Human coronavirus NL63 utilizes heparan sulfate proteoglycans for attachment to target cells.
Identifieur interne : 001638 ( Main/Exploration ); précédent : 001637; suivant : 001639Human coronavirus NL63 utilizes heparan sulfate proteoglycans for attachment to target cells.
Auteurs : Aleksandra Milewska [Pologne] ; Miroslaw Zarebski [Pologne] ; Paulina Nowak [Pologne] ; Karol Stozek [Pologne] ; Jan Potempa [États-Unis] ; Krzysztof Pyrc [Pologne]Source :
- Journal of virology [ 1098-5514 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Peptidyl-Dipeptidase A.
- métabolisme : Peptidyl-Dipeptidase A, Protéoglycanes à sulfate d'héparane.
- physiologie : Coronavirus humain NL63.
- Animaux, Attachement viral, Humains, Lignée cellulaire.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Peptidyl-Dipeptidase A.
- chemical , metabolism : Heparan Sulfate Proteoglycans, Peptidyl-Dipeptidase A.
- physiology : Coronavirus NL63, Human.
- Animals, Cell Line, Humans, Virus Attachment.
Abstract
Human coronavirus NL63 (HCoV-NL63) is an alphacoronavirus that was first identified in 2004 in the nasopharyngeal aspirate from a 7-month-old patient with a respiratory tract infection. Previous studies showed that HCoV-NL63 and the genetically distant severe acute respiratory syndrome (SARS)-CoV employ the same receptor for host cell entry, angiotensin-converting enzyme 2 (ACE2), but it is largely unclear whether ACE2 interactions are sufficient to allow HCoV-NL63 binding to cells. The present study showed that directed expression of angiotensin-converting enzyme 2 (ACE2) on cells previously resistant to HCoV-NL63 renders them susceptible, showing that ACE2 protein acts as a functional receptor and that its expression is required for infection. However, comparative analysis showed that directed expression or selective scission of the ACE2 protein had no measurable effect on virus adhesion. In contrast, binding of HCoV-NL63 to heparan sulfates was required for viral attachment and infection of target cells, showing that these molecules serve as attachment receptors for HCoV-NL63.
DOI: 10.1128/JVI.02078-14
PubMed: 25187545
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Human coronavirus NL63 (HCoV-NL63) is an alphacoronavirus that was first identified in 2004 in the nasopharyngeal aspirate from a 7-month-old patient with a respiratory tract infection. Previous studies showed that HCoV-NL63 and the genetically distant severe acute respiratory syndrome (SARS)-CoV employ the same receptor for host cell entry, angiotensin-converting enzyme 2 (ACE2), but it is largely unclear whether ACE2 interactions are sufficient to allow HCoV-NL63 binding to cells. The present study showed that directed expression of angiotensin-converting enzyme 2 (ACE2) on cells previously resistant to HCoV-NL63 renders them susceptible, showing that ACE2 protein acts as a functional receptor and that its expression is required for infection. However, comparative analysis showed that directed expression or selective scission of the ACE2 protein had no measurable effect on virus adhesion. In contrast, binding of HCoV-NL63 to heparan sulfates was required for viral attachment and infection of target cells, showing that these molecules serve as attachment receptors for HCoV-NL63.</div>
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