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Specific Asparagine-Linked Glycosylation Sites Are Critical for DC-SIGN- and L-SIGN-Mediated Severe Acute Respiratory Syndrome Coronavirus Entry▿

Identifieur interne : 001A47 ( Ncbi/Curation ); précédent : 001A46; suivant : 001A48

Specific Asparagine-Linked Glycosylation Sites Are Critical for DC-SIGN- and L-SIGN-Mediated Severe Acute Respiratory Syndrome Coronavirus Entry▿

Auteurs : Dong P. Han ; Motashim Lohani ; Michael W. Cho

Source :

Journal of Virology [ 0022-538X ] ; 2007.

RBID : PMC:2168787

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Asparagine (chemistry), Cell Adhesion Molecules (chemistry), Chlorocebus aethiops, Glycosylation, HeLa Cells, Humans, Lectins (chemistry), Lectins, C-Type (chemistry), Molecular Sequence Data, Mutagenesis, Site-Directed, Receptors, Cell Surface (chemistry), SARS Virus (metabolism), Sequence Homology, Amino Acid, Severe Acute Respiratory Syndrome (virology), Vero Cells.
MESH :
- chemical , chemistry : Asparagine, Cell Adhesion Molecules, Lectins, Lectins, C-Type, Receptors, Cell Surface.
- metabolism : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Animals, Chlorocebus aethiops, Glycosylation, HeLa Cells, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Vero Cells.

Abstract

Severe acute respiratory syndrome (SARS) is caused by a newly emerged coronavirus (CoV) designated SARS-CoV. The virus utilizes angiotensin-converting enzyme 2 (ACE2) as the primary receptor. Although the idea is less clear and somewhat controversial, SARS-CoV is thought to use C-type lectins DC-SIGN and/or L-SIGN (collectively referred to as DC/L-SIGN) as alternative receptors or as enhancer factors that facilitate ACE2-mediated virus infection. In this study, the function of DC/L-SIGN in SARS-CoV infection was examined in detail. The results of our study clearly demonstrate that both proteins serve as receptors independently of ACE2 and that there is a minimal level of synergy between DC/L-SIGN and ACE2. As expected, glycans on spike (S) glycoprotein are important for DC/L-SIGN-mediated virus infection. Site-directed mutagenesis analyses have identified seven glycosylation sites on the S protein critical for DC/L-SIGN-mediated virus entry. They include asparagine residues at amino acid positions 109, 118, 119, 158, 227, 589, and 699, which are distinct from residues of the ACE2-binding domain (amino acids 318 to 510). Amino acid sequence analyses of S proteins encoded by viruses isolated from animals and humans suggest that glycosylation sites N227 and N699 have facilitated zoonotic transmission.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2168787

DOI: 10.1128/JVI.00315-07
PubMed: 17715238
PubMed Central: 2168787

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PMC:2168787

Le document en format XML

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<term>Humains</term>
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<front><div type="abstract" xml:lang="en"><p>Severe acute respiratory syndrome (SARS) is caused by a newly emerged coronavirus (CoV) designated SARS-CoV. The virus utilizes angiotensin-converting enzyme 2 (ACE2) as the primary receptor. Although the idea is less clear and somewhat controversial, SARS-CoV is thought to use C-type lectins DC-SIGN and/or L-SIGN (collectively referred to as DC/L-SIGN) as alternative receptors or as enhancer factors that facilitate ACE2-mediated virus infection. In this study, the function of DC/L-SIGN in SARS-CoV infection was examined in detail. The results of our study clearly demonstrate that both proteins serve as receptors independently of ACE2 and that there is a minimal level of synergy between DC/L-SIGN and ACE2. As expected, glycans on spike (S) glycoprotein are important for DC/L-SIGN-mediated virus infection. Site-directed mutagenesis analyses have identified seven glycosylation sites on the S protein critical for DC/L-SIGN-mediated virus entry. They include asparagine residues at amino acid positions 109, 118, 119, 158, 227, 589, and 699, which are distinct from residues of the ACE2-binding domain (amino acids 318 to 510). Amino acid sequence analyses of S proteins encoded by viruses isolated from animals and humans suggest that glycosylation sites N227 and N699 have facilitated zoonotic transmission.</p>
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Specific Asparagine-Linked Glycosylation Sites Are Critical for DC-SIGN- and L-SIGN-Mediated Severe Acute Respiratory Syndrome Coronavirus Entry▿

Specific Asparagine-Linked Glycosylation Sites Are Critical for DC-SIGN- and L-SIGN-Mediated Severe Acute Respiratory Syndrome Coronavirus Entry▿

Source :

Descripteurs français

English descriptors

Abstract

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Le document en format XML

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