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The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages.

Identifieur interne : 003579 ( Main/Exploration ); précédent : 003578; suivant : 003580

The 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 Lu

Source :

RBID : pubmed:17412287

Descripteurs français

English descriptors

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>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>Glycoprotéines membranaires (immunologie)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
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<term>Inflammation (immunologie)</term>
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<term>Macrophages (anatomopathologie)</term>
<term>Macrophages (immunologie)</term>
<term>Poumon (anatomopathologie)</term>
<term>Poumon (immunologie)</term>
<term>Protéine D associée au surfactant pulmonaire (métabolisme)</term>
<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>
<term>Virus du SRAS (immunologie)</term>
<term>Virus du SRAS (métabolisme)</term>
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<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<term>Poumon</term>
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<term>Glycoprotéines membranaires</term>
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<term>Macrophage Activation</term>
<term>Macrophages</term>
<term>SARS Virus</term>
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<term>Membrane Glycoproteins</term>
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<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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