Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.

V Stalin Raj; Saskia L Smits; Lisette B Provacia; Judith M A van den Brand; Lidewij Wiersma; Werner J D Ouwendijk; Theo M Bestebroer; Monique I Spronken; Geert van Amerongen; Peter J M Rottier; Ron A M Fouchier; Berend Jan Bosch; Albert D M E Osterhaus; Bart L Haagmans

doi:10.1128/JVI.02935-13

Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.

V Stalin Raj
, Saskia L Smits
, Lisette B Provacia
, Judith M A van den Brand
, Lidewij Wiersma
, Werner J D Ouwendijk
, Theo M Bestebroer
, Monique I Spronken
, Geert van Amerongen
, Peter J M Rottier
, Ron A M Fouchier
, Berend Jan Bosch
, Albert D M E Osterhaus
, Bart L Haagmans

VPDC Pathology

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) replicates in cells of different species using dipeptidyl peptidase 4 (DPP4) as a functional receptor. Here we show the resistance of ferrets to MERS-CoV infection and inability of ferret DDP4 to bind MERS-CoV. Site-directed mutagenesis of amino acids variable in ferret DPP4 thus revealed the functional human DPP4 virus binding site. Adenosine deaminase (ADA), a DPP4 binding protein, competed for virus binding, acting as a natural antagonist for MERS-CoV infection.

Original language	English
Pages (from-to)	1834-8
Number of pages	5
Journal	Journal of Virology
Volume	88
Issue number	3
DOIs	https://doi.org/10.1128/JVI.02935-13
Publication status	Published - 2014

Keywords

Molecular Sequence Data
Protein Binding
Receptors, Virus
Adenosine Deaminase: metabolism
Amino Acid Sequence
Animals
Coronaviridae
Coronaviridae Infections
Coronaviridae Infections: enzymology
Coronaviridae Infections: virology
Coronaviridae: genetics
Coronaviridae: physiology
Dipeptidyl Peptidase 4
Dipeptidyl Peptidase 4: chemistry
Adenosine Deaminase
Virus Internalization
Spike Glycoprotein, Coronavirus: metabolism
Spike Glycoprotein, Coronavirus: genetics
Spike Glycoprotein, Coronavirus
Sequence Alignment
Receptors, Virus: metabolism
Adenosine Deaminase: genetics
Receptors, Virus: genetics
Receptors, Virus: chemistry
Dipeptidyl Peptidase 4: genetics
Dipeptidyl Peptidase 4: metabolism
Disease Models, Animal
Ferrets
Humans

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Raj, V. S., Smits, S. L., Provacia, L. B., van den Brand, J. M. A., Wiersma, L., Ouwendijk, W. J. D., Bestebroer, T. M., Spronken, M. I., van Amerongen, G., Rottier, P. J. M., Fouchier, R. A. M., Bosch, B. J., Osterhaus, A. D. M. E., & Haagmans, B. L. (2014). Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus. Journal of Virology, 88(3), 1834-8. https://doi.org/10.1128/JVI.02935-13

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title = "Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.",

abstract = "Middle East respiratory syndrome coronavirus (MERS-CoV) replicates in cells of different species using dipeptidyl peptidase 4 (DPP4) as a functional receptor. Here we show the resistance of ferrets to MERS-CoV infection and inability of ferret DDP4 to bind MERS-CoV. Site-directed mutagenesis of amino acids variable in ferret DPP4 thus revealed the functional human DPP4 virus binding site. Adenosine deaminase (ADA), a DPP4 binding protein, competed for virus binding, acting as a natural antagonist for MERS-CoV infection.",

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author = "Raj, \{V Stalin\} and Smits, \{Saskia L\} and Provacia, \{Lisette B\} and \{van den Brand\}, \{Judith M A\} and Lidewij Wiersma and Ouwendijk, \{Werner J D\} and Bestebroer, \{Theo M\} and Spronken, \{Monique I\} and \{van Amerongen\}, Geert and Rottier, \{Peter J M\} and Fouchier, \{Ron A M\} and Bosch, \{Berend Jan\} and Osterhaus, \{Albert D M E\} and Haagmans, \{Bart L\}",

year = "2014",

doi = "10.1128/JVI.02935-13",

language = "English",

volume = "88",

pages = "1834--8",

journal = "Journal of Virology",

issn = "0022-538X",

publisher = "American Society for Microbiology",

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Raj, VS, Smits, SL, Provacia, LB, van den Brand, JMA, Wiersma, L, Ouwendijk, WJD, Bestebroer, TM, Spronken, MI, van Amerongen, G, Rottier, PJM, Fouchier, RAM, Bosch, BJ, Osterhaus, ADME & Haagmans, BL 2014, 'Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.', Journal of Virology, vol. 88, no. 3, pp. 1834-8. https://doi.org/10.1128/JVI.02935-13

TY - JOUR

T1 - Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.

AU - Raj, V Stalin

AU - Smits, Saskia L

AU - Provacia, Lisette B

AU - van den Brand, Judith M A

AU - Wiersma, Lidewij

AU - Ouwendijk, Werner J D

AU - Bestebroer, Theo M

AU - Spronken, Monique I

AU - van Amerongen, Geert

AU - Rottier, Peter J M

AU - Fouchier, Ron A M

AU - Bosch, Berend Jan

AU - Osterhaus, Albert D M E

AU - Haagmans, Bart L

PY - 2014

Y1 - 2014

N2 - Middle East respiratory syndrome coronavirus (MERS-CoV) replicates in cells of different species using dipeptidyl peptidase 4 (DPP4) as a functional receptor. Here we show the resistance of ferrets to MERS-CoV infection and inability of ferret DDP4 to bind MERS-CoV. Site-directed mutagenesis of amino acids variable in ferret DPP4 thus revealed the functional human DPP4 virus binding site. Adenosine deaminase (ADA), a DPP4 binding protein, competed for virus binding, acting as a natural antagonist for MERS-CoV infection.

AB - Middle East respiratory syndrome coronavirus (MERS-CoV) replicates in cells of different species using dipeptidyl peptidase 4 (DPP4) as a functional receptor. Here we show the resistance of ferrets to MERS-CoV infection and inability of ferret DDP4 to bind MERS-CoV. Site-directed mutagenesis of amino acids variable in ferret DPP4 thus revealed the functional human DPP4 virus binding site. Adenosine deaminase (ADA), a DPP4 binding protein, competed for virus binding, acting as a natural antagonist for MERS-CoV infection.

KW - Molecular Sequence Data

KW - Protein Binding

KW - Receptors, Virus

KW - Adenosine Deaminase: metabolism

KW - Amino Acid Sequence

KW - Animals

KW - Coronaviridae

KW - Coronaviridae Infections

KW - Coronaviridae Infections: enzymology

KW - Coronaviridae Infections: virology

KW - Coronaviridae: genetics

KW - Coronaviridae: physiology

KW - Dipeptidyl Peptidase 4

KW - Dipeptidyl Peptidase 4: chemistry

KW - Adenosine Deaminase

KW - Virus Internalization

KW - Spike Glycoprotein, Coronavirus: metabolism

KW - Spike Glycoprotein, Coronavirus: genetics

KW - Spike Glycoprotein, Coronavirus

KW - Sequence Alignment

KW - Receptors, Virus: metabolism

KW - Adenosine Deaminase: genetics

KW - Receptors, Virus: genetics

KW - Receptors, Virus: chemistry

KW - Dipeptidyl Peptidase 4: genetics

KW - Dipeptidyl Peptidase 4: metabolism

KW - Disease Models, Animal

KW - Ferrets

KW - Humans

U2 - 10.1128/JVI.02935-13

DO - 10.1128/JVI.02935-13

M3 - Article

C2 - 24257613

SN - 0022-538X

VL - 88

SP - 1834

EP - 1838

JO - Journal of Virology

JF - Journal of Virology

IS - 3

ER -

Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus.

Abstract

Keywords

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