Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry.
Identifieur interne : 002735 ( PubMed/Corpus ); précédent : 002734; suivant : 002736Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry.
Auteurs : Heike Hofmann ; Krzysztof Pyrc ; Lia Van Der Hoek ; Martina Geier ; Ben Berkhout ; Stefan PöhlmannSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2005.
English descriptors
- KwdEn :
- Carboxypeptidases (metabolism), Cell Line, Coronavirus 229E, Human (metabolism), Coronavirus Infections (metabolism), Flow Cytometry, Humans, Membrane Glycoproteins (metabolism), Neutralization Tests, Peptidyl-Dipeptidase A, Plasmids (genetics), Receptors, Virus (metabolism), Respiratory Tract Diseases (virology), SARS Virus (metabolism), Species Specificity, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism).
- MESH :
- chemical , metabolism : Carboxypeptidases, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- genetics : Plasmids.
- metabolism : Coronavirus 229E, Human, Coronavirus Infections, SARS Virus.
- virology : Respiratory Tract Diseases.
- Cell Line, Flow Cytometry, Humans, Neutralization Tests, Peptidyl-Dipeptidase A, Species Specificity, Spike Glycoprotein, Coronavirus.
Abstract
Coronavirus (CoV) infection of humans is usually not associated with severe disease. However, discovery of the severe acute respiratory syndrome (SARS) CoV revealed that highly pathogenic human CoVs (HCoVs) can evolve. The identification and characterization of new HCoVs is, therefore, an important task. Recently, a HCoV termed NL63 was discovered in patients with respiratory tract illness. Here, cell tropism and receptor usage of HCoV-NL63 were analyzed. The NL63 spike (S) protein mediated infection of different target cells compared with the closely related 229E-S protein but facilitated entry into cells known to be permissive to SARS-CoV-S-driven infection. An analysis of receptor engagement revealed that NL63-S binds angiotensin-converting enzyme (ACE) 2, the receptor for SARS-CoV, and HCoV-NL63 uses ACE2 as a receptor for infection of target cells. Potent neutralizing activity directed against NL63- but not 229E-S protein was detected in virtually all sera from patients 8 years of age or older, suggesting that HCoV-NL63 infection of humans is common and usually acquired during childhood. Here, we show that SARS-CoV shares its receptor ACE2 with HCoV-NL63. Because the two viruses differ dramatically in their ability to induce disease, analysis of HCoV-NL63 might unravel pathogenicity factors in SARS-CoV. The frequent HCoV-NL63 infection of humans suggests that highly pathogenic variants have ample opportunity to evolve, underlining the need for vaccines against HCoVs.
DOI: 10.1073/pnas.0409465102
PubMed: 15897467
Links to Exploration step
pubmed:15897467Le document en format XML
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<term>Coronavirus Infections (metabolism)</term>
<term>Flow Cytometry</term>
<term>Humans</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Neutralization Tests</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Plasmids (genetics)</term>
<term>Receptors, Virus (metabolism)</term>
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<term>Spike Glycoprotein, Coronavirus</term>
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<term>Receptors, Virus</term>
<term>Viral Envelope Proteins</term>
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<front><div type="abstract" xml:lang="en">Coronavirus (CoV) infection of humans is usually not associated with severe disease. However, discovery of the severe acute respiratory syndrome (SARS) CoV revealed that highly pathogenic human CoVs (HCoVs) can evolve. The identification and characterization of new HCoVs is, therefore, an important task. Recently, a HCoV termed NL63 was discovered in patients with respiratory tract illness. Here, cell tropism and receptor usage of HCoV-NL63 were analyzed. The NL63 spike (S) protein mediated infection of different target cells compared with the closely related 229E-S protein but facilitated entry into cells known to be permissive to SARS-CoV-S-driven infection. An analysis of receptor engagement revealed that NL63-S binds angiotensin-converting enzyme (ACE) 2, the receptor for SARS-CoV, and HCoV-NL63 uses ACE2 as a receptor for infection of target cells. Potent neutralizing activity directed against NL63- but not 229E-S protein was detected in virtually all sera from patients 8 years of age or older, suggesting that HCoV-NL63 infection of humans is common and usually acquired during childhood. Here, we show that SARS-CoV shares its receptor ACE2 with HCoV-NL63. Because the two viruses differ dramatically in their ability to induce disease, analysis of HCoV-NL63 might unravel pathogenicity factors in SARS-CoV. The frequent HCoV-NL63 infection of humans suggests that highly pathogenic variants have ample opportunity to evolve, underlining the need for vaccines against HCoVs.</div>
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<Reference><Citation>Science. 2003 May 30;300(5624):1399-404</Citation>
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