SrasV1, Main, Exploration, bibRecord, 004442

Identifying epitopes responsible for neutralizing antibody and DC-SIGN binding on the spike glycoprotein of the severe acute respiratory syndrome coronavirus

Identifieur interne : 004442 ( Main/Exploration ); précédent : 004441; suivant : 004443

Identifying epitopes responsible for neutralizing antibody and DC-SIGN binding on the spike glycoprotein of the severe acute respiratory syndrome coronavirus

Auteurs : Yi-Ping Shih [Taïwan] ; Chia-Yen Chen [Taïwan] ; Shih-Jen Liu [Taïwan] ; Kuan-Hsuan Chen [Taïwan] ; Yuan-Ming Lee [Taïwan] ; Yu-Chan Chao [Taïwan] ; Yi-Ming Arthur Chen [Taïwan]

Source :

Journal of virology [ 0022-538X ] ; 2006.

RBID : Pascal:06-0518524

Descripteurs français

English descriptors

KwdEn :
- Antibodies, Monoclonal, Antibodies, Viral, Antigenic determinant, Antigens, Viral (genetics), Baculoviridae (genetics), Base Sequence, Binding Sites (genetics), Cell Adhesion Molecules (metabolism), Coronavirus, DNA, Viral (genetics), Dendritic Cells (immunology), Dendritic Cells (virology), Epitope Mapping, Epitopes (chemistry), Epitopes (genetics), Glycoprotein, Glycosylation, Humans, In Vitro Techniques, Lectins, C-Type (metabolism), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Microbiology, Models, Molecular, Mutagenesis, Site-Directed, Neutralization Tests, Neutralizing antibody, Protein Binding, Protein Structure, Tertiary, Receptors, Cell Surface (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (immunology), SARS Virus (genetics), SARS Virus (immunology), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (virology), Severe acute respiratory syndrome, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Virology.
MESH :
- chemical , chemistry : Epitopes, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , genetics : Antigens, Viral, DNA, Viral, Epitopes, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Cell Adhesion Molecules, Lectins, C-Type, Receptors, Cell Surface.
- chemical : Antibodies, Monoclonal, Antibodies, Viral, Spike Glycoprotein, Coronavirus.
- genetics : Baculoviridae, Binding Sites, SARS Virus.
- immunology : Dendritic Cells, SARS Virus, Severe Acute Respiratory Syndrome.
- virology : Dendritic Cells, Severe Acute Respiratory Syndrome.
- Base Sequence, Epitope Mapping, Glycosylation, Humans, In Vitro Techniques, Models, Molecular, Mutagenesis, Site-Directed, Neutralization Tests, Protein Binding, Protein Structure, Tertiary.

Abstract

The severe acute respiratory syndrome-associated coronavirus (SARS-CoV) uses dendritic cell-specific ICAM-3 grabbing nonintegrin (DC-SIGN) to facilitate cell entry via cellular receptor-angiotensin-converting enzyme 2. For this project, we used recombinant baculoviruses expressing different lengths of SARS-CoV spike (S) protein in a capture assay to deduce the minimal DC-SIGN binding region. Our results identified the region location between amino acid (aa) residues 324 to 386 of the S protein. We then generated nine monoclonal antibodies (MAbs) against the S protein to map the DC-SIGN-binding domain using capture assays with pseudotyped viruses and observed that MAb SIa5 significantly blocked S protein-DC-SIGN interaction. An enhancement assay using the HKU39849 SARS-CoV strain and human immature dendritic cells confirmed our observation. Data from a pepscan analysis and M13 phage peptide display library system mapped the reactive MAb SIa5 epitope to aa residues 363 to 368 of the S protein. Results from a capture assay testing three pseudotyped viruses with mutated N-linked glycosylation sites of the S protein indicate that only two pseudotyped viruses (N330Q and N357Q, both of which lost glycosylation sites near the SIa5 epitope) had diminished DC-SIGN-binding capacity. We also noted that MAb SIb4 exerted a neutralizing effect against HKU39849; its reactive epitope was mapped to aa residues 435 to 439 of the S protein. We offer the data to facilitate the development of therapeutic agents and preventive vaccines against SARS-CoV infection.

Affiliations:

Taïwan

Le document en format XML

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<term>Baculoviridae (genetics)</term>
<term>Base Sequence</term>
<term>Binding Sites (genetics)</term>
<term>Cell Adhesion Molecules (metabolism)</term>
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<term>Epitopes (genetics)</term>
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<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Microbiology</term>
<term>Models, Molecular</term>
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<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (immunology)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (immunology)</term>
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<term>Viral Envelope Proteins (genetics)</term>
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<term>Anticorps monoclonaux</term>
<term>Antigènes viraux (génétique)</term>
<term>Baculoviridae (génétique)</term>
<term>Cartographie épitopique</term>
<term>Cellules dendritiques (immunologie)</term>
<term>Cellules dendritiques (virologie)</term>
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<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Glycosylation</term>
<term>Humains</term>
<term>Lectines de type C (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Molécules d'adhérence cellulaire (métabolisme)</term>
<term>Mutagenèse dirigée</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
<term>Protéines recombinantes ()</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (immunologie)</term>
<term>Récepteurs de surface cellulaire (métabolisme)</term>
<term>Sites de fixation (génétique)</term>
<term>Structure tertiaire des protéines</term>
<term>Syndrome respiratoire aigu sévère (immunologie)</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Séquence nucléotidique</term>
<term>Techniques in vitro</term>
<term>Tests de neutralisation</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (immunologie)</term>
<term>Épitopes ()</term>
<term>Épitopes (génétique)</term>
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<term>Viral Envelope Proteins</term>
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<term>Epitopes</term>
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<term>Recombinant Proteins</term>
<term>Viral Envelope Proteins</term>
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<term>Baculoviridae</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
<term>Sites de fixation</term>
<term>Virus du SRAS</term>
<term>Épitopes</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Cellules dendritiques</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Dendritic Cells</term>
<term>SARS Virus</term>
<term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lectines de type C</term>
<term>Molécules d'adhérence cellulaire</term>
<term>Récepteurs de surface cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Cellules dendritiques</term>
<term>Syndrome respiratoire aigu sévère</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Dendritic Cells</term>
<term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term>
<term>Epitope Mapping</term>
<term>Glycosylation</term>
<term>Humans</term>
<term>In Vitro Techniques</term>
<term>Models, Molecular</term>
<term>Mutagenesis, Site-Directed</term>
<term>Neutralization Tests</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Anticorps antiviraux</term>
<term>Anticorps monoclonaux</term>
<term>Cartographie épitopique</term>
<term>Coronavirus</term>
<term>Déterminant antigénique</term>
<term>Anticorps neutralisant</term>
<term>Glycoprotéine</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Glycosylation</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Microbiologie</term>
<term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence nucléotidique</term>
<term>Techniques in vitro</term>
<term>Tests de neutralisation</term>
<term>Virologie</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Épitopes</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome-associated coronavirus (SARS-CoV) uses dendritic cell-specific ICAM-3 grabbing nonintegrin (DC-SIGN) to facilitate cell entry via cellular receptor-angiotensin-converting enzyme 2. For this project, we used recombinant baculoviruses expressing different lengths of SARS-CoV spike (S) protein in a capture assay to deduce the minimal DC-SIGN binding region. Our results identified the region location between amino acid (aa) residues 324 to 386 of the S protein. We then generated nine monoclonal antibodies (MAbs) against the S protein to map the DC-SIGN-binding domain using capture assays with pseudotyped viruses and observed that MAb SIa5 significantly blocked S protein-DC-SIGN interaction. An enhancement assay using the HKU39849 SARS-CoV strain and human immature dendritic cells confirmed our observation. Data from a pepscan analysis and M13 phage peptide display library system mapped the reactive MAb SIa5 epitope to aa residues 363 to 368 of the S protein. Results from a capture assay testing three pseudotyped viruses with mutated N-linked glycosylation sites of the S protein indicate that only two pseudotyped viruses (N330Q and N357Q, both of which lost glycosylation sites near the SIa5 epitope) had diminished DC-SIGN-binding capacity. We also noted that MAb SIb4 exerted a neutralizing effect against HKU39849; its reactive epitope was mapped to aa residues 435 to 439 of the S protein. We offer the data to facilitate the development of therapeutic agents and preventive vaccines against SARS-CoV infection.</div>
</front>
</TEI>
<affiliations><list><country><li>Taïwan</li>
</country>
</list>
<tree><country name="Taïwan"><noRegion><name sortKey="Shih, Yi Ping" sort="Shih, Yi Ping" uniqKey="Shih Y" first="Yi-Ping" last="Shih">Yi-Ping Shih</name>
</noRegion>
<name sortKey="Chao, Yu Chan" sort="Chao, Yu Chan" uniqKey="Chao Y" first="Yu-Chan" last="Chao">Yu-Chan Chao</name>
<name sortKey="Chen, Chia Yen" sort="Chen, Chia Yen" uniqKey="Chen C" first="Chia-Yen" last="Chen">Chia-Yen Chen</name>
<name sortKey="Chen, Chia Yen" sort="Chen, Chia Yen" uniqKey="Chen C" first="Chia-Yen" last="Chen">Chia-Yen Chen</name>
<name sortKey="Chen, Kuan Hsuan" sort="Chen, Kuan Hsuan" uniqKey="Chen K" first="Kuan-Hsuan" last="Chen">Kuan-Hsuan Chen</name>
<name sortKey="Chen, Yi Ming Arthur" sort="Chen, Yi Ming Arthur" uniqKey="Chen Y" first="Yi-Ming Arthur" last="Chen">Yi-Ming Arthur Chen</name>
<name sortKey="Chen, Yi Ming Arthur" sort="Chen, Yi Ming Arthur" uniqKey="Chen Y" first="Yi-Ming Arthur" last="Chen">Yi-Ming Arthur Chen</name>
<name sortKey="Lee, Yuan Ming" sort="Lee, Yuan Ming" uniqKey="Lee Y" first="Yuan-Ming" last="Lee">Yuan-Ming Lee</name>
<name sortKey="Lee, Yuan Ming" sort="Lee, Yuan Ming" uniqKey="Lee Y" first="Yuan-Ming" last="Lee">Yuan-Ming Lee</name>
<name sortKey="Liu, Shih Jen" sort="Liu, Shih Jen" uniqKey="Liu S" first="Shih-Jen" last="Liu">Shih-Jen Liu</name>
<name sortKey="Shih, Yi Ping" sort="Shih, Yi Ping" uniqKey="Shih Y" first="Yi-Ping" last="Shih">Yi-Ping Shih</name>
</country>
</tree>
</affiliations>
</record>

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Identifying epitopes responsible for neutralizing antibody and DC-SIGN binding on the spike glycoprotein of the severe acute respiratory syndrome coronavirus

Identifying epitopes responsible for neutralizing antibody and DC-SIGN binding on the spike glycoprotein of the severe acute respiratory syndrome coronavirus

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