OmniVira

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

Kayla M Peck1 Adam S Cockrell2 Boyd L Yount3 Trevor Scobey3 Ralph S Baric4 Mark T Heise5
Affiliations 5 institutions
  1. Department of Biology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA.
  2. Genetics, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA.
  3. Epidemiology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA.
  4. Epidemiology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA Microbiology and Immunology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA [email protected] [email protected].
  5. Genetics, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA Microbiology and Immunology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA [email protected] [email protected].
PMID25653445 DOI10.1128/JVI.03445-14 Year2015 Journal Journal of virology J Virol Languageeng Statusppublish

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.

Models, Molecular 99 Virus Internalization 100 Amino Acid Sequence 128 Animals 1948 Coronavirus Infections 171 Dipeptidyl Peptidase 4 32 Fluorescent Antibody Technique 2 Glycosylation 22 Mice 253 Middle East Respiratory Syndrome Coronavirus 68 Molecular Sequence Data 160 Species Specificity 84 Dpp4 protein, mouse 1

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