Adenosine deaminase acts as a natural antagonist for dipeptidyl peptidase 4-mediated entry of the Middle East respiratory syndrome coronavirus
VS Raj, SL Smits, LB Provacia… - Journal of …, 2014 - Am Soc Microbiol
Journal of virology, 2014•Am Soc Microbiol
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.
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.
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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