The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages.
Identifieur interne : 003579 ( Main/Exploration ); précédent : 003578; suivant : 003580The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages.
Auteurs : Rikke Leth-Larsen [Singapour] ; Fei Zhong ; Vincent T K. Chow ; Uffe Holmskov ; Jinhua LuSource :
- Immunobiology [ 0171-2985 ] ; 2007.
Descripteurs français
- KwdFr :
- Activation des macrophages (immunologie), Animaux, Cellules Vero, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Humains, Inflammation (immunologie), Lignée cellulaire, Macrophages (anatomopathologie), Macrophages (immunologie), Poumon (anatomopathologie), Poumon (immunologie), Protéine D associée au surfactant pulmonaire (métabolisme), Protéine D associée au surfactant pulmonaire (physiologie), Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Virus du SRAS (immunologie), Virus du SRAS (métabolisme).
- MESH :
- anatomopathologie : Macrophages, Poumon.
- immunologie : Activation des macrophages, Glycoprotéines membranaires, Inflammation, Macrophages, Poumon, Protéines de l'enveloppe virale, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéine D associée au surfactant pulmonaire, Protéines de l'enveloppe virale, Virus du SRAS.
- physiologie : Protéine D associée au surfactant pulmonaire.
- Animaux, Cellules Vero, Glycoprotéine de spicule des coronavirus, Humains, Lignée cellulaire.
English descriptors
- KwdEn :
- Animals, Cell Line, Chlorocebus aethiops, Humans, Inflammation (immunology), Lung (immunology), Lung (pathology), Macrophage Activation (immunology), Macrophages (immunology), Macrophages (pathology), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Pulmonary Surfactant-Associated Protein D (metabolism), Pulmonary Surfactant-Associated Protein D (physiology), SARS Virus (immunology), SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , immunology : Membrane Glycoproteins, Viral Envelope Proteins.
- immunology : Inflammation, Lung, Macrophage Activation, Macrophages, SARS Virus.
- chemical , metabolism : Membrane Glycoproteins, Pulmonary Surfactant-Associated Protein D, SARS Virus, Viral Envelope Proteins.
- pathology : Lung, Macrophages.
- chemical , physiology : Pulmonary Surfactant-Associated Protein D.
- Animals, Cell Line, Chlorocebus aethiops, Humans, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) infects host cells with its surface glycosylated spike-protein (S-protein). Here we expressed the SARS-CoV S-protein to investigate its interactions with innate immune mechanisms in the lung. The purified S-protein was detected as a 210 kDa glycosylated protein. It was not secreted in the presence of tunicamycin and was detected as a 130 kDa protein in the cell lysate. The purified S-protein bound to Vero but not 293T cells and was itself recognized by lung surfactant protein D (SP-D), a collectin found in the lung alveoli. The binding required Ca(2+) and was inhibited by maltose. The serum collectin, mannan-binding lectin (MBL), exhibited no detectable binding to the purified S-protein. S-protein binds and activates macrophages but not dendritic cells (DCs). It suggests that SARS-CoV interacts with innate immune mechanisms in the lung through its S-protein and regulates pulmonary inflammation.
DOI: 10.1016/j.imbio.2006.12.001
PubMed: 17412287
Affiliations:
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Le document en format XML
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<term>Humans</term>
<term>Inflammation (immunology)</term>
<term>Lung (immunology)</term>
<term>Lung (pathology)</term>
<term>Macrophage Activation (immunology)</term>
<term>Macrophages (immunology)</term>
<term>Macrophages (pathology)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Pulmonary Surfactant-Associated Protein D (metabolism)</term>
<term>Pulmonary Surfactant-Associated Protein D (physiology)</term>
<term>SARS Virus (immunology)</term>
<term>SARS Virus (metabolism)</term>
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<term>Viral Envelope Proteins (immunology)</term>
<term>Viral Envelope Proteins (metabolism)</term>
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<term>Animaux</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
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<term>Macrophages (immunologie)</term>
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<term>Poumon (immunologie)</term>
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<term>Protéine D associée au surfactant pulmonaire (physiologie)</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
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<term>Virus du SRAS (métabolisme)</term>
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<term>Viral Envelope Proteins</term>
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<term>Macrophages</term>
<term>Poumon</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus du SRAS</term>
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<term>Lung</term>
<term>Macrophage Activation</term>
<term>Macrophages</term>
<term>SARS Virus</term>
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<term>Viral Envelope Proteins</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) infects host cells with its surface glycosylated spike-protein (S-protein). Here we expressed the SARS-CoV S-protein to investigate its interactions with innate immune mechanisms in the lung. The purified S-protein was detected as a 210 kDa glycosylated protein. It was not secreted in the presence of tunicamycin and was detected as a 130 kDa protein in the cell lysate. The purified S-protein bound to Vero but not 293T cells and was itself recognized by lung surfactant protein D (SP-D), a collectin found in the lung alveoli. The binding required Ca(2+) and was inhibited by maltose. The serum collectin, mannan-binding lectin (MBL), exhibited no detectable binding to the purified S-protein. S-protein binds and activates macrophages but not dendritic cells (DCs). It suggests that SARS-CoV interacts with innate immune mechanisms in the lung through its S-protein and regulates pulmonary inflammation.</div>
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