Specific asparagine-linked glycosylation sites are critical for DC-SIGN-and L-SIGN-mediated severe acute respiratory syndrome coronavirus entry
Identifieur interne : 003B24 ( Main/Exploration ); précédent : 003B23; suivant : 003B25Specific asparagine-linked glycosylation sites are critical for DC-SIGN-and L-SIGN-mediated severe acute respiratory syndrome coronavirus entry
Auteurs : Dong P. Han [États-Unis] ; Motashim Lohani [États-Unis] ; Michael W. Cho [États-Unis]Source :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux, Asparagine (), Cellules HeLa, Cellules Vero, Données de séquences moléculaires, Glycosylation, Humains, Lectines (), Lectines de type C (), Molécules d'adhérence cellulaire (), Mutagenèse dirigée, Récepteurs de surface cellulaire (), Similitude de séquences d'acides aminés, Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Pascal (Inist)
- Animaux, Asparagine, Cellules HeLa, Cellules Vero, Coronavirus, Asparagine, Données de séquences moléculaires, Glycosylation, Aigu, Humains, Lectines, Lectines de type C, Molécules d'adhérence cellulaire, Mutagenèse dirigée, Récepteurs de surface cellulaire, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Virologie.
English descriptors
- KwdEn :
- Acute, Amino Acid Sequence, Animals, Asparagine, Asparagine (chemistry), Cell Adhesion Molecules (chemistry), Chlorocebus aethiops, Coronavirus, 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, Virology.
- 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.
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Affiliations:
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Le document en format XML
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Han</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Medicine, Case Western Reserve University School of Medicine</s1><s2>Cleveland, Ohio 44106</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Cleveland, Ohio 44106</wicri:noRegion></affiliation></author><author><name sortKey="Lohani, Motashim" sort="Lohani, Motashim" uniqKey="Lohani M" first="Motashim" last="Lohani">Motashim Lohani</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Medicine, Case Western Reserve University School of Medicine</s1><s2>Cleveland, Ohio 44106</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Cleveland, Ohio 44106</wicri:noRegion></affiliation></author><author><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Medicine, Case Western Reserve University School of Medicine</s1><s2>Cleveland, Ohio 44106</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Cleveland, Ohio 44106</wicri:noRegion></affiliation><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Biochemistry, Case Western Reserve University School of Medicine</s1><s2>Cleveland, Ohio 44106</s2><s3>USA</s3><sZ>3 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Cleveland, Ohio 44106</wicri:noRegion></affiliation><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine</s1><s2>Cleveland, Ohio 44106</s2><s3>USA</s3><sZ>3 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Cleveland, Ohio 44106</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno><imprint><date when="2007">2007</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acute</term><term>Amino Acid Sequence</term><term>Animals</term><term>Asparagine</term><term>Asparagine (chemistry)</term><term>Cell Adhesion Molecules (chemistry)</term><term>Chlorocebus aethiops</term><term>Coronavirus</term><term>Glycosylation</term><term>HeLa Cells</term><term>Humans</term><term>Lectins (chemistry)</term><term>Lectins, C-Type (chemistry)</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Receptors, Cell Surface (chemistry)</term><term>SARS Virus (metabolism)</term><term>Sequence Homology, Amino Acid</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Vero Cells</term><term>Virology</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Asparagine ()</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Données de séquences moléculaires</term><term>Glycosylation</term><term>Humains</term><term>Lectines ()</term><term>Lectines de type C ()</term><term>Molécules d'adhérence cellulaire ()</term><term>Mutagenèse dirigée</term><term>Récepteurs de surface cellulaire ()</term><term>Similitude de séquences d'acides aminés</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Asparagine</term><term>Cell Adhesion Molecules</term><term>Lectins</term><term>Lectins, C-Type</term><term>Receptors, Cell Surface</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Chlorocebus aethiops</term><term>Glycosylation</term><term>HeLa Cells</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Animaux</term><term>Asparagine</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Coronavirus</term><term>Asparagine</term><term>Données de séquences moléculaires</term><term>Glycosylation</term><term>Aigu</term><term>Humains</term><term>Lectines</term><term>Lectines de type C</term><term>Molécules d'adhérence cellulaire</term><term>Mutagenèse dirigée</term><term>Récepteurs de surface cellulaire</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Virologie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Han, Dong P" sort="Han, Dong P" uniqKey="Han D" first="Dong P." last="Han">Dong P. Han</name></noRegion><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><name sortKey="Lohani, Motashim" sort="Lohani, Motashim" uniqKey="Lohani M" first="Motashim" last="Lohani">Motashim Lohani</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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