Association of host tropism of Middle East syndrome coronavirus with the amino acid structure of host cell receptor dipeptidyl peptidase 4.
Identifieur interne : 001991 ( PubMed/Checkpoint ); précédent : 001990; suivant : 001992Association of host tropism of Middle East syndrome coronavirus with the amino acid structure of host cell receptor dipeptidyl peptidase 4.
Auteurs : M. Kandeel ; M A Elaiziz ; A. Kandeel ; A A Altaher ; Y. KitadeSource :
- Acta virologica [ 0001-723X ] ; 2014.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Coronavirus du syndrome respiratoire du Moyen-Orient (), Coronavirus du syndrome respiratoire du Moyen-Orient (génétique), Coronavirus du syndrome respiratoire du Moyen-Orient (physiologie), Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (métabolisme), Données de séquences moléculaires, Humains, Infections à coronavirus (enzymologie), Infections à coronavirus (génétique), Infections à coronavirus (médecine vétérinaire), Infections à coronavirus (virologie), Mammifères (génétique), Mammifères (virologie), Récepteurs viraux (), Récepteurs viraux (génétique), Récepteurs viraux (métabolisme), Séquence d'acides aminés, Tropisme viral.
- MESH :
- enzymologie : Infections à coronavirus.
- génétique : Coronavirus du syndrome respiratoire du Moyen-Orient, Dipeptidyl peptidase 4, Infections à coronavirus, Mammifères, Récepteurs viraux.
- médecine vétérinaire : Infections à coronavirus.
- métabolisme : Dipeptidyl peptidase 4, Récepteurs viraux.
- physiologie : Coronavirus du syndrome respiratoire du Moyen-Orient.
- virologie : Infections à coronavirus, Mammifères.
- Alignement de séquences, Animaux, Coronavirus du syndrome respiratoire du Moyen-Orient, Dipeptidyl peptidase 4, Données de séquences moléculaires, Humains, Récepteurs viraux, Séquence d'acides aminés, Tropisme viral.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Coronavirus Infections (enzymology), Coronavirus Infections (genetics), Coronavirus Infections (veterinary), Coronavirus Infections (virology), Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Humans, Mammals (genetics), Mammals (virology), Middle East Respiratory Syndrome Coronavirus (classification), Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (physiology), Molecular Sequence Data, Receptors, Virus (chemistry), Receptors, Virus (genetics), Receptors, Virus (metabolism), Sequence Alignment, Viral Tropism.
- MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4, Receptors, Virus.
- classification : Middle East Respiratory Syndrome Coronavirus.
- enzymology : Coronavirus Infections.
- genetics : Coronavirus Infections, Dipeptidyl Peptidase 4, Mammals, Middle East Respiratory Syndrome Coronavirus, Receptors, Virus.
- chemical , metabolism : Dipeptidyl Peptidase 4, Receptors, Virus.
- physiology : Middle East Respiratory Syndrome Coronavirus.
- veterinary : Coronavirus Infections.
- virology : Coronavirus Infections, Mammals.
- Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Sequence Alignment, Viral Tropism.
Abstract
The Middle East syndrome coronavirus (MERS-CoV) is a recently emerging betacoronavirus with high fatality. Recently, dipeptidyle peptidase (CD26, DPP4) was identified as the host cell receptor for MERS-CoV. Interestingly, despite of common presence of DPP4 receptors the binding and infection of various cells shows imminent variability. In this report, we provide a tool for prediction of the host tropism of the virus based on the host receptor binding interface. We found out that, in the binding of MERS-CoV to cells the amino acid residues in lancets 4 and 5 of DPP4 receptor, namely K267, Q286, T288, R317, R336, Q344 A291, L294, and I295 are involved. Changes in these residues correspond to profound decrease in virus binding to cells. The nine residues at the interface between the virus spikes and the lancets 4 and 5 of host DPP4 can be used as a predictive tool for the host tropism and virus affinity to host cell receptors.
DOI: 10.4149/av_2014_04_359
PubMed: 25518718
Affiliations:
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pubmed:25518718Le document en format XML
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<front><div type="abstract" xml:lang="en">The Middle East syndrome coronavirus (MERS-CoV) is a recently emerging betacoronavirus with high fatality. Recently, dipeptidyle peptidase (CD26, DPP4) was identified as the host cell receptor for MERS-CoV. Interestingly, despite of common presence of DPP4 receptors the binding and infection of various cells shows imminent variability. In this report, we provide a tool for prediction of the host tropism of the virus based on the host receptor binding interface. We found out that, in the binding of MERS-CoV to cells the amino acid residues in lancets 4 and 5 of DPP4 receptor, namely K267, Q286, T288, R317, R336, Q344 A291, L294, and I295 are involved. Changes in these residues correspond to profound decrease in virus binding to cells. The nine residues at the interface between the virus spikes and the lancets 4 and 5 of host DPP4 can be used as a predictive tool for the host tropism and virus affinity to host cell receptors.</div>
</front>
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<Abstract><AbstractText>The Middle East syndrome coronavirus (MERS-CoV) is a recently emerging betacoronavirus with high fatality. Recently, dipeptidyle peptidase (CD26, DPP4) was identified as the host cell receptor for MERS-CoV. Interestingly, despite of common presence of DPP4 receptors the binding and infection of various cells shows imminent variability. In this report, we provide a tool for prediction of the host tropism of the virus based on the host receptor binding interface. We found out that, in the binding of MERS-CoV to cells the amino acid residues in lancets 4 and 5 of DPP4 receptor, namely K267, Q286, T288, R317, R336, Q344 A291, L294, and I295 are involved. Changes in these residues correspond to profound decrease in virus binding to cells. The nine residues at the interface between the virus spikes and the lancets 4 and 5 of host DPP4 can be used as a predictive tool for the host tropism and virus affinity to host cell receptors.</AbstractText>
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