SrasV1, Ncbi, Merge, bibRecord, 001D84

Conserved amino acids W423 and N424 in receptor-binding domain of SARS-CoV are potential targets for therapeutic monoclonal antibody.

Identifieur interne : 001D84 ( Ncbi/Merge ); précédent : 001D83; suivant : 001D85

Conserved amino acids W423 and N424 in receptor-binding domain of SARS-CoV are potential targets for therapeutic monoclonal antibody.

Auteurs : Chao Bian [République populaire de Chine] ; Xiuqin Zhang ; Xingfeng Cai ; Linqi Zhang ; Zhiwei Chen ; Ye Zha ; Ying Xu ; Ke Xu ; Wei Lu ; Linchen Yan ; Jianwei Yuan ; Jiannan Feng ; Pei Hao ; Qidi Wang ; Guoping Zhao ; Gang Liu ; Xueliang Zhu ; Hao Shen ; Bojian Zheng ; Beifen Shen ; Bing Sun

Source :

Virology [ 1096-0341 ] ; 2009.

RBID : pubmed:18986662

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (isolation & purification), Antibodies, Monoclonal (therapeutic use), Antibodies, Viral (immunology), Antibodies, Viral (isolation & purification), Antibodies, Viral (therapeutic use), Conserved Sequence (immunology), Epitopes (immunology), Female, Humans, Membrane Glycoproteins (antagonists & inhibitors), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Mice, Mice, Inbred BALB C, Models, Molecular, Molecular Sequence Data, Neutralization Tests, Protein Structure, Tertiary, SARS Virus (immunology), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (antagonists & inhibitors), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology), Virus Attachment.
MESH :
- chemical , antagonists & inhibitors : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Epitopes, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , isolation & purification : Antibodies, Monoclonal, Antibodies, Viral.
- chemical , therapeutic use : Antibodies, Monoclonal, Antibodies, Viral.
- immunology : Conserved Sequence, SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Female, Humans, Mice, Mice, Inbred BALB C, Models, Molecular, Molecular Sequence Data, Neutralization Tests, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Virus Attachment.

Abstract

The receptor-binding domain (RBD) on spike protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the main region interacting with the viral receptor-ACE2 and is a useful target for induction of neutralizing antibodies against SARS-CoV infection. Here we generated two monoclonal antibodies (mAbs), targeting RBD, with marked virus neutralizing activity. The mAbs recognize a new conformational epitope which consists of several discontinuous peptides (aa. 343-367, 373-390 and 411-428) and is spatially located neighboring the receptor-binding motif (RPM) region of the RBD. Importantly, W423 and N424 residues are essential for mAb recognition and are highly conserved among 107 different strains of SARS, indicating that the residues are the most critical in the epitope which is a novel potential target for therapeutic mAbs. A human-mouse chimeric antibody, based upon the original murine mAb, was also constructed and shown to possess good neutralizing activity and high affinity.

DOI: 10.1016/j.virol.2008.09.029
PubMed: 18986662

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001A34
to stream PubMed, to step Curation: 001A34
to stream PubMed, to step Checkpoint: 001920

Links to Exploration step

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The receptor-binding domain (RBD) on spike protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the main region interacting with the viral receptor-ACE2 and is a useful target for induction of neutralizing antibodies against SARS-CoV infection. Here we generated two monoclonal antibodies (mAbs), targeting RBD, with marked virus neutralizing activity. The mAbs recognize a new conformational epitope which consists of several discontinuous peptides (aa. 343-367, 373-390 and 411-428) and is spatially located neighboring the receptor-binding motif (RPM) region of the RBD. Importantly, W423 and N424 residues are essential for mAb recognition and are highly conserved among 107 different strains of SARS, indicating that the residues are the most critical in the epitope which is a novel potential target for therapeutic mAbs. A human-mouse chimeric antibody, based upon the original murine mAb, was also constructed and shown to possess good neutralizing activity and high affinity.</div>
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<Abstract><AbstractText>The receptor-binding domain (RBD) on spike protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the main region interacting with the viral receptor-ACE2 and is a useful target for induction of neutralizing antibodies against SARS-CoV infection. Here we generated two monoclonal antibodies (mAbs), targeting RBD, with marked virus neutralizing activity. The mAbs recognize a new conformational epitope which consists of several discontinuous peptides (aa. 343-367, 373-390 and 411-428) and is spatially located neighboring the receptor-binding motif (RPM) region of the RBD. Importantly, W423 and N424 residues are essential for mAb recognition and are highly conserved among 107 different strains of SARS, indicating that the residues are the most critical in the epitope which is a novel potential target for therapeutic mAbs. A human-mouse chimeric antibody, based upon the original murine mAb, was also constructed and shown to possess good neutralizing activity and high affinity.</AbstractText>
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Conserved amino acids W423 and N424 in receptor-binding domain of SARS-CoV are potential targets for therapeutic monoclonal antibody.

Conserved amino acids W423 and N424 in receptor-binding domain of SARS-CoV are potential targets for therapeutic monoclonal antibody.

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