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A truncated receptor-binding domain of MERS-CoV spike protein potently inhibits MERS-CoV infection and induces strong neutralizing antibody responses: implication for developing therapeutics and vaccines.

Identifieur interne : 001C10 ( PubMed/Checkpoint ); précédent : 001C09; suivant : 001C11

A truncated receptor-binding domain of MERS-CoV spike protein potently inhibits MERS-CoV infection and induces strong neutralizing antibody responses: implication for developing therapeutics and vaccines.

Auteurs : Lanying Du [États-Unis] ; Zhihua Kou ; Cuiqing Ma ; Xinrong Tao ; Lili Wang ; Guangyu Zhao ; Yaoqing Chen ; Fei Yu ; Chien-Te K. Tseng ; Yusen Zhou ; Shibo Jiang

Source :

PloS one [ 1932-6203 ] ; 2013.

RBID : pubmed:24324708

Descripteurs français

KwdFr :
- Animaux, Anticorps neutralisants (immunologie), Coronavirus (physiologie), Cristallographie aux rayons X, Femelle, Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Immunoglobuline G (métabolisme), Infections de l'appareil respiratoire (immunologie), Infections de l'appareil respiratoire (traitement médicamenteux), Infections de l'appareil respiratoire (virologie), Production d'anticorps (immunologie), Protéines recombinantes (immunologie), Récepteur Fc (métabolisme), Souris, Souris de lignée BALB C, Spécificité des anticorps (immunologie), Structure tertiaire des protéines, Sérums immuns (immunologie), Vaccination, Vaccins (immunologie), Vaccins antiviraux (immunologie), Vaccins antiviraux (usage thérapeutique).
MESH :
- immunologie : Anticorps neutralisants, Infections de l'appareil respiratoire, Production d'anticorps, Protéines recombinantes, Spécificité des anticorps, Sérums immuns, Vaccins, Vaccins antiviraux.
- métabolisme : Glycoprotéine de spicule des coronavirus, Immunoglobuline G, Récepteur Fc.
- physiologie : Coronavirus.
- traitement médicamenteux : Infections de l'appareil respiratoire.
- usage thérapeutique : Vaccins antiviraux.
- virologie : Infections de l'appareil respiratoire.
- Animaux, Cristallographie aux rayons X, Femelle, Humains, Souris, Souris de lignée BALB C, Structure tertiaire des protéines, Vaccination.

English descriptors

KwdEn :
- Animals, Antibodies, Neutralizing (immunology), Antibody Formation (immunology), Antibody Specificity (immunology), Coronavirus (physiology), Crystallography, X-Ray, Female, Humans, Immune Sera (immunology), Immunoglobulin G (metabolism), Mice, Mice, Inbred BALB C, Protein Structure, Tertiary, Receptors, Fc (metabolism), Recombinant Proteins (immunology), Respiratory Tract Infections (drug therapy), Respiratory Tract Infections (immunology), Respiratory Tract Infections (virology), Spike Glycoprotein, Coronavirus (metabolism), Vaccination, Vaccines (immunology), Viral Vaccines (immunology), Viral Vaccines (therapeutic use).
MESH :
- chemical , immunology : Antibodies, Neutralizing, Immune Sera, Recombinant Proteins, Vaccines, Viral Vaccines.
- drug therapy : Respiratory Tract Infections.
- immunology : Antibody Formation, Antibody Specificity, Respiratory Tract Infections.
- chemical , metabolism : Immunoglobulin G, Receptors, Fc, Spike Glycoprotein, Coronavirus.
- physiology : Coronavirus.
- chemical , therapeutic use : Viral Vaccines.
- virology : Respiratory Tract Infections.
- Animals, Crystallography, X-Ray, Female, Humans, Mice, Mice, Inbred BALB C, Protein Structure, Tertiary, Vaccination.

Abstract

An emerging respiratory infectious disease with high mortality, Middle East respiratory syndrome (MERS), is caused by a novel coronavirus (MERS-CoV). It was first reported in 2012 in Saudi Arabia and has now spread to eight countries. Development of effective therapeutics and vaccines is crucial to save lives and halt the spread of MERS-CoV. Here, we show that a recombinant protein containing a 212-amino acid fragment (residues 377-588) in the truncated receptor-binding domain (RBD: residues 367-606) of MERS-CoV spike (S) protein fused with human IgG Fc fragment (S377-588-Fc) is highly expressed in the culture supernatant of transfected 293T cells. The purified S377-588-Fc protein efficiently binds to dipeptidyl peptidase 4 (DPP4), the receptor of MERS-CoV, and potently inhibited MERS-CoV infection, suggesting its potential to be further developed as a therapeutic modality for treating MERS-CoV infection and saving the patients' lives. The recombinant S377-588-Fc is able to induce in the vaccinated mice strong MERS-CoV S-specific antibodies, which blocks the binding of RBD to DPP4 receptor and effectively neutralizes MERS-CoV infection. These findings indicate that this truncated RBD protein shows promise for further development as an effective and safe vaccine for the prevention of MERS-CoV infection.

DOI: 10.1371/journal.pone.0081587
PubMed: 24324708

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">An emerging respiratory infectious disease with high mortality, Middle East respiratory syndrome (MERS), is caused by a novel coronavirus (MERS-CoV). It was first reported in 2012 in Saudi Arabia and has now spread to eight countries. Development of effective therapeutics and vaccines is crucial to save lives and halt the spread of MERS-CoV. Here, we show that a recombinant protein containing a 212-amino acid fragment (residues 377-588) in the truncated receptor-binding domain (RBD: residues 367-606) of MERS-CoV spike (S) protein fused with human IgG Fc fragment (S377-588-Fc) is highly expressed in the culture supernatant of transfected 293T cells. The purified S377-588-Fc protein efficiently binds to dipeptidyl peptidase 4 (DPP4), the receptor of MERS-CoV, and potently inhibited MERS-CoV infection, suggesting its potential to be further developed as a therapeutic modality for treating MERS-CoV infection and saving the patients' lives. The recombinant S377-588-Fc is able to induce in the vaccinated mice strong MERS-CoV S-specific antibodies, which blocks the binding of RBD to DPP4 receptor and effectively neutralizes MERS-CoV infection. These findings indicate that this truncated RBD protein shows promise for further development as an effective and safe vaccine for the prevention of MERS-CoV infection. </div>
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<Abstract><AbstractText>An emerging respiratory infectious disease with high mortality, Middle East respiratory syndrome (MERS), is caused by a novel coronavirus (MERS-CoV). It was first reported in 2012 in Saudi Arabia and has now spread to eight countries. Development of effective therapeutics and vaccines is crucial to save lives and halt the spread of MERS-CoV. Here, we show that a recombinant protein containing a 212-amino acid fragment (residues 377-588) in the truncated receptor-binding domain (RBD: residues 367-606) of MERS-CoV spike (S) protein fused with human IgG Fc fragment (S377-588-Fc) is highly expressed in the culture supernatant of transfected 293T cells. The purified S377-588-Fc protein efficiently binds to dipeptidyl peptidase 4 (DPP4), the receptor of MERS-CoV, and potently inhibited MERS-CoV infection, suggesting its potential to be further developed as a therapeutic modality for treating MERS-CoV infection and saving the patients' lives. The recombinant S377-588-Fc is able to induce in the vaccinated mice strong MERS-CoV S-specific antibodies, which blocks the binding of RBD to DPP4 receptor and effectively neutralizes MERS-CoV infection. These findings indicate that this truncated RBD protein shows promise for further development as an effective and safe vaccine for the prevention of MERS-CoV infection. </AbstractText>
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A truncated receptor-binding domain of MERS-CoV spike protein potently inhibits MERS-CoV infection and induces strong neutralizing antibody responses: implication for developing therapeutics and vaccines.

A truncated receptor-binding domain of MERS-CoV spike protein potently inhibits MERS-CoV infection and induces strong neutralizing antibody responses: implication for developing therapeutics and vaccines.

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