Please use this identifier to cite or link to this item:
|Title:||The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages||Authors:||Leth-Larsen, R.
|Issue Date:||2007||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.||Source Title:||Immunobiology||URI:||http://scholarbank.nus.edu.sg/handle/10635/24861||ISSN:||01712985||DOI:||10.1016/j.imbio.2006.12.001|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on May 20, 2020
WEB OF SCIENCETM
checked on May 12, 2020
checked on May 13, 2020
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.