Permissivity of Dipeptidyl Peptidase 4 Orthologs to Middle East Respiratory Syndrome Coronavirus Is Governed by Glycosylation and Other Complex Determinants.
Identifieur interne : 000C36 ( Main/Exploration ); précédent : 000C35; suivant : 000C37Permissivity of Dipeptidyl Peptidase 4 Orthologs to Middle East Respiratory Syndrome Coronavirus Is Governed by Glycosylation and Other Complex Determinants.
Auteurs : Kayla M. Peck [États-Unis] ; Trevor Scobey [États-Unis] ; Jesica Swanstrom [États-Unis] ; Kara L. Jensen [États-Unis] ; Christina L. Burch [États-Unis] ; Ralph S. Baric [États-Unis] ; Mark T. Heise [États-Unis]Source :
- Journal of virology [ 1098-5514 ] ; 2017.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Attachement viral, Cellules HEK293, Cellules Vero, Cochons d'Inde, Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme), Cricetinae, Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (métabolisme), Furets, Glycosylation, Humains, Infections à coronavirus (anatomopathologie), Infections à coronavirus (génétique), Infections à coronavirus (virologie), Lignée cellulaire, Récepteurs viraux (génétique), Récepteurs viraux (métabolisme), Similitude de séquences d'acides aminés, Spécificité d'hôte (physiologie), Séquence d'acides aminés (génétique).
- MESH :
- anatomopathologie : Infections à coronavirus.
- génétique : Dipeptidyl peptidase 4, Infections à coronavirus, Récepteurs viraux, Séquence d'acides aminés.
- métabolisme : Coronavirus du syndrome respiratoire du Moyen-Orient, Dipeptidyl peptidase 4, Récepteurs viraux.
- physiologie : Spécificité d'hôte.
- virologie : Infections à coronavirus.
- Alignement de séquences, Animaux, Attachement viral, Cellules HEK293, Cellules Vero, Cochons d'Inde, Cricetinae, Furets, Glycosylation, Humains, Lignée cellulaire, Similitude de séquences d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (genetics), Animals, Cell Line, Chlorocebus aethiops, Coronavirus Infections (genetics), Coronavirus Infections (pathology), Coronavirus Infections (virology), Cricetinae, Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Ferrets, Glycosylation, Guinea Pigs, HEK293 Cells, Host Specificity (physiology), Humans, Middle East Respiratory Syndrome Coronavirus (metabolism), Receptors, Virus (genetics), Receptors, Virus (metabolism), Sequence Alignment, Sequence Homology, Amino Acid, Vero Cells, Virus Attachment.
- MESH :
- chemical , genetics : Dipeptidyl Peptidase 4, Receptors, Virus.
- genetics : Amino Acid Sequence, Coronavirus Infections.
- chemical , metabolism : Dipeptidyl Peptidase 4, Middle East Respiratory Syndrome Coronavirus, Receptors, Virus.
- pathology : Coronavirus Infections.
- physiology : Host Specificity.
- virology : Coronavirus Infections.
- Animals, Cell Line, Chlorocebus aethiops, Cricetinae, Ferrets, Glycosylation, Guinea Pigs, HEK293 Cells, Humans, Sequence Alignment, Sequence Homology, Amino Acid, Vero Cells, Virus Attachment.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes dipeptidyl peptidase 4 (DPP4) as an entry receptor. While bat, camel, and human DPP4 support MERS-CoV infection, several DPP4 orthologs, including mouse, ferret, hamster, and guinea pig DPP4, do not. Previous work revealed that glycosylation of mouse DPP4 plays a role in blocking MERS-CoV infection. Here, we tested whether glycosylation also acts as a determinant of permissivity for ferret, hamster, and guinea pig DPP4. We found that, while glycosylation plays an important role in these orthologs, additional sequence and structural determinants impact their ability to act as functional receptors for MERS-CoV. These results provide insight into DPP4 species-specific differences impacting MERS-CoV host range and better inform our understanding of virus-receptor interactions associated with disease emergence and host susceptibility.IMPORTANCE MERS-CoV is a recently emerged zoonotic virus that is still circulating in the human population with an ∼35% mortality rate. With no available vaccines or therapeutics, the study of MERS-CoV pathogenesis is crucial for its control and prevention. However, in vivo studies are limited because MERS-CoV cannot infect wild-type mice due to incompatibilities between the virus spike and the mouse host cell receptor, mouse DPP4 (mDPP4). Specifically, mDPP4 has a nonconserved glycosylation site that acts as a barrier to MERS-CoV infection. Thus, one mouse model strategy has been to modify the mouse genome to remove this glycosylation site. Here, we investigated whether glycosylation acts as a barrier to infection for other nonpermissive small-animal species, namely, ferret, guinea pig, and hamster. Understanding the virus-receptor interactions for these DPP4 orthologs will help in the development of additional animal models while also revealing species-specific differences impacting MERS-CoV host range.
DOI: 10.1128/JVI.00534-17
PubMed: 28747502
Affiliations:
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Peck</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Scobey, Trevor" sort="Scobey, Trevor" uniqKey="Scobey T" first="Trevor" last="Scobey">Trevor Scobey</name><affiliation wicri:level="2"><nlm:affiliation>Department of Epidemiology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Epidemiology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Swanstrom, Jesica" sort="Swanstrom, Jesica" uniqKey="Swanstrom J" first="Jesica" last="Swanstrom">Jesica Swanstrom</name><affiliation wicri:level="2"><nlm:affiliation>Department of Epidemiology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Epidemiology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Jensen, Kara L" sort="Jensen, Kara L" uniqKey="Jensen K" first="Kara L" last="Jensen">Kara L. 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Heise</name><affiliation wicri:level="2"><nlm:affiliation>Department of Genetics, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA rbaric@email.unc.edu mark_heisem@med.unc.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Genetics, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (genetics)</term><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Coronavirus Infections (genetics)</term><term>Coronavirus Infections (pathology)</term><term>Coronavirus Infections (virology)</term><term>Cricetinae</term><term>Dipeptidyl Peptidase 4 (genetics)</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Ferrets</term><term>Glycosylation</term><term>Guinea Pigs</term><term>HEK293 Cells</term><term>Host Specificity (physiology)</term><term>Humans</term><term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term><term>Receptors, Virus (genetics)</term><term>Receptors, Virus (metabolism)</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term><term>Virus Attachment</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Attachement viral</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Cochons d'Inde</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme)</term><term>Cricetinae</term><term>Dipeptidyl peptidase 4 (génétique)</term><term>Dipeptidyl peptidase 4 (métabolisme)</term><term>Furets</term><term>Glycosylation</term><term>Humains</term><term>Infections à coronavirus (anatomopathologie)</term><term>Infections à coronavirus (génétique)</term><term>Infections à coronavirus (virologie)</term><term>Lignée cellulaire</term><term>Récepteurs viraux (génétique)</term><term>Récepteurs viraux (métabolisme)</term><term>Similitude de séquences d'acides aminés</term><term>Spécificité d'hôte (physiologie)</term><term>Séquence d'acides aminés (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Infections à coronavirus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Sequence</term><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Dipeptidyl peptidase 4</term><term>Infections à coronavirus</term><term>Récepteurs viraux</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Middle East Respiratory Syndrome Coronavirus</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term><term>Dipeptidyl peptidase 4</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Spécificité d'hôte</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Host Specificity</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Cricetinae</term><term>Ferrets</term><term>Glycosylation</term><term>Guinea Pigs</term><term>HEK293 Cells</term><term>Humans</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term><term>Virus Attachment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Attachement viral</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Cochons d'Inde</term><term>Cricetinae</term><term>Furets</term><term>Glycosylation</term><term>Humains</term><term>Lignée cellulaire</term><term>Similitude de séquences d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes dipeptidyl peptidase 4 (DPP4) as an entry receptor. While bat, camel, and human DPP4 support MERS-CoV infection, several DPP4 orthologs, including mouse, ferret, hamster, and guinea pig DPP4, do not. Previous work revealed that glycosylation of mouse DPP4 plays a role in blocking MERS-CoV infection. Here, we tested whether glycosylation also acts as a determinant of permissivity for ferret, hamster, and guinea pig DPP4. We found that, while glycosylation plays an important role in these orthologs, additional sequence and structural determinants impact their ability to act as functional receptors for MERS-CoV. These results provide insight into DPP4 species-specific differences impacting MERS-CoV host range and better inform our understanding of virus-receptor interactions associated with disease emergence and host susceptibility.<b>IMPORTANCE</b> MERS-CoV is a recently emerged zoonotic virus that is still circulating in the human population with an ∼35% mortality rate. With no available vaccines or therapeutics, the study of MERS-CoV pathogenesis is crucial for its control and prevention. However, <i>in vivo</i> studies are limited because MERS-CoV cannot infect wild-type mice due to incompatibilities between the virus spike and the mouse host cell receptor, mouse DPP4 (mDPP4). Specifically, mDPP4 has a nonconserved glycosylation site that acts as a barrier to MERS-CoV infection. Thus, one mouse model strategy has been to modify the mouse genome to remove this glycosylation site. Here, we investigated whether glycosylation acts as a barrier to infection for other nonpermissive small-animal species, namely, ferret, guinea pig, and hamster. Understanding the virus-receptor interactions for these DPP4 orthologs will help in the development of additional animal models while also revealing species-specific differences impacting MERS-CoV host range.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li></region></list><tree><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Peck, Kayla M" sort="Peck, Kayla M" uniqKey="Peck K" first="Kayla M" last="Peck">Kayla M. Peck</name></region><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name><name sortKey="Burch, Christina L" sort="Burch, Christina L" uniqKey="Burch C" first="Christina L" last="Burch">Christina L. Burch</name><name sortKey="Heise, Mark T" sort="Heise, Mark T" uniqKey="Heise M" first="Mark T" last="Heise">Mark T. Heise</name><name sortKey="Jensen, Kara L" sort="Jensen, Kara L" uniqKey="Jensen K" first="Kara L" last="Jensen">Kara L. Jensen</name><name sortKey="Scobey, Trevor" sort="Scobey, Trevor" uniqKey="Scobey T" first="Trevor" last="Scobey">Trevor Scobey</name><name sortKey="Swanstrom, Jesica" sort="Swanstrom, Jesica" uniqKey="Swanstrom J" first="Jesica" last="Swanstrom">Jesica Swanstrom</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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