SrasV1, Ncbi, Merge, bibRecord, 002920

Substitution at aspartic acid 1128 in the SARS coronavirus spike glycoprotein mediates escape from a S2 domain-targeting neutralizing monoclonal antibody.

Identifieur interne : 002920 ( Ncbi/Merge ); précédent : 002919; suivant : 002921

Substitution at aspartic acid 1128 in the SARS coronavirus spike glycoprotein mediates escape from a S2 domain-targeting neutralizing monoclonal antibody.

Auteurs : Oi-Wing Ng [Singapour] ; Choong-Tat Keng [Singapour] ; Cynthia Sau-Wai Leung [République populaire de Chine] ; J S Malik Peiris [République populaire de Chine] ; Leo Lit Man Poon [République populaire de Chine] ; Yee-Joo Tan [Singapour]

Source :

PloS one [ 1932-6203 ] ; 2014.

RBID : pubmed:25019613

Descripteurs français

KwdFr :
- Acide aspartique (), Alignement de séquences, Animaux, Anticorps antiviraux (physiologie), Anticorps monoclonaux (physiologie), Anticorps neutralisants (physiologie), Cartographie épitopique, Cellules CHO, Cellules HEK293, Cellules Vero, Chiroptera (virologie), Cricetulus, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (immunologie), Humains, Souris de lignée BALB C, Substitution d'acide aminé, Séquence d'acides aminés, Tests de neutralisation, Virion (génétique), Virion (pathogénicité), Virus du SRAS (génétique), Virus du SRAS (métabolisme), Virus du SRAS (pathogénicité), Viverridae (virologie).
MESH :
- génétique : Glycoprotéine de spicule des coronavirus, Virion, Virus du SRAS.
- immunologie : Glycoprotéine de spicule des coronavirus.
- métabolisme : Virus du SRAS.
- pathogénicité : Virion, Virus du SRAS.
- physiologie : Anticorps antiviraux, Anticorps monoclonaux, Anticorps neutralisants.
- virologie : Chiroptera, Viverridae.
- Acide aspartique, Alignement de séquences, Animaux, Cartographie épitopique, Cellules CHO, Cellules HEK293, Cellules Vero, Cricetulus, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Humains, Souris de lignée BALB C, Substitution d'acide aminé, Séquence d'acides aminés, Tests de neutralisation.

English descriptors

KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Animals, Antibodies, Monoclonal (physiology), Antibodies, Neutralizing (physiology), Antibodies, Viral (physiology), Aspartic Acid (chemistry), CHO Cells, Chiroptera (virology), Chlorocebus aethiops, Cricetulus, Epitope Mapping, HEK293 Cells, Humans, Mice, Inbred BALB C, Molecular Sequence Data, Neutralization Tests, SARS Virus (genetics), SARS Virus (metabolism), SARS Virus (pathogenicity), Sequence Alignment, Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (immunology), Vero Cells, Virion (genetics), Virion (pathogenicity), Viverridae (virology).
MESH :
- chemical , chemistry : Aspartic Acid, Spike Glycoprotein, Coronavirus.
- chemical , genetics : Spike Glycoprotein, Coronavirus.
- chemical , immunology : Spike Glycoprotein, Coronavirus.
- chemical , physiology : Antibodies, Monoclonal, Antibodies, Neutralizing, Antibodies, Viral.
- genetics : SARS Virus, Virion.
- metabolism : SARS Virus.
- pathogenicity : SARS Virus, Virion.
- virology : Chiroptera, Viverridae.
- Amino Acid Sequence, Amino Acid Substitution, Animals, CHO Cells, Chlorocebus aethiops, Cricetulus, Epitope Mapping, HEK293 Cells, Humans, Mice, Inbred BALB C, Molecular Sequence Data, Neutralization Tests, Sequence Alignment, Vero Cells.

Abstract

The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is the etiological agent for the infectious disease, SARS, which first emerged 10 years ago. SARS-CoV is a zoonotic virus that has crossed the species barriers to infect humans. Bats, which harbour a diverse pool of SARS-like CoVs (SL-CoVs), are believed to be the natural reservoir. The SARS-CoV surface Spike (S) protein is a major antigenic determinant in eliciting neutralizing antibody production during SARS-CoV infection. In our previous work, we showed that a panel of murine monoclonal antibodies (mAbs) that target the S2 subunit of the S protein are capable of neutralizing SARS-CoV infection in vitro (Lip KM et al, J Virol. 2006 Jan; 80(2): 941-50). In this study, we report our findings on the characterization of one of these mAbs, known as 1A9, which binds to the S protein at a novel epitope within the S2 subunit at amino acids 1111-1130. MAb 1A9 is a broadly neutralizing mAb that prevents viral entry mediated by the S proteins of human and civet SARS-CoVs as well as bat SL-CoVs. By generating mutant SARS-CoV that escapes the neutralization by mAb 1A9, the residue D1128 in S was found to be crucial for its interaction with mAb 1A9. S protein containing the substitution of D1128 with alanine (D1128A) exhibited a significant decrease in binding capability to mAb 1A9 compared to wild-type S protein. By using a pseudotyped viral entry assay, it was shown that the D1128A substitution in the escape virus allows it to overcome the viral entry blockage by mAb 1A9. In addition, the D1128A mutation was found to exert no effects on the S protein cell surface expression and incorporation into virion particles, suggesting that the escape virus retains the same viral entry property as the wild-type virus.

DOI: 10.1371/journal.pone.0102415
PubMed: 25019613

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to stream PubMed, to step Corpus: 000F67
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<term>CHO Cells</term>
<term>Chlorocebus aethiops</term>
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<front><div type="abstract" xml:lang="en">The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is the etiological agent for the infectious disease, SARS, which first emerged 10 years ago. SARS-CoV is a zoonotic virus that has crossed the species barriers to infect humans. Bats, which harbour a diverse pool of SARS-like CoVs (SL-CoVs), are believed to be the natural reservoir. The SARS-CoV surface Spike (S) protein is a major antigenic determinant in eliciting neutralizing antibody production during SARS-CoV infection. In our previous work, we showed that a panel of murine monoclonal antibodies (mAbs) that target the S2 subunit of the S protein are capable of neutralizing SARS-CoV infection in vitro (Lip KM et al, J Virol. 2006 Jan; 80(2): 941-50). In this study, we report our findings on the characterization of one of these mAbs, known as 1A9, which binds to the S protein at a novel epitope within the S2 subunit at amino acids 1111-1130. MAb 1A9 is a broadly neutralizing mAb that prevents viral entry mediated by the S proteins of human and civet SARS-CoVs as well as bat SL-CoVs. By generating mutant SARS-CoV that escapes the neutralization by mAb 1A9, the residue D1128 in S was found to be crucial for its interaction with mAb 1A9. S protein containing the substitution of D1128 with alanine (D1128A) exhibited a significant decrease in binding capability to mAb 1A9 compared to wild-type S protein. By using a pseudotyped viral entry assay, it was shown that the D1128A substitution in the escape virus allows it to overcome the viral entry blockage by mAb 1A9. In addition, the D1128A mutation was found to exert no effects on the S protein cell surface expression and incorporation into virion particles, suggesting that the escape virus retains the same viral entry property as the wild-type virus. </div>
</front>
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<Abstract><AbstractText>The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is the etiological agent for the infectious disease, SARS, which first emerged 10 years ago. SARS-CoV is a zoonotic virus that has crossed the species barriers to infect humans. Bats, which harbour a diverse pool of SARS-like CoVs (SL-CoVs), are believed to be the natural reservoir. The SARS-CoV surface Spike (S) protein is a major antigenic determinant in eliciting neutralizing antibody production during SARS-CoV infection. In our previous work, we showed that a panel of murine monoclonal antibodies (mAbs) that target the S2 subunit of the S protein are capable of neutralizing SARS-CoV infection in vitro (Lip KM et al, J Virol. 2006 Jan; 80(2): 941-50). In this study, we report our findings on the characterization of one of these mAbs, known as 1A9, which binds to the S protein at a novel epitope within the S2 subunit at amino acids 1111-1130. MAb 1A9 is a broadly neutralizing mAb that prevents viral entry mediated by the S proteins of human and civet SARS-CoVs as well as bat SL-CoVs. By generating mutant SARS-CoV that escapes the neutralization by mAb 1A9, the residue D1128 in S was found to be crucial for its interaction with mAb 1A9. S protein containing the substitution of D1128 with alanine (D1128A) exhibited a significant decrease in binding capability to mAb 1A9 compared to wild-type S protein. By using a pseudotyped viral entry assay, it was shown that the D1128A substitution in the escape virus allows it to overcome the viral entry blockage by mAb 1A9. In addition, the D1128A mutation was found to exert no effects on the S protein cell surface expression and incorporation into virion particles, suggesting that the escape virus retains the same viral entry property as the wild-type virus. </AbstractText>
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<ForeName>Oi-Wing</ForeName>
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<ForeName>Choong-Tat</ForeName>
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<Author ValidYN="Y"><LastName>Leung</LastName>
<ForeName>Cynthia Sau-Wai</ForeName>
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Substitution at aspartic acid 1128 in the SARS coronavirus spike glycoprotein mediates escape from a S2 domain-targeting neutralizing monoclonal antibody.

Substitution at aspartic acid 1128 in the SARS coronavirus spike glycoprotein mediates escape from a S2 domain-targeting neutralizing monoclonal antibody.

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