemp, Fred
Ren, Junyuan
Chen, Hongying
Xu, Xiaodong
Berkhout, Ben
van der Hoek, Lia
Jones, Ian M.
author_sort Mathewson, Alison C.
collection PubMed
description 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.
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spelling pubmed-28869582010-07-06 Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2 Mathewson, Alison C. Bishop, Alexandra Yao, Yongxiu Kemp, Fred Ren, Junyuan Chen, Hongying Xu, Xiaodong Berkhout, Ben van der Hoek, Lia Jones, Ian M. J Gen Virol Animal 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. Society for General Microbiology 2008-11 /pmc/articles/PMC2886958/ /pubmed/18931070 http://dx.doi.org/10.1099/vir.0.2008/003962-0 Text en Copyright © 2008, SGM http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Animal
Mathewson, Alison C.
Bishop, Alexandra
Yao, Yongxiu
Kemp, Fred
Ren, Junyuan
Chen, Hongying
Xu, Xiaodong
Berkhout, Ben
van der Hoek, Lia
Jones, Ian M.
Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2
title Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2
title_full Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2
title_fullStr Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2
title_full_unstemmed Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2
title_short Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2
title_sort interaction of severe acute respiratory syndrome-coronavirus and nl63 coronavirus spike proteins with angiotensin converting enzyme-2
topic Animal
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886958/
https://www.ncbi.nlm.nih.gov/pubmed/18931070
http://dx.doi.org/10.1099/vir.0.2008/003962-0
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