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|Title:||The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages|
|Authors:||Leth-Larsen, R. |
|Citation:||Leth-Larsen, R., Zhong, F., Chow, V.T.K., Lu, J., Holmskov, U. (2007). The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages. Immunobiology 212 (3) : 201-211. ScholarBank@NUS Repository. https://doi.org/10.1016/j.imbio.2006.12.001|
|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 Ca2+ 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. © 2006 Elsevier GmbH. All rights reserved.|
|Appears in Collections:||Staff Publications|
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