MersV1, PubMed, Curation, bibRecord, 001B76

Inhibition of Middle East respiratory syndrome coronavirus infection by anti-CD26 monoclonal antibody.

Identifieur interne : 001B76 ( PubMed/Curation ); précédent : 001B75; suivant : 001B77

Inhibition of Middle East respiratory syndrome coronavirus infection by anti-CD26 monoclonal antibody.

Auteurs : Kei Ohnuma [Japon] ; Bart L. Haagmans ; Ryo Hatano ; V Stalin Raj ; Huihui Mou ; Satoshi Iwata ; Nam H. Dang ; Berend Jan Bosch ; Chikao Morimoto

Source :

Journal of virology [ 1098-5514 ] ; 2013.

RBID : pubmed:24067970

Descripteurs français

KwdFr :
- Anticorps antiviraux (immunologie), Anticorps antiviraux (pharmacologie), Anticorps monoclonaux (immunologie), Anticorps monoclonaux (pharmacologie), Cartographie épitopique, Coronaviridae (), Coronaviridae (génétique), Coronaviridae (physiologie), Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (immunologie), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Infections à Coronaviridae (enzymologie), Infections à Coronaviridae (immunologie), Infections à Coronaviridae (traitement médicamenteux), Infections à Coronaviridae (virologie), Liaison aux protéines, Pénétration virale (), Structure tertiaire des protéines.
MESH :
- enzymologie : Infections à Coronaviridae.
- génétique : Coronaviridae, Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus.
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Dipeptidyl peptidase 4, Infections à Coronaviridae.
- métabolisme : Glycoprotéine de spicule des coronavirus.
- pharmacologie : Anticorps antiviraux, Anticorps monoclonaux.
- physiologie : Coronaviridae.
- traitement médicamenteux : Infections à Coronaviridae.
- virologie : Infections à Coronaviridae.
- Cartographie épitopique, Coronaviridae, Dipeptidyl peptidase 4, Humains, Liaison aux protéines, Pénétration virale, Structure tertiaire des protéines.

English descriptors

KwdEn :
- Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (pharmacology), Antibodies, Viral (immunology), Antibodies, Viral (pharmacology), Coronaviridae (drug effects), Coronaviridae (genetics), Coronaviridae (physiology), Coronaviridae Infections (drug therapy), Coronaviridae Infections (enzymology), Coronaviridae Infections (immunology), Coronaviridae Infections (virology), Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (immunology), Epitope Mapping, Humans, Protein Binding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Virus Internalization (drug effects).
MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4.
- chemical , genetics : Dipeptidyl Peptidase 4, Spike Glycoprotein, Coronavirus.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Dipeptidyl Peptidase 4.
- chemical , metabolism : Spike Glycoprotein, Coronavirus.
- chemical , pharmacology : Antibodies, Monoclonal, Antibodies, Viral.
- drug effects : Coronaviridae, Virus Internalization.
- drug therapy : Coronaviridae Infections.
- enzymology : Coronaviridae Infections.
- genetics : Coronaviridae.
- immunology : Coronaviridae Infections.
- physiology : Coronaviridae.
- virology : Coronaviridae Infections.
- Epitope Mapping, Humans, Protein Binding, Protein Structure, Tertiary.

Abstract

We identified the domains of CD26 involved in the binding of Middle East respiratory syndrome coronavirus (MERS-CoV) using distinct clones of anti-CD26 monoclonal antibodies (MAbs). One clone, named 2F9, almost completely inhibited viral entry. The humanized anti-CD26 MAb YS110 also significantly inhibited infection. These findings indicate that both 2F9 and YS110 are potential therapeutic agents for MERS-CoV infection. YS110, in particular, is a good candidate for immediate testing as a therapeutic modality for MERS.

DOI: 10.1128/JVI.02448-13
PubMed: 24067970

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Le document en format XML

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<front><div type="abstract" xml:lang="en">We identified the domains of CD26 involved in the binding of Middle East respiratory syndrome coronavirus (MERS-CoV) using distinct clones of anti-CD26 monoclonal antibodies (MAbs). One clone, named 2F9, almost completely inhibited viral entry. The humanized anti-CD26 MAb YS110 also significantly inhibited infection. These findings indicate that both 2F9 and YS110 are potential therapeutic agents for MERS-CoV infection. YS110, in particular, is a good candidate for immediate testing as a therapeutic modality for MERS. </div>
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<Abstract><AbstractText>We identified the domains of CD26 involved in the binding of Middle East respiratory syndrome coronavirus (MERS-CoV) using distinct clones of anti-CD26 monoclonal antibodies (MAbs). One clone, named 2F9, almost completely inhibited viral entry. The humanized anti-CD26 MAb YS110 also significantly inhibited infection. These findings indicate that both 2F9 and YS110 are potential therapeutic agents for MERS-CoV infection. YS110, in particular, is a good candidate for immediate testing as a therapeutic modality for MERS. </AbstractText>
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Inhibition of Middle East respiratory syndrome coronavirus infection by anti-CD26 monoclonal antibody.

Inhibition of Middle East respiratory syndrome coronavirus infection by anti-CD26 monoclonal antibody.

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