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

Rikke Leth-Larsen, Fei Zhong, Vincent T K Chow, Uffe Holmskov, Jinhua Lu

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

 
Udgivelsesdato: 2007
OriginalsprogEngelsk
TidsskriftImmunobiology
Vol/bind212
Udgave nummer3
Sider (fra-til)201-11
Antal sider10
ISSN0171-2985
DOI
StatusUdgivet - 1. jan. 2007

Fingeraftryk

Coronavirus Spike Glycoproteins
Pulmonary Surfactant-Associated Proteins
Pulmonary Surfactant-Associated Protein D
SARS Virus
Macrophages
Severe Acute Respiratory Syndrome
Proteins
Coronavirus
Lung
Tunicamycin
Maltose
HEK293 Cells

Citer dette

@article{b36ea030ec5111dc86ef000ea68e967b,
title = "The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages",
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",
keywords = "Animals, Cell Line, Cercopithecus aethiops, Humans, Inflammation, Lung, Macrophage Activation, Macrophages, Membrane Glycoproteins, Pulmonary Surfactant-Associated Protein D, SARS Virus, Vero Cells, Viral Envelope Proteins",
author = "Rikke Leth-Larsen and Fei Zhong and Chow, {Vincent T K} and Uffe Holmskov and Jinhua Lu",
year = "2007",
month = "1",
day = "1",
doi = "10.1016/j.imbio.2006.12.001",
language = "English",
volume = "212",
pages = "201--11",
journal = "Immunobiology",
issn = "0171-2985",
publisher = "Elsevier",
number = "3",

}

The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages. / Leth-Larsen, Rikke; Zhong, Fei; Chow, Vincent T K; Holmskov, Uffe; Lu, Jinhua.

I: Immunobiology, Bind 212, Nr. 3, 01.01.2007, s. 201-11.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages

AU - Leth-Larsen, Rikke

AU - Zhong, Fei

AU - Chow, Vincent T K

AU - Holmskov, Uffe

AU - Lu, Jinhua

PY - 2007/1/1

Y1 - 2007/1/1

N2 - 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

AB - 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

KW - Animals

KW - Cell Line

KW - Cercopithecus aethiops

KW - Humans

KW - Inflammation

KW - Lung

KW - Macrophage Activation

KW - Macrophages

KW - Membrane Glycoproteins

KW - Pulmonary Surfactant-Associated Protein D

KW - SARS Virus

KW - Vero Cells

KW - Viral Envelope Proteins

U2 - 10.1016/j.imbio.2006.12.001

DO - 10.1016/j.imbio.2006.12.001

M3 - Journal article

VL - 212

SP - 201

EP - 211

JO - Immunobiology

JF - Immunobiology

SN - 0171-2985

IS - 3

ER -