Journal of Virology 2014-02-01

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

Index: J. Virol. 88(3) , 1834-8, (2014)

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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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