Serveur d'exploration MERS

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Glycosylation of mouse DPP4 plays a role in inhibiting Middle East respiratory syndrome coronavirus infection.

Identifieur interne : 001778 ( Main/Exploration ); précédent : 001777; suivant : 001779

Glycosylation of mouse DPP4 plays a role in inhibiting Middle East respiratory syndrome coronavirus infection.

Auteurs : Kayla M. Peck [États-Unis] ; Adam S. Cockrell [États-Unis] ; Boyd L. Yount [États-Unis] ; Trevor Scobey [États-Unis] ; Ralph S. Baric [États-Unis] ; Mark T. Heise [États-Unis]

Source :

RBID : pubmed:25653445

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English descriptors

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes dipeptidyl peptidase 4 (DPP4) as an entry receptor. Mouse DPP4 (mDPP4) does not support MERS-CoV entry; however, changes at positions 288 and 330 can confer permissivity. Position 330 changes the charge and glycosylation state of mDPP4. We show that glycosylation is a major factor impacting DPP4 receptor function. These results provide insight into DPP4 species-specific differences impacting MERS-CoV host range and may inform MERS-CoV mouse model development.

DOI: 10.1128/JVI.03445-14
PubMed: 25653445


Affiliations:


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<term>Dipeptidyl Peptidase 4 (chemistry)</term>
<term>Dipeptidyl Peptidase 4 (genetics)</term>
<term>Dipeptidyl Peptidase 4 (metabolism)</term>
<term>Fluorescent Antibody Technique</term>
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<term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term>
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<div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes dipeptidyl peptidase 4 (DPP4) as an entry receptor. Mouse DPP4 (mDPP4) does not support MERS-CoV entry; however, changes at positions 288 and 330 can confer permissivity. Position 330 changes the charge and glycosylation state of mDPP4. We show that glycosylation is a major factor impacting DPP4 receptor function. These results provide insight into DPP4 species-specific differences impacting MERS-CoV host range and may inform MERS-CoV mouse model development. </div>
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